A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.
A synthetic amino acid that depletes glutathione by irreversibly inhibiting gamma-glutamylcysteine synthetase. Inhibition of this enzyme is a critical step in glutathione biosynthesis. It has been shown to inhibit the proliferative response in human T-lymphocytes and inhibit macrophage activation. (J Biol Chem 1995;270(33):1945-7)
A glutathione transferase that catalyzes the conjugation of electrophilic substrates to GLUTATHIONE. This enzyme has been shown to provide cellular protection against redox-mediated damage by FREE RADICALS.
One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.
A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
Methionine Sulfoximine is a toxic compound that functions as an inhibitor of methionine metabolism, being formed through the oxidation of methionine by the enzyme methionine sulfoxide reductase.
Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Compounds containing the -SH radical.
An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of GLUTATHIONE PEROXIDASE.
An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.
**Maleates** are organic compounds that contain a carboxylic acid group and a hydroxyl group attached to adjacent carbon atoms, often used as intermediates in the synthesis of pharmaceuticals and other chemicals, or as drugs themselves, such as maleic acid or its salts.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.
The N-acetyl derivative of CYSTEINE. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates.
An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.
An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
The dialdehyde of malonic acid.
The rate dynamics in chemical or physical systems.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
A cyclized derivative of L-GLUTAMIC ACID. Elevated blood levels may be associated with problems of GLUTAMINE or GLUTATHIONE metabolism.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
Low-molecular-weight end products, probably malondialdehyde, that are formed during the decomposition of lipid peroxidation products. These compounds react with thiobarbituric acid to form a fluorescent red adduct.
Electron-accepting molecules in chemical reactions in which electrons are transferred from one molecule to another (OXIDATION-REDUCTION).
A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.
Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.
A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant.
A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed)
A compound that inhibits symport of sodium, potassium, and chloride primarily in the ascending limb of Henle, but also in the proximal and distal tubules. This pharmacological action results in excretion of these ions, increased urinary output, and reduction in extracellular fluid. This compound has been classified as a loop or high ceiling diuretic.
Peroxides produced in the presence of a free radical by the oxidation of unsaturated fatty acids in the cell in the presence of molecular oxygen. The formation of lipid peroxides results in the destruction of the original lipid leading to the loss of integrity of the membranes. They therefore cause a variety of toxic effects in vivo and their formation is considered a pathological process in biological systems. Their formation can be inhibited by antioxidants, such as vitamin E, structural separation or low oxygen tension.
A direct-acting oxidative stress-inducing agent used to examine the effects of oxidant stress on Ca(2+)-dependent signal transduction in vascular endothelial cells. It is also used as a catalyst in polymerization reactions and to introduce peroxy groups into organic molecules.
A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An enzyme that catalyzes the interconversion of methylglyoxal and lactate, with glutathione serving as a coenzyme. EC 4.4.1.5.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
Organic compounds containing a carbonyl group in the form -CHO.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.
Analgesic antipyretic derivative of acetanilide. It has weak anti-inflammatory properties and is used as a common analgesic, but may cause liver, blood cell, and kidney damage.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
The relationship between the dose of an administered drug and the response of the organism to the drug.
Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.
A selenium compound with the molecular formula H2SO3. It used as a source of SELENIUM, especially for patients that develop selenium deficiency following prolonged PARENTERAL NUTRITION.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Substances that influence the course of a chemical reaction by ready combination with free radicals. Among other effects, this combining activity protects pancreatic islets against damage by cytokines and prevents myocardial and pulmonary perfusion injuries.
Drugs that are chemically similar to naturally occurring metabolites, but differ enough to interfere with normal metabolic pathways. (From AMA Drug Evaluations Annual, 1994, p2033)
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Organic compounds which contain selenium as an integral part of the molecule.
Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Established cell cultures that have the potential to propagate indefinitely.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A basic-leucine zipper transcription factor that was originally described as a transcriptional regulator controlling expression of the BETA-GLOBIN gene. It may regulate the expression of a wide variety of genes that play a role in protecting cells from oxidative damage.
Organic compounds with the general formula R-NCS.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A generic descriptor for all TOCOPHEROLS and TOCOTRIENOLS that exhibit ALPHA-TOCOPHEROL activity. By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An effective soil fumigant, insecticide, and nematocide. In humans, it causes severe burning of skin and irritation of the eyes and respiratory tract. Prolonged inhalation may cause liver necrosis. It is also used in gasoline. Members of this group have caused liver and lung cancers in rodents. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), 1,2-dibromoethane may reasonably be anticipated to be a carcinogen.
The disodium salt of selenious acid. It is used therapeutically to supply the trace element selenium and is prepared by the reaction of SELENIUM DIOXIDE with SODIUM HYDROXIDE.
Mixture of 2- and 3-tert-butyl-4-methoxyphenols that is used as an antioxidant in foods, cosmetics, and pharmaceuticals.
A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
Proteins prepared by recombinant DNA technology.
A chlorinated hydrocarbon that has been used as an inhalation anesthetic and acts as a narcotic in high concentrations. Its primary use is as a solvent in manufacturing and food technology.
Nitroso compounds are organic or inorganic substances containing the nitroso functional group, which consists of a nitrogen atom bonded to an oxygen atom through a single covalent bond, often abbreviated as -NO.
Elements of limited time intervals, contributing to particular results or situations.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.
A potent hepatotoxic and hepatocarcinogenic mycotoxin produced by the Aspergillus flavus group of fungi. It is also mutagenic, teratogenic, and causes immunosuppression in animals. It is found as a contaminant in peanuts, cottonseed meal, corn, and other grains. The mycotoxin requires epoxidation to aflatoxin B1 2,3-oxide for activation. Microsomal monooxygenases biotransform the toxin to the less toxic metabolites aflatoxin M1 and Q1.
Peptides composed of two amino acid units.
An extracellular selenoprotein that contains most of the SELENIUM in PLASMA. Selenoprotein P functions as an antioxidant and appears to transport selenium from the LIVER to peripheral tissues.
The appearance of carbonyl groups (such as aldehyde or ketone groups) in PROTEINS as the result of several oxidative modification reactions. It is a standard marker for OXIDATIVE STRESS. Carbonylated proteins tend to be more hydrophobic and resistant to proteolysis.
A spectrum of clinical liver diseases ranging from mild biochemical abnormalities to ACUTE LIVER FAILURE, caused by drugs, drug metabolites, and chemicals from the environment.
Chemical substances that are foreign to the biological system. They include naturally occurring compounds, drugs, environmental agents, carcinogens, insecticides, etc.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Derivatives of benzene in which one or more hydrogen atoms on the benzene ring are replaced by bromine atoms.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
**Mercaptoethanol, also known as β-mercaptoethanol or BME, is an organosulfur compound with the formula HOCH2CH2SH, functionally serving as a reducing agent and a sulfhydryl group protector in biochemical and molecular biology applications.**
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
'Benzene derivatives' are organic compounds that contain a benzene ring as the core structure, with various functional groups attached to it, and can have diverse chemical properties and uses, including as solvents, intermediates in chemical synthesis, and pharmaceuticals.
A phenolphthalein that is used as a diagnostic aid in hepatic function determination.
A sequence-related subfamily of ATP-BINDING CASSETTE TRANSPORTERS that actively transport organic substrates. Although considered organic anion transporters, a subset of proteins in this family have also been shown to convey drug resistance to neutral organic drugs. Their cellular function may have clinical significance for CHEMOTHERAPY in that they transport a variety of ANTINEOPLASTIC AGENTS. Overexpression of proteins in this class by NEOPLASMS is considered a possible mechanism in the development of multidrug resistance (DRUG RESISTANCE, MULTIPLE). Although similar in function to P-GLYCOPROTEINS, the proteins in this class share little sequence homology to the p-glycoprotein family of proteins.
F344 rats are an inbred strain of albino laboratory rats (Rattus norvegicus) that have been widely used in biomedical research due to their consistent and reliable genetic background, which facilitates the study of disease mechanisms and therapeutic interventions.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
'Sulfur-containing amino acids' are a category of amino acids, the building blocks of proteins, that include methionine and cysteine, which contain sulfur atoms as part of their side chains, playing crucial roles in protein structure, enzyme function, and antioxidant defense.
Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard.
A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Poly-glutathione peptides composed of (Glu-Cys)n-Gly where n is two to seven. They are biosynthesized by glutathione gamma-glutamylcysteinyltransferase and are found in many PLANTS; YEASTS; and algae. They sequester HEAVY METALS.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
The regular and simultaneous occurrence in a single interbreeding population of two or more discontinuous genotypes. The concept includes differences in genotypes ranging in size from a single nucleotide site (POLYMORPHISM, SINGLE NUCLEOTIDE) to large nucleotide sequences visible at a chromosomal level.
Azoles with an OXYGEN and a NITROGEN next to each other at the 1,2 positions, in contrast to OXAZOLES that have nitrogens at the 1,3 positions.
A non-selective post-emergence, translocated herbicide. According to the Seventh Annual Report on Carcinogens (PB95-109781, 1994) this substance may reasonably be anticipated to be a carcinogen. (From Merck Index, 12th ed) It is an irreversible inhibitor of CATALASE, and thus impairs activity of peroxisomes.
Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.
An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse.
Diminished or failed response of an organism, disease or tissue to the intended effectiveness of a chemical or drug. It should be differentiated from DRUG TOLERANCE which is the progressive diminution of the susceptibility of a human or animal to the effects of a drug, as a result of continued administration.
Reduced (protonated) form of THIAZOLES. They can be oxidized to THIAZOLIDINEDIONES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A synthetic naphthoquinone without the isoprenoid side chain and biological activity, but can be converted to active vitamin K2, menaquinone, after alkylation in vivo.
A sulfur-containing essential L-amino acid that is important in many body functions.
Substances that increase the risk of NEOPLASMS in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Hydrolyzes pyroglutamic acid in the presence of ATP to glutamate plus ADP and inorganic phosphate. Deficiency leads to pyroglutamic acidurea.
A subtype of thioredoxin reductase found primarily in the CYTOSOL.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The conjugation product of LEUKOTRIENE A4 and glutathione. It is the major arachidonic acid metabolite in macrophages and human mast cells as well as in antigen-sensitized lung tissue. It stimulates mucus secretion in the lung, and produces contractions of nonvascular and some VASCULAR SMOOTH MUSCLE. (From Dictionary of Prostaglandins and Related Compounds, 1990)
Organic derivatives of thiocyanic acid which contain the general formula R-SCN.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.
Experimentally induced tumors of the LIVER.
A dietary deficiency of riboflavin causing a syndrome chiefly marked by cheilitis, angular stomatitis, glossitis associated with a purplish red or magenta-colored tongue that may show fissures, corneal vascularization, dyssebacia, and anemia. (Dorland, 27th ed)
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.
Acrolein is an unsaturated aldehyde (C3H4O), highly reactive, toxic and naturally occurring compound that can be found in certain foods, tobacco smoke and is produced as a result of environmental pollution or industrial processes.
An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.
A sulfhydryl reagent that is widely used in experimental biochemical studies.
A poisonous dipyridilium compound used as contact herbicide. Contact with concentrated solutions causes irritation of the skin, cracking and shedding of the nails, and delayed healing of cuts and wounds.
Inorganic compounds that contain selenium as an integral part of the molecule.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
The reversibly oxidized form of ascorbic acid. It is the lactone of 2,3-DIKETOGULONIC ACID and has antiscorbutic activity in man on oral ingestion.
The conjugation of exogenous substances with various hydrophilic substituents to form water soluble products that are excretable in URINE. Phase II modifications include GLUTATHIONE conjugation; ACYLATION; and AMINATION. Phase II enzymes include GLUTATHIONE TRANSFERASE and GLUCURONOSYLTRANSFERASE. In a sense these reactions detoxify phase I reaction products.
'Amino Acid Transport System y+', also known as System Y+, is a sodium-independent cationic amino acid transporter that mediates the uptake of primarily basic amino acids, such as arginine and lysine, into cells through a facilitated diffusion process.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
Diagnostic aid in pancreas function determination.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.
Hydroquinones are chemical compounds that function as potent depigmenting agents, inhibiting the enzymatic conversion of tyrosine to melanin, used topically in the treatment of various dermatological disorders such as melasma, freckles, and hyperpigmentation.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.
A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.
A quinone fungicide used for treatment of seeds and foliage.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Synthetic or natural substances which are given to prevent a disease or disorder or are used in the process of treating a disease or injury due to a poisonous agent.
A cell-cycle phase nonspecific alkylating antineoplastic agent. It is used in the treatment of brain tumors and various other malignant neoplasms. (From Martindale, The Extra Pharmacopoeia, 30th ed, p462) This substance may reasonably be anticipated to be a carcinogen according to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985). (From Merck Index, 11th ed)
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Transport proteins that carry specific substances in the blood or across cell membranes.
An emulsifying agent produced in the LIVER and secreted into the DUODENUM. Its composition includes BILE ACIDS AND SALTS; CHOLESTEROL; and ELECTROLYTES. It aids DIGESTION of fats in the duodenum.
A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.
The main structural component of the LIVER. They are specialized EPITHELIAL CELLS that are organized into interconnected plates called lobules.

Overexpression of CuZn superoxide dismutase protects RAW 264.7 macrophages against nitric oxide cytotoxicity. (1/9145)

Initiation of nitric oxide (NO.)-mediated apoptotic cell death in RAW 264.7 macrophages is associated with up-regulation of mitochondrial manganese superoxide dismutase (MnSOD; SOD2) and down-regulation of cytosolic copper zinc superoxide dismutase (CuZnSOD; SOD1) at their individual mRNA and protein levels. To evaluate the decreased CuZnSOD expression and the initiation of apoptosis we stably transfected macrophages to overexpress human CuZnSOD. Individual clones revealed a 2-fold increase in CuZnSOD activity. Expression of a functional and thus protective CuZnSOD was verified by attenuated superoxide (O2(.)-)-mediated apoptotic as well as necrotic cell death. In this study we showed that SOD-overexpressing macrophages (R-SOD1-12) were also protected against NO.-initiated programmed cell death. Protection was substantial towards NO. derived from exogenously added NO donors or when NO. was generated by inducible NO synthase activation, and was evident at the level of p53 accumulation, caspase activation and DNA fragmentation. Stimulation of parent and SOD-overexpressing cells with a combination of lipopolysaccharide and murine interferon gamma produced equivalent amounts of nitrite/nitrate, which ruled out attenuated inducible NO. synthase activity during protection. Because protection by a O2(.)--scavenging system during NO. -intoxication implies a role of NO. and O2(.)- in the progression of cell damage, we used uric acid to delineate the role of peroxynitrite during NO.-elicited apoptosis. The peroxynitrite scavenger uric acid left S-nitrosoglutathione or spermine-NO-elicited apoptosis unaltered, blocking only 3-morpholinosydnonimine-mediated cell death. As a result we exclude peroxynitrite from contributing, to any major extent, to NO. -mediated apoptosis. Therefore protection observed with CuZnSOD overexpression is unlikely to stem from interference with peroxynitrite formation and/or action. Unequivocally, the down-regulation of CuZnSOD is associated with NO. cytotoxicity, whereas CuZnSOD overexpression protects macrophages from apoptosis.  (+info)

Differential regulation of vascular endothelial growth factor and its receptor fms-like-tyrosine kinase is mediated by nitric oxide in rat renal mesangial cells. (2/9145)

Under conditions associated with local and systemic inflammation, mesangial cells and invading immune cells are likely to be responsible for the release of large amounts of nitric oxide (NO) in the glomerulus. To further define the mechanisms of NO action in the glomerulus, we attempted to identify genes which are regulated by NO in rat glomerular mesangial cells. We identified vascular endothelial growth factor (VEGF) and its receptor fms-like tyrosine kinase (FLT-1) to be under the regulatory control of exogenously applied NO in these cells. Using S-nitroso-glutathione (GSNO) as an NO-donating agent, VEGF expression was strongly induced, whereas expression of its FLT-1 receptor simultaneously decreased. Expressional regulation of VEGF and FLT-1 mRNA was transient and occurred rapidly within 1-3 h after GSNO treatment. Expression of a second VEGF-specific receptor, fetal liver kinase-1 (FLK-1/KDR), could not be detected. The inflammatory cytokine interleukin-1beta mediated a moderate increase in VEGF expression after 24 h and had no influence on FLT-1 expression. In contrast, platelet-derived growth factor-BB and basic fibroblast growth factor had no effect on VEGF expression, but strongly induced FLT-1 mRNA levels. Obviously, there is a differential regulation of VEGF and its receptor FLT-1 by NO, cytokines and growth factors in rat mesangial cells.  (+info)

Canalicular multispecific organic anion transporter/multidrug resistance protein 2 mediates low-affinity transport of reduced glutathione. (3/9145)

The canalicular multispecific organic anion transporter (cMOAT), a member of the ATP-binding cassette transporter family, mediates the transport of a broad range of non-bile salt organic anions from liver into bile. cMOAT-deficient Wistar rats (TR-) are mutated in the gene encoding cMOAT, leading to defective hepatobiliary transport of a whole range of substrates, including bilirubin glucuronide. These mutants also have impaired hepatobiliary excretion of GSH and, as a result, the bile flow in these animals is reduced. In the present work we demonstrate a role for cMOAT in the excretion of GSH both in vivo and in vitro. Biliary GSH excretion in rats heterozygous for the cMOAT mutation (TR/tr) was decreased to 63% of controls (TR/TR) (114+/-24 versus 181+/-20 nmol/min per kg body weight). Madin-Darby canine kidney (MDCK) II cells stably expressing the human cMOAT protein displayed >10-fold increase in apical GSH excretion compared with wild-type MDCKII cells (141+/-6.1 pmol/min per mg of protein versus 13.2+/-1.3 pmol/min per mg of protein in wild-type MDCKII cells). Similarly, MDCKII cells expressing the human multidrug resistance protein 1 showed a 4-fold increase in GSH excretion across the basolateral membrane. In several independent cMOAT-transfectants, the level of GSH excretion correlated with the expression level of the protein. Furthermore, we have shown, in cMOAT-transfected cells, that GSH is a low-affinity substrate for the transporter and that its excretion is reduced upon ATP depletion. In membrane vesicles isolated from cMOAT-expressing MDCKII cells, ATP-dependent S-(2,4-dinitrophenyl)glutathione uptake is competitively inhibited by high concentrations of GSH (Ki approximately 20 mM). We concluded that cMOAT mediates low-affinity transport of GSH. However, since hepatocellular GSH concentrations are high (5-10 mM), cMOAT might serve an important physiological function in maintenance of bile flow in addition to hepatic GSH turnover.  (+info)

Regulation of 2-carboxy-D-arabinitol 1-phosphate phosphatase: activation by glutathione and interaction with thiol reagents. (4/9145)

2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase de- grades CA1P, an inhibitor associated with the regulation of ribulose bisphosphate carboxylase/oxygenase in numerous plant species. CA1P phosphatase purified from Phaseolus vulgaris was partially inactivated by oxidizing conditions during dialysis in air-equilibrated buffer. Phosphatase activity could then be stimulated 1.3-fold by dithiothreitol and also by addition of reduced thioredoxin from Escherichia coli. These effects were enhanced synergistically by the positive effector, fructose 1, 6-bisphosphate (FBP). Most notably, CA1P phosphatase activity was stimulated up to 35-fold by glutathione, and was sensitive to the ratio of reduced (GSH) to oxidized (GSSG) forms. At concentrations of glutathione approximating measured levels in chloroplasts of P. vulgaris (5 mM total S), CA1P phosphatase exhibited >20-fold stimulation by a change in the redox status of glutathione from 60 to 100% GSH. This stimulation was augmented further by reduced E. coli thioredoxin. In contrast, FBP, which activates CA1P phosphatase under reducing conditions, was strongly inhibitory in the presence of GSSG. We propose that glutathione may have an appreciable role in the light/dark regulation of CA1P phosphatase in vivo. A model for the reversible activation of CA1P phosphatase by GSH was derived based upon the various responses of the enzyme's activity to a range of thiol reagents including N-ethylmaleimide, 5, 5'-dithiobis-(2-nitrobenzoic acid) and arsenite. These data indicate that the bean enzyme contains two physically distinct sets of thiol groups that are critical to its redox regulation.  (+info)

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. (5/9145)

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.  (+info)

Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. (6/9145)

Myeloperoxidase (MPO) is the most abundant protein in neutrophils and plays a central role in microbial killing and inflammatory tissue damage. Because most of the non-steroidal anti-inflammatory drugs and other drugs contain a thiol group, it is necessary to understand how these substrates are oxidized by MPO. We have performed transient kinetic measurements to study the oxidation of 14 aliphatic and aromatic mono- and dithiols by the MPO intermediates, Compound I (k3) and Compound II (k4), using sequential mixing stopped-flow techniques. The one-electron reduction of Compound I by aromatic thiols (e.g. methimidazole, 2-mercaptopurine and 6-mercaptopurine) varied by less than a factor of seven (between 1.39 +/- 0.12 x 10(5) M(-1) s(-1) and 9.16 +/- 1.63 x 10(5) M(-1) s(-1)), whereas reduction by aliphatic thiols was demonstrated to depend on their overall net charge and hydrophobic character and not on the percentage of thiol deprotonation or redox potential. Cysteamine, cysteine methyl ester, cysteine ethyl ester and alpha-lipoic acid showed k3 values comparable to aromatic thiols, whereas a free carboxy group (e.g. cysteine, N-acetylcysteine, glutathione) diminished k3 dramatically. The one-electron reduction of Compound II was far more constrained by the nature of the substrate. Reduction by methimidazole, 2-mercaptopurine and 6-mercaptopurine showed second-order rate constants (k4) of 1.33 +/- 0.08 x 10(5) M(-1) s(-1), 5.25 +/- 0.07 x 10(5) M(-1) s(-1) and 3.03 +/- 0.07 x 10(3) M(-1) s(-1). Even at high concentrations cysteine, penicillamine and glutathione could not reduce Compound II, whereas cysteamine (4.27 +/- 0.05 x 10(3) M(-1) s(-1)), cysteine methyl ester (8.14 +/- 0.08 x 10(3) M(-1) s(-1)), cysteine ethyl ester (3.76 +/- 0.17 x 10(3) M(-1) s(-1)) and alpha-lipoic acid (4.78 +/- 0.07 x 10(4) M(-1) s(-1)) were demonstrated to reduce Compound II and thus could be expected to be oxidized by MPO without co-substrates.  (+info)

Glutathione-independent prostaglandin D2 synthase in ram and stallion epididymal fluids: origin and regulation. (7/9145)

Microsequencing after two-dimensional electrophoresis revealed a major protein, glutathione-independent prostaglandin D2 synthase (PGDS) in the anterior epididymal region fluid of the ram and stallion. In this epididymal region, PGDS was a polymorphic compound with a molecular mass around 30 kDa and a range of pI from 4 to 7. PGDS represented 15% and 8% of the total luminal proteins present in this region in the ram and stallion, respectively. The secretion of the protein as judged by in vitro biosynthesis, and the presence of its mRNA as studied by Northern blot analysis, were limited to the proximal caput epididymidis. Using a specific polyclonal antibody raised against a synthetic peptide, PGDS was found throughout the epididymis, decreasing in concentration toward the cauda region. PGDS was also detected in the testicular fluid and seminal plasma by Western blotting. Castration and efferent duct ligation in the ram led to a decrease in PGDS mRNA and secretion. PGDS mRNA was not detected in the stallion 1 mo after castration, and it was restored by testosterone supplementation. This study showed that PGDS is present in the environment of spermatozoa throughout the male genital tract. Its function in the maturation and/or protection of spermatozoa is unknown.  (+info)

Nitric oxide inhibits cardiac energy production via inhibition of mitochondrial creatine kinase. (8/9145)

Nitric oxide biosynthesis in cardiac muscle leads to a decreased oxygen consumption and lower ATP synthesis. It is suggested that this effect of nitric oxide is mainly due to the inhibition of the mitochondrial respiratory chain enzyme, cytochrome c oxidase. However, this work demonstrates that nitric oxide is able to inhibit soluble mitochondrial creatine kinase (CK), mitochondrial CK bound in purified mitochondria, CK in situ in skinned fibres as well as the functional activity of mitochondrial CK in situ in skinned fibres. Since mitochondrial isoenzyme is functionally coupled to oxidative phosphorylation, its inhibition also leads to decreased sensitivity of mitochondrial respiration to ADP and thus decreases ATP synthesis and oxygen consumption under physiological ADP concentrations.  (+info)

Glutathione is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It is a vital antioxidant that plays an essential role in maintaining cellular health and function. Glutathione helps protect cells from oxidative stress by neutralizing free radicals, which are unstable molecules that can damage cells and contribute to aging and diseases such as cancer, heart disease, and dementia. It also supports the immune system, detoxifies harmful substances, and regulates various cellular processes, including DNA synthesis and repair.

Glutathione is found in every cell of the body, with particularly high concentrations in the liver, lungs, and eyes. The body can produce its own glutathione, but levels may decline with age, illness, or exposure to toxins. As such, maintaining optimal glutathione levels through diet, supplementation, or other means is essential for overall health and well-being.

Glutathione transferases (GSTs) are a group of enzymes involved in the detoxification of xenobiotics and endogenous compounds. They facilitate the conjugation of these compounds with glutathione, a tripeptide consisting of cysteine, glutamic acid, and glycine, which results in more water-soluble products that can be easily excreted from the body.

GSTs play a crucial role in protecting cells against oxidative stress and chemical injury by neutralizing reactive electrophilic species and peroxides. They are found in various tissues, including the liver, kidneys, lungs, and intestines, and are classified into several families based on their structure and function.

Abnormalities in GST activity have been associated with increased susceptibility to certain diseases, such as cancer, neurological disorders, and respiratory diseases. Therefore, GSTs have become a subject of interest in toxicology, pharmacology, and clinical research.

Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.

Glutathione reductase (GR) is an enzyme that plays a crucial role in maintaining the cellular redox state. The primary function of GR is to reduce oxidized glutathione (GSSG) to its reduced form (GSH), which is an essential intracellular antioxidant. This enzyme utilizes nicotinamide adenine dinucleotide phosphate (NADPH) as a reducing agent in the reaction, converting it to NADP+. The medical definition of Glutathione Reductase is:

Glutathione reductase (GSR; EC 1.8.1.7) is a homodimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH) in the presence of NADPH as a cofactor. This enzyme is essential for maintaining the cellular redox balance and protecting cells from oxidative stress by regenerating the active form of glutathione, a vital antioxidant and detoxifying agent.

Glutathione disulfide (GSSG) is the oxidized form of glutathione (GSH), which is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It plays a crucial role in maintaining cellular redox homeostasis by scavenging free radicals and reactive oxygen species (ROS) in the body.

Glutathione exists in two forms - reduced (GSH) and oxidized (GSSG). In the reduced form, glutathione has a sulfhydryl group (-SH), which can donate an electron to neutralize free radicals and ROS. When glutathione donates an electron, it becomes oxidized and forms glutathione disulfide (GSSG).

Glutathione disulfide is a dimer of two glutathione molecules linked by a disulfide bond (-S-S-) between the sulfur atoms of their cysteine residues. The body can recycle GSSG back to its reduced form (GSH) through the action of an enzyme called glutathione reductase, which requires NADPH as a reducing agent.

Maintaining a proper balance between GSH and GSSG is essential for cellular health, as it helps regulate various physiological processes such as DNA synthesis, gene expression, immune function, and apoptosis (programmed cell death). An imbalance in glutathione homeostasis can lead to oxidative stress, inflammation, and the development of various diseases.

Glutathione synthase is a type of enzyme involved in the synthesis of glutathione, a vital antioxidant that helps protect cells from damage caused by free radicals and peroxides. Glutathione synthase specifically catalyzes the final step in glutathione biosynthesis, which is the reaction between gamma-glutamylcysteine and glycine to form glutathione. This enzyme plays a crucial role in maintaining cellular health and function by helping to regulate oxidative stress and other important physiological processes.

Buthionine Sulfoximine (BSO) is a chemical compound that is known to inhibit the enzyme gamma-glutamylcysteine synthetase, which plays a crucial role in the production of glutathione, a powerful antioxidant in the body. By inhibiting this enzyme, BSO can deplete glutathione levels in cells, making it a useful tool in research to study the effects of glutathione depletion on various biological processes. It is often used in laboratory experiments and clinical trials for its potential therapeutic benefits in cancer treatment and other diseases associated with oxidative stress. However, its use as a therapeutic agent is still being investigated and has not yet been approved by regulatory agencies for widespread clinical use.

Glutathione S-transferase Pi (GSTP1) is a member of the glutathione S-transferase (GST) family, which are enzymes involved in the detoxification of xenobiotics and endogenous compounds. GSTs catalyze the conjugation of reduced glutathione to these electrophilic compounds, facilitating their excretion from the body.

GSTP1 is primarily found in the cytosol of cells and has a high affinity for a variety of substrates, including polycyclic aromatic hydrocarbons, heterocyclic amines, and certain chemotherapeutic drugs. It plays an essential role in protecting cells against oxidative stress and chemical-induced damage.

Polymorphisms in the GSTP1 gene have been associated with altered enzyme activity and susceptibility to various diseases, including cancer, neurological disorders, and respiratory diseases. The most common polymorphism in GSTP1 is a single nucleotide substitution (Ile105Val), which has been shown to reduce the enzyme's catalytic activity and increase the risk of developing certain types of cancer.

Glutamate-cysteine ligase (GCL) is an essential enzyme in the biosynthesis of glutathione, a major antioxidant in cells. It catalyzes the reaction between glutamate and cysteine to form γ-glutamylcysteine, which is then combined with glycine by glutathione synthetase to produce glutathione.

GCL has two subunits: a catalytic subunit (GCLC) and a modulatory subunit (GCLM). The former contains the active site for the formation of the peptide bond between glutamate and cysteine, while the latter regulates the activity of GCLC by affecting its sensitivity to feedback inhibition by glutathione.

The proper functioning of GCL is critical for maintaining cellular redox homeostasis and protecting against oxidative stress, making it a potential target for therapeutic intervention in various diseases associated with oxidative damage, such as neurodegenerative disorders, cancer, and aging-related conditions.

Dinitrochlorobenzene (DNCB) is a chemical compound that is classified as an aromatic organic compound. Its medical definition relates to its use as a topical immunotherapy for the treatment of certain skin conditions. DNCB is a potent sensitizer and hapten, which means that it can cause an immune response when it comes into contact with the skin.

When applied to the skin, DNCB can stimulate the production of antibodies and activate immune cells, leading to an inflammatory reaction. This property has been exploited in the treatment of conditions such as alopecia areata, a type of hair loss that is thought to be caused by an autoimmune response. By sensitizing the patient's immune system to DNCB, it may be possible to modulate the immune response and promote hair growth.

However, the use of DNCB as a therapeutic agent is not without risks. It can cause significant local reactions, including redness, swelling, and blistering, and there is a risk of systemic toxicity if it is absorbed into the bloodstream. As such, its use is generally restricted to specialized medical settings where it can be administered under close supervision.

Oxidative stress is defined as an imbalance between the production of reactive oxygen species (free radicals) and the body's ability to detoxify them or repair the damage they cause. This imbalance can lead to cellular damage, oxidation of proteins, lipids, and DNA, disruption of cellular functions, and activation of inflammatory responses. Prolonged or excessive oxidative stress has been linked to various health conditions, including cancer, cardiovascular diseases, neurodegenerative disorders, and aging-related diseases.

Methionine Sulfoximine (MSO) is not a medical term itself, but it is a compound that has been used in research and scientific studies. It's a stable analogue of the essential amino acid methionine, which can be found in some foods like sesame seeds, Brazil nuts, and fish.

Methionine Sulfoximine has been used in research to study the metabolism and transport of methionine in cells and organisms. It is also known for its ability to inhibit the enzyme cystathionine β-synthase (CBS), which plays a role in the metabolism of homocysteine, an amino acid associated with cardiovascular disease when present at high levels.

However, Methionine Sulfoximine is not used as a therapeutic agent or medication in humans due to its potential toxicity and lack of established clinical benefits.

Antioxidants are substances that can prevent or slow damage to cells caused by free radicals, which are unstable molecules that the body produces as a reaction to environmental and other pressures. Antioxidants are able to neutralize free radicals by donating an electron to them, thus stabilizing them and preventing them from causing further damage to the cells.

Antioxidants can be found in a variety of foods, including fruits, vegetables, nuts, and grains. Some common antioxidants include vitamins C and E, beta-carotene, and selenium. Antioxidants are also available as dietary supplements.

In addition to their role in protecting cells from damage, antioxidants have been studied for their potential to prevent or treat a number of health conditions, including cancer, heart disease, and age-related macular degeneration. However, more research is needed to fully understand the potential benefits and risks of using antioxidant supplements.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.

Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.

The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.

It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.

Catalase is a type of enzyme that is found in many living organisms, including humans. Its primary function is to catalyze the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from the harmful effects of hydrogen peroxide, which can be toxic at high concentrations.

The chemical reaction catalyzed by catalase can be represented as follows:

H2O2 + Catalase → H2O + O2 + Catalase

Catalase is a powerful antioxidant enzyme that plays an important role in protecting cells from oxidative damage. It is found in high concentrations in tissues that produce or are exposed to hydrogen peroxide, such as the liver, kidneys, and erythrocytes (red blood cells).

Deficiency in catalase activity has been linked to several diseases, including cancer, neurodegenerative disorders, and aging. On the other hand, overexpression of catalase has been shown to have potential therapeutic benefits in various disease models, such as reducing inflammation and oxidative stress.

"Maleate" is not a medical term in and of itself, but it is a chemical compound that can be found in some medications. Maleic acid or its salts (maleates) are used as a keratolytic agent in topical medications, which means they help to break down and remove dead skin cells. They can also be used as a preservative or a buffering agent in various pharmaceutical preparations.

Maleic acid is a type of organic compound known as a dicarboxylic acid, which contains two carboxyl groups. In the case of maleic acid, these carboxyl groups are located on a single carbon atom, which makes it a cis-conjugated diacid. This structural feature gives maleic acid unique chemical properties that can be useful in various pharmaceutical and industrial applications.

It's worth noting that maleic acid and its salts should not be confused with "maleate" as a gender-specific term, which refers to something related to or characteristic of males.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

Lipid peroxidation is a process in which free radicals, such as reactive oxygen species (ROS), steal electrons from lipids containing carbon-carbon double bonds, particularly polyunsaturated fatty acids (PUFAs). This results in the formation of lipid hydroperoxides, which can decompose to form a variety of compounds including reactive carbonyl compounds, aldehydes, and ketones.

Malondialdehyde (MDA) is one such compound that is commonly used as a marker for lipid peroxidation. Lipid peroxidation can cause damage to cell membranes, leading to changes in their fluidity and permeability, and can also result in the modification of proteins and DNA, contributing to cellular dysfunction and ultimately cell death. It is associated with various pathological conditions such as atherosclerosis, neurodegenerative diseases, and cancer.

Acetylcysteine is a medication that is used for its antioxidant effects and to help loosen thick mucus in the lungs. It is commonly used to treat conditions such as chronic bronchitis, emphysema, and cystic fibrosis. Acetylcysteine is also known by the brand names Mucomyst and Accolate. It works by thinning and breaking down mucus in the airways, making it easier to cough up and clear the airways. Additionally, acetylcysteine is an antioxidant that helps to protect cells from damage caused by free radicals. It is available as a oral tablet, liquid, or inhaled medication.

Gamma-glutamyltransferase (GGT), also known as gamma-glutamyl transpeptidase, is an enzyme found in many tissues, including the liver, bile ducts, and pancreas. GGT is involved in the metabolism of certain amino acids and plays a role in the detoxification of various substances in the body.

GGT is often measured as a part of a panel of tests used to evaluate liver function. Elevated levels of GGT in the blood may indicate liver disease or injury, bile duct obstruction, or alcohol consumption. However, it's important to note that several other factors can also affect GGT levels, so abnormal results should be interpreted in conjunction with other clinical findings and diagnostic tests.

Medical Definition:

Superoxide dismutase (SOD) is an enzyme that catalyzes the dismutation of superoxide radicals (O2-) into oxygen (O2) and hydrogen peroxide (H2O2). This essential antioxidant defense mechanism helps protect the body's cells from damage caused by reactive oxygen species (ROS), which are produced during normal metabolic processes and can lead to oxidative stress when their levels become too high.

There are three main types of superoxide dismutase found in different cellular locations:
1. Copper-zinc superoxide dismutase (CuZnSOD or SOD1) - Present mainly in the cytoplasm of cells.
2. Manganese superoxide dismutase (MnSOD or SOD2) - Located within the mitochondrial matrix.
3. Extracellular superoxide dismutase (EcSOD or SOD3) - Found in the extracellular spaces, such as blood vessels and connective tissues.

Imbalances in SOD levels or activity have been linked to various pathological conditions, including neurodegenerative diseases, cancer, and aging-related disorders.

Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Reactive Oxygen Species (ROS) are highly reactive molecules containing oxygen, including peroxides, superoxide, hydroxyl radical, and singlet oxygen. They are naturally produced as byproducts of normal cellular metabolism in the mitochondria, and can also be generated by external sources such as ionizing radiation, tobacco smoke, and air pollutants. At low or moderate concentrations, ROS play important roles in cell signaling and homeostasis, but at high concentrations, they can cause significant damage to cell structures, including lipids, proteins, and DNA, leading to oxidative stress and potential cell death.

Cystine is a naturally occurring amino acid in the body, which is formed from the oxidation of two cysteine molecules. It is a non-essential amino acid, meaning that it can be produced by the body and does not need to be obtained through diet. Cystine plays important roles in various biological processes, including protein structure and antioxidant defense. However, when cystine accumulates in large amounts, it can form crystals or stones, leading to conditions such as cystinuria, a genetic disorder characterized by the formation of cystine kidney stones.

Malondialdehyde (MDA) is a naturally occurring organic compound that is formed as a byproduct of lipid peroxidation, a process in which free radicals or reactive oxygen species react with polyunsaturated fatty acids. MDA is a highly reactive aldehyde that can modify proteins, DNA, and other biomolecules, leading to cellular damage and dysfunction. It is often used as a marker of oxidative stress in biological systems and has been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Glutaredoxins (Grxs) are small, ubiquitous proteins that belong to the thioredoxin superfamily. They play a crucial role in maintaining the redox balance within cells by catalyzing the reversible reduction of disulfide bonds and mixed disulfides between protein thiols and low molecular weight compounds, using glutathione (GSH) as a reducing cofactor.

Glutaredoxins are involved in various cellular processes, such as:

1. DNA synthesis and repair
2. Protein folding and degradation
3. Antioxidant defense
4. Regulation of enzyme activities
5. Iron-sulfur cluster biogenesis

There are two main classes of glutaredoxins, Grx1 and Grx2, which differ in their active site sequences and functions. In humans, Grx1 is primarily located in the cytosol, while Grx2 is found in both the cytosol and mitochondria.

The medical relevance of glutaredoxins lies in their role as antioxidant proteins that protect cells from oxidative stress and maintain cellular redox homeostasis. Dysregulation of glutaredoxin function has been implicated in several pathological conditions, including neurodegenerative diseases, cancer, and aging-related disorders.

Pyrrolidonecarboxylic acid, also known as Proline or Prolinic acid, is an organic compound with the formula N-pyrrolidinecarboxylic acid. It is a cyclic amino acid, which means that its side chain is bonded to the rest of the molecule in a ring structure.

Proline is an important constituent of many proteins and plays a crucial role in maintaining the structural integrity of the protein. It is classified as a non-essential amino acid because it can be synthesized by the human body from other amino acids, such as glutamic acid.

Pyrrolidonecarboxylic acid has a variety of uses in medicine and industry, including as a chiral auxiliary in organic synthesis, a building block for pharmaceuticals, and a component in cosmetics and personal care products. It is also used as a buffering agent and a stabilizer in various medical and industrial applications.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Thiobarbituric acid reactive substances (TBARS) is not a medical term per se, but rather a method used to measure lipid peroxidation in biological samples. Lipid peroxidation is a process by which free radicals steal electrons from lipids, leading to cellular damage and potential disease progression.

The TBARS assay measures the amount of malondialdehyde (MDA), a byproduct of lipid peroxidation, that reacts with thiobarbituric acid (TBA) to produce a pink-colored complex. The concentration of this complex is then measured and used as an indicator of lipid peroxidation in the sample.

While TBARS has been widely used as a measure of oxidative stress, it has limitations, including potential interference from other compounds that can react with TBA and produce similar-colored complexes. Therefore, more specific and sensitive methods for measuring lipid peroxidation have since been developed.

Medical definitions of "oxidants" refer to them as oxidizing agents or substances that can gain electrons and be reduced. They are capable of accepting electrons from other molecules in chemical reactions, leading to the production of oxidation products. In biological systems, oxidants play a crucial role in various cellular processes such as energy production and immune responses. However, an imbalance between oxidant and antioxidant levels can lead to a state of oxidative stress, which has been linked to several diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Examples of oxidants include reactive oxygen species (ROS), such as superoxide anion, hydrogen peroxide, and hydroxyl radical, as well as reactive nitrogen species (RNS), such as nitric oxide and peroxynitrite.

I couldn't find a medical definition for "diamide" as it is not a term commonly used in medicine or biomedical sciences. The term "diamide" is a chemical name that refers to a compound containing two amide groups. It may have various uses in different scientific fields, such as chemistry and biochemistry, but it is not a medical term.

Metabolic detoxification, in the context of drugs, refers to the series of biochemical processes that the body undergoes to transform drugs or other xenobiotics into water-soluble compounds so they can be excreted. This process typically involves two phases:

1. Phase I Detoxification: In this phase, enzymes such as cytochrome P450 oxidases introduce functional groups into the drug molecule, making it more polar and reactive. This can result in the formation of metabolites that are less active than the parent compound or, in some cases, more toxic.

2. Phase II Detoxification: In this phase, enzymes such as glutathione S-transferases, UDP-glucuronosyltransferases, and sulfotransferases conjugate these polar and reactive metabolites with endogenous molecules like glutathione, glucuronic acid, or sulfate. This further increases the water solubility of the compound, allowing it to be excreted by the kidneys or bile.

It's important to note that while these processes are essential for eliminating drugs and other harmful substances from the body, they can also produce reactive metabolites that may cause damage to cells and tissues if not properly regulated. Therefore, maintaining a balance in the activity of these detoxification enzymes is crucial for overall health and well-being.

Ascorbic acid is the chemical name for Vitamin C. It is a water-soluble vitamin that is essential for human health. Ascorbic acid is required for the synthesis of collagen, a protein that plays a role in the structure of bones, tendons, ligaments, and blood vessels. It also functions as an antioxidant, helping to protect cells from damage caused by free radicals.

Ascorbic acid cannot be produced by the human body and must be obtained through diet or supplementation. Good food sources of vitamin C include citrus fruits, strawberries, bell peppers, broccoli, and spinach.

In the medical field, ascorbic acid is used to treat or prevent vitamin C deficiency and related conditions, such as scurvy. It may also be used in the treatment of various other health conditions, including common cold, cancer, and cardiovascular disease, although its effectiveness for these uses is still a matter of scientific debate.

Peroxides, in a medical context, most commonly refer to chemical compounds that contain the peroxide ion (O2−2). Peroxides are characterized by the presence of an oxygen-oxygen single bond and can be found in various substances.

In dentistry, hydrogen peroxide (H2O2) is a widely used agent for teeth whitening or bleaching due to its oxidizing properties. It can help remove stains and discoloration on the tooth surface by breaking down into water and oxygen-free radicals, which react with the stain molecules, ultimately leading to their oxidation and elimination.

However, it is essential to note that high concentrations of hydrogen peroxide or prolonged exposure can cause tooth sensitivity, irritation to the oral soft tissues, and potential damage to the dental pulp. Therefore, professional supervision and appropriate concentration control are crucial when using peroxides for dental treatments.

Ethacrynic acid is a loop diuretic drug that is primarily used to treat edema (swelling) associated with heart failure, liver cirrhosis, and kidney disease. It works by increasing the excretion of water and sodium in the urine, which helps reduce fluid buildup in the body. Ethacrynic acid is also known as a "high-ceiling" diuretic because it has a strong effect on urine production.

The drug is available in oral form and is typically taken once or twice a day, depending on the severity of the edema and the patient's response to treatment. Ethacrynic acid can have side effects, including hearing loss, kidney damage, and electrolyte imbalances, so it is important for patients to be monitored closely by their healthcare provider while taking this medication.

It is worth noting that ethacrynic acid is not as commonly used as other loop diuretics, such as furosemide or torsemide, due to its higher risk of side effects and the availability of safer alternatives.

Lipid peroxides are chemical compounds that form when lipids (fats or fat-like substances) oxidize. This process, known as lipid peroxidation, involves the reaction of lipids with oxygen in a way that leads to the formation of hydroperoxides and various aldehydes, such as malondialdehyde.

Lipid peroxidation is a naturally occurring process that can also be accelerated by factors such as exposure to radiation, certain chemicals, or enzymatic reactions. It plays a role in many biological processes, including cell signaling and regulation of gene expression, but it can also contribute to the development of various diseases when it becomes excessive.

Examples of lipid peroxides include phospholipid hydroperoxides, cholesteryl ester hydroperoxides, and triglyceride hydroperoxides. These compounds are often used as markers of oxidative stress in biological systems and have been implicated in the pathogenesis of atherosclerosis, cancer, neurodegenerative diseases, and other conditions associated with oxidative damage.

Tert-butylhydroperoxide (t-BuOOH) is not typically considered a medical term, but rather a chemical compound. It is used in some medical and laboratory contexts. Here's a definition:

Tert-butylhydroperoxide (t-BuOOH) is an organic peroxide with the formula (CH3)3COOH. It is a colorless liquid, commercially available in concentrations up to 70%. It is used as an initiator in chemical reactions, a source of hydroxyl radicals in free-radical chemistry, and as a reagent in organic synthesis. Its use in medical contexts is typically limited to laboratory research and not as a therapeutic agent.

Handling tert-butylhydroperoxide requires caution due to its potential to cause fires and explosions when it comes into contact with certain substances, especially reducing agents and strong acids. Always follow safety guidelines and use appropriate personal protective equipment when handling this compound.

S-Nitrosoglutathione (GSNO) is defined as a type of nitrosothiol, which is a class of compounds containing a nitroso (−NO) group attached to a sulfur atom. Specifically, GSNO is the result of the attachment of a nitric oxide (NO) molecule to the sulfur atom of the tripeptide glutathione (GSH). This compound has been the subject of extensive research due to its potential role in the regulation of various biological processes, including cell signaling, vasodilation, and neurotransmission, among others. It is also known to have antioxidant properties and to play a role in the immune response. However, it should be noted that abnormal levels of GSNO have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and cardiovascular disorders.

Thioredoxins are a group of small proteins that contain a redox-active disulfide bond and play a crucial role in the redox regulation of cellular processes. They function as electron donors and help to maintain the intracellular reducing environment by reducing disulfide bonds in other proteins, thereby regulating their activity. Thioredoxins also have antioxidant properties and protect cells from oxidative stress by scavenging reactive oxygen species (ROS) and repairing oxidatively damaged proteins. They are widely distributed in various organisms, including bacteria, plants, and animals, and are involved in many physiological processes such as DNA synthesis, protein folding, and apoptosis.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Lactoylglutathione lyase is not a commonly used term in medicine, but it is a biochemical term that refers to an enzyme also known as glyoxalase I. This enzyme plays a role in the detoxification of methylglyoxal, a reactive dicarbonyl compound that can cause damage to proteins and DNA. Methylglyoxal is produced during normal metabolic processes, particularly in the breakdown of glucose and other sugars.

Glyoxalase I catalyzes the conversion of hemithioacetal (formed from methylglyoxal and glutathione) to S-D-lactoylglutathione, which is then converted to D-lactic acid and glutathione by glyoxalase II. The overall reaction helps to prevent the accumulation of toxic levels of methylglyoxal in cells.

Defects or mutations in the gene that encodes for glyoxalase I can lead to an increased risk of developing certain diseases, such as diabetes and neurodegenerative disorders.

Thioredoxin-disulfide reductase (Txnrd, TrxR) is an enzyme that belongs to the pyridine nucleotide-disulfide oxidoreductase family. It plays a crucial role in maintaining the intracellular redox balance by reducing disulfide bonds in proteins and keeping them in their reduced state. This enzyme utilizes NADPH as an electron donor to reduce thioredoxin (Trx), which then transfers its electrons to various target proteins, thereby regulating their activity, protein folding, and antioxidant defense mechanisms.

Txnrd is essential for several cellular processes, including DNA synthesis, gene expression, signal transduction, and protection against oxidative stress. Dysregulation of Txnrd has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. Therefore, understanding the function and regulation of this enzyme is of great interest for developing novel therapeutic strategies.

Aldehydes are a class of organic compounds characterized by the presence of a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bonded oxygen atom, also known as a formyl or aldehyde group. The general chemical structure of an aldehyde is R-CHO, where R represents a hydrocarbon chain.

Aldehydes are important in biochemistry and medicine as they are involved in various metabolic processes and are found in many biological molecules. For example, glucose is converted to pyruvate through a series of reactions that involve aldehyde intermediates. Additionally, some aldehydes have been identified as toxicants or environmental pollutants, such as formaldehyde, which is a known carcinogen and respiratory irritant.

Formaldehyde is also commonly used in medical and laboratory settings for its disinfectant properties and as a fixative for tissue samples. However, exposure to high levels of formaldehyde can be harmful to human health, causing symptoms such as coughing, wheezing, and irritation of the eyes, nose, and throat. Therefore, appropriate safety measures must be taken when handling aldehydes in medical and laboratory settings.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Dithiothreitol (DTT) is a reducing agent, which is a type of chemical compound that breaks disulfide bonds between cysteine residues in proteins. DTT is commonly used in biochemistry and molecular biology research to prevent the formation of disulfide bonds during protein purification and manipulation.

Chemically, DTT is a small molecule with two sulfhydryl groups (-SH) that can donate electrons to oxidized cysteine residues in proteins, converting them to their reduced form (-S-H). This reaction reduces disulfide bonds and helps to maintain the solubility and stability of proteins.

DTT is also used as an antioxidant to prevent the oxidation of other molecules, such as DNA and enzymes, during experimental procedures. However, it should be noted that DTT can also reduce other types of bonds, including those in metal ions and certain chemical dyes, so its use must be carefully controlled and monitored.

Acetaminophen is a medication used to relieve pain and reduce fever. It is a commonly used over-the-counter drug and is also available in prescription-strength formulations. Acetaminophen works by inhibiting the production of prostaglandins, chemicals in the body that cause inflammation and trigger pain signals.

Acetaminophen is available in many different forms, including tablets, capsules, liquids, and suppositories. It is often found in combination with other medications, such as cough and cold products, sleep aids, and opioid pain relievers.

While acetaminophen is generally considered safe when used as directed, it can cause serious liver damage or even death if taken in excessive amounts. It is important to follow the dosing instructions carefully and avoid taking more than the recommended dose, especially if you are also taking other medications that contain acetaminophen.

If you have any questions about using acetaminophen or are concerned about potential side effects, it is always best to consult with a healthcare professional.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.

Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.

Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.

A dose-response relationship in the context of drugs refers to the changes in the effects or symptoms that occur as the dose of a drug is increased or decreased. Generally, as the dose of a drug is increased, the severity or intensity of its effects also increases. Conversely, as the dose is decreased, the effects of the drug become less severe or may disappear altogether.

The dose-response relationship is an important concept in pharmacology and toxicology because it helps to establish the safe and effective dosage range for a drug. By understanding how changes in the dose of a drug affect its therapeutic and adverse effects, healthcare providers can optimize treatment plans for their patients while minimizing the risk of harm.

The dose-response relationship is typically depicted as a curve that shows the relationship between the dose of a drug and its effect. The shape of the curve may vary depending on the drug and the specific effect being measured. Some drugs may have a steep dose-response curve, meaning that small changes in the dose can result in large differences in the effect. Other drugs may have a more gradual dose-response curve, where larger changes in the dose are needed to produce significant effects.

In addition to helping establish safe and effective dosages, the dose-response relationship is also used to evaluate the potential therapeutic benefits and risks of new drugs during clinical trials. By systematically testing different doses of a drug in controlled studies, researchers can identify the optimal dosage range for the drug and assess its safety and efficacy.

Selenoproteins are a specific group of proteins that contain the essential micronutrient selenium in the form of selenocysteine (Sec), which is a naturally occurring amino acid. Selenocysteine is encoded by the opal codon UGA, which typically serves as a stop codon in mRNA.

There are 25 known human selenoproteins, and they play crucial roles in various physiological processes, including antioxidant defense, DNA synthesis, thyroid hormone metabolism, and immune function. Some of the well-known selenoproteins include glutathione peroxidases (GPxs), thioredoxin reductases (TrxRs), and iodothyronine deiodinases (IDIs).

The presence of selenocysteine in these proteins makes them particularly efficient at catalyzing redox reactions, which involve the gain or loss of electrons. This property is essential for their functions as antioxidants and regulators of cellular signaling pathways.

Deficiencies in selenium can lead to impaired function of selenoproteins, potentially resulting in various health issues, such as increased oxidative stress, weakened immune response, and disrupted thyroid hormone metabolism.

Selenious acid, also known as selenic acid or hydrogen selenite, is not a substance that has a widely accepted medical definition. However, it is a chemical compound with the formula H2SeO3. It is a colorless, odorless liquid that is used in some industrial processes and is highly toxic if ingested or inhaled.

In the context of human health, selenium is an essential trace element that plays a critical role in various biological processes, including antioxidant defense systems, thyroid hormone metabolism, and immune function. Selenium can be found in various forms, including selenomethionine, selenocysteine, and selenite.

Selenious acid is not a form of selenium that is typically used or encountered in medical or nutritional contexts. However, it is possible that small amounts of selenious acid may be produced as an intermediate during the metabolism of certain selenium compounds in the body.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

Free radical scavengers, also known as antioxidants, are substances that neutralize or stabilize free radicals. Free radicals are highly reactive atoms or molecules with unpaired electrons, capable of causing damage to cells and tissues in the body through a process called oxidative stress. Antioxidants donate an electron to the free radical, thereby neutralizing it and preventing it from causing further damage. They can be found naturally in foods such as fruits, vegetables, and nuts, or they can be synthesized and used as dietary supplements. Examples of antioxidants include vitamins C and E, beta-carotene, and selenium.

Antimetabolites are a class of drugs that interfere with the normal metabolic processes of cells, particularly those involved in DNA replication and cell division. They are commonly used as chemotherapeutic agents to treat various types of cancer because many cancer cells divide more rapidly than normal cells. Antimetabolites work by mimicking natural substances needed for cell growth and division, such as nucleotides or amino acids, and getting incorporated into the growing cells' DNA or protein structures, which ultimately leads to the termination of cell division and death of the cancer cells. Examples of antimetabolites include methotrexate, 5-fluorouracil, and capecitabine.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Organoselenium compounds are organic chemicals that contain selenium, a naturally occurring non-metal element, in their structure. Selenium is chemically related to sulfur and can replace it in many organic molecules. Organoselenium compounds have been studied for their potential therapeutic benefits, including antioxidant, anti-cancer, and anti-inflammatory effects. They are also used as catalysts in chemical reactions. These compounds contain at least one carbon atom bonded to selenium, which can take the form of a variety of functional groups such as selenoethers, selenols, and selenoesters.

Free radicals are molecules or atoms that have one or more unpaired electrons in their outermost shell, making them highly reactive. They can be formed naturally in the body through processes such as metabolism and exercise, or they can come from external sources like pollution, radiation, and certain chemicals. Free radicals can cause damage to cells and contribute to the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Antioxidants are substances that can neutralize free radicals and help protect against their harmful effects.

Cell survival refers to the ability of a cell to continue living and functioning normally, despite being exposed to potentially harmful conditions or treatments. This can include exposure to toxins, radiation, chemotherapeutic drugs, or other stressors that can damage cells or interfere with their normal processes.

In scientific research, measures of cell survival are often used to evaluate the effectiveness of various therapies or treatments. For example, researchers may expose cells to a particular drug or treatment and then measure the percentage of cells that survive to assess its potential therapeutic value. Similarly, in toxicology studies, measures of cell survival can help to determine the safety of various chemicals or substances.

It's important to note that cell survival is not the same as cell proliferation, which refers to the ability of cells to divide and multiply. While some treatments may promote cell survival, they may also inhibit cell proliferation, making them useful for treating diseases such as cancer. Conversely, other treatments may be designed to specifically target and kill cancer cells, even if it means sacrificing some healthy cells in the process.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Biotransformation is the metabolic modification of a chemical compound, typically a xenobiotic (a foreign chemical substance found within an living organism), by a biological system. This process often involves enzymatic conversion of the parent compound to one or more metabolites, which may be more or less active, toxic, or mutagenic than the original substance.

In the context of pharmacology and toxicology, biotransformation is an important aspect of drug metabolism and elimination from the body. The liver is the primary site of biotransformation, but other organs such as the kidneys, lungs, and gastrointestinal tract can also play a role.

Biotransformation can occur in two phases: phase I reactions involve functionalization of the parent compound through oxidation, reduction, or hydrolysis, while phase II reactions involve conjugation of the metabolite with endogenous molecules such as glucuronic acid, sulfate, or acetate to increase its water solubility and facilitate excretion.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Nuclear factor erythroid-derived 2-like 2 (NFE2L2), also known as NF-E2-related factor 2 (NRF2), is a protein that plays a crucial role in the regulation of cellular responses to oxidative stress and electrophilic substances. It is a transcription factor that binds to the antioxidant response element (ARE) in the promoter region of various genes, inducing their expression and promoting cellular defense against harmful stimuli.

Under normal conditions, NRF2 is bound to its inhibitor, Kelch-like ECH-associated protein 1 (KEAP1), in the cytoplasm, where it is targeted for degradation by the proteasome. However, upon exposure to oxidative stress or electrophilic substances, KEAP1 undergoes conformational changes, leading to the release and stabilization of NRF2. Subsequently, NRF2 translocates to the nucleus, forms a complex with small Maf proteins, and binds to AREs, inducing the expression of genes involved in antioxidant response, detoxification, and cellular protection.

Genetic variations or dysregulation of the NFE2L2/KEAP1 pathway have been implicated in several diseases, including cancer, neurodegenerative disorders, and pulmonary fibrosis, highlighting its importance in maintaining cellular homeostasis and preventing disease progression.

Isothiocyanates are organic compounds that contain a functional group made up of a carbon atom, a nitrogen atom, and a sulfur atom, with the formula RN=C=S (where R can be an alkyl or aryl group). They are commonly found in cruciferous vegetables such as broccoli, brussels sprouts, and wasabi. Isothiocyanates have been studied for their potential health benefits, including their anticancer and anti-inflammatory properties. However, they can also be toxic in high concentrations.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Medical Definition of Vitamin E:

Vitamin E is a fat-soluble antioxidant that plays a crucial role in protecting your body's cells from damage caused by free radicals, which are unstable molecules produced when your body breaks down food or is exposed to environmental toxins like cigarette smoke and radiation. Vitamin E is also involved in immune function, DNA repair, and other metabolic processes.

It is a collective name for a group of eight fat-soluble compounds that include four tocopherols and four tocotrienols. Alpha-tocopherol is the most biologically active form of vitamin E in humans and is the one most commonly found in supplements.

Vitamin E deficiency is rare but can occur in people with certain genetic disorders or who cannot absorb fat properly. Symptoms of deficiency include nerve and muscle damage, loss of feeling in the arms and legs, muscle weakness, and vision problems.

Food sources of vitamin E include vegetable oils (such as sunflower, safflower, and wheat germ oil), nuts and seeds (like almonds, peanuts, and sunflower seeds), and fortified foods (such as cereals and some fruit juices).

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Ethylene dibromide (EDB) is an organic compound with the formula C2H4Br2. It is a colorless, volatile liquid with a chloroform-like odor. Ethylene dibromide is a member of the family of organobromine compounds.

Ethylene dibromide has been used as a pesticide, a fumigant, and a lead scavenger in gasoline. However, due to its toxicity and environmental persistence, its use has been largely phased out in many countries. It is still used in some industrial applications, such as the production of other chemicals.

Ethylene dibromide is a known human carcinogen and can cause a variety of health effects, including respiratory irritation, nausea, vomiting, and damage to the nervous system. Long-term exposure has been linked to an increased risk of cancer, particularly of the liver and kidneys. Therefore, it is important to handle this chemical with care and to use appropriate personal protective equipment when working with it.

Sodium Selenite is not a medical term per se, but it is a chemical compound with the formula Na2SeO3. It is used in medicine as a dietary supplement and also in veterinary medicine. Medically, it is used to treat selenium deficiency, which is rare.

Selenium is an essential trace element for human health, playing a crucial role in various physiological processes, such as antioxidant defense systems, thyroid hormone metabolism, and DNA synthesis. Sodium Selenite serves as a source of selenium in these medical applications.

Please note that supplementation with sodium selenite should be under the supervision of a healthcare professional, as excessive selenium intake can lead to selenosis, a condition characterized by symptoms like nausea, vomiting, hair loss, and neurological damage.

Butylated hydroxyanisole (BHA) is a synthetic antioxidant that is commonly used as a food additive to prevent or slow down the oxidation of fats, oils, and other lipids. This helps to maintain the quality, stability, and safety of food products by preventing rancidity and off-flavors. BHA is also used in cosmetics, pharmaceuticals, and animal feeds for similar purposes.

In medical terms, BHA is classified as a chemical preservative and antioxidant. It is a white or creamy white crystalline powder that is soluble in alcohol and ether but insoluble in water. BHA is often used in combination with other antioxidants, such as butylated hydroxytoluene (BHT), to provide a synergistic effect and enhance the overall stability of food products.

While BHA is generally recognized as safe by regulatory agencies such as the U.S. Food and Drug Administration (FDA) and the European Food Safety Authority (EFSA), some studies have suggested that high doses of BHA may have potential health risks, including possible carcinogenic effects. However, these findings are not conclusive, and further research is needed to fully understand the potential health impacts of BHA exposure.

Selenocysteine (Sec) is a rare, naturally occurring amino acid that contains selenium. It is encoded by the opal (TGA) codon, which typically signals stop translation in mRNA. However, when followed by a specific hairpin-like structure called the Sec insertion sequence (SECIS) element in the 3' untranslated region of the mRNA, the TGA codon is interpreted as a signal for selenocysteine incorporation during protein synthesis.

Selenocysteine plays an essential role in several enzymes involved in antioxidant defense and redox homeostasis, such as glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases. These enzymes require selenocysteine for their catalytic activity due to its unique chemical properties, which allow them to neutralize harmful reactive oxygen species (ROS) and maintain proper cellular function.

In summary, selenocysteine is a specialized amino acid containing selenium that is encoded by the TGA codon in mRNA when accompanied by a SECIS element. It is crucial for the activity of several enzymes involved in antioxidant defense and redox homeostasis.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Methylene chloride, also known as dichloromethane, is an organic compound with the formula CH2Cl2. It is a colorless, volatile liquid with a mild sweet aroma. In terms of medical definitions, methylene chloride is not typically included due to its primarily industrial uses. However, it is important to note that exposure to high levels of methylene chloride can cause harmful health effects, including irritation to the eyes, skin, and respiratory tract; headaches; dizziness; and, at very high concentrations, unconsciousness and death. Chronic exposure to methylene chloride has been linked to liver toxicity, and it is considered a possible human carcinogen by the International Agency for Research on Cancer (IARC).

Nitroso compounds are a class of chemical compounds that contain a nitroso functional group, which is composed of a nitrogen atom bonded to an oxygen atom with a single covalent bond. The general formula for nitroso compounds is R-N=O, where R represents an organic group such as an alkyl or aryl group.

Nitroso compounds are known to be reactive and can form under various physiological conditions. They have been implicated in the formation of carcinogenic substances and have been linked to DNA damage and mutations. In the medical field, nitroso compounds have been studied for their potential use as therapeutic agents, particularly in the treatment of cancer and cardiovascular diseases. However, their use is limited due to their potential toxicity and carcinogenicity.

It's worth noting that exposure to high levels of nitroso compounds can be harmful to human health, and may cause respiratory, dermal, and ocular irritation, as well as potential genotoxic effects. Therefore, handling and storage of nitroso compounds should be done with caution, following appropriate safety guidelines.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Aflatoxin B1 is a toxic metabolite produced by certain strains of the fungus Aspergillus flavus and Aspergillus parasiticus. It is a potent carcinogen and is classified as a Group 1 carcinogen by the International Agency for Research on Cancer (IARC). Aflatoxin B1 contamination can occur in a variety of agricultural products, including grains, nuts, spices, and dried fruits, and is a particular concern in regions with hot and humid climates. Exposure to aflatoxin B1 can occur through the consumption of contaminated food and has been linked to various health effects, including liver cancer, immune suppression, and stunted growth in children.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Selenoprotein P is a protein that contains several selenocysteine residues and is encoded by the SEPP1 gene in humans. It is primarily synthesized in the liver and secreted into the bloodstream, where it functions as a major antioxidant and a selenium transport protein. Selenoprotein P plays a crucial role in protecting cells against oxidative stress and has been implicated in various physiological processes, including neuroprotection, fertility, and immune function. Additionally, selenoprotein P has been suggested as a potential biomarker for selenium status and oxidative stress in the body.

Protein carbonylation is a post-translational modification of proteins, which involves the introduction of carbonyl groups (-CO) into amino acid side chains. This process can occur as a result of various reactive oxygen species (ROS) and oxidative stress, leading to the formation of protein adducts that can alter protein structure and function. Carbonylation can also be induced by advanced glycation end-products (AGEs), which are formed during non-enzymatic glycation reactions between reducing sugars and proteins. Protein carbonylation is often associated with aging, neurodegenerative diseases, and other pathological conditions characterized by oxidative stress and protein misfolding.

Drug-Induced Liver Injury (DILI) is a medical term that refers to liver damage or injury caused by the use of medications or drugs. This condition can vary in severity, from mild abnormalities in liver function tests to severe liver failure, which may require a liver transplant.

The exact mechanism of DILI can differ depending on the drug involved, but it generally occurs when the liver metabolizes the drug into toxic compounds that damage liver cells. This can happen through various pathways, including direct toxicity to liver cells, immune-mediated reactions, or metabolic idiosyncrasies.

Symptoms of DILI may include jaundice (yellowing of the skin and eyes), fatigue, abdominal pain, nausea, vomiting, loss of appetite, and dark urine. In severe cases, it can lead to complications such as ascites, encephalopathy, and bleeding disorders.

The diagnosis of DILI is often challenging because it requires the exclusion of other potential causes of liver injury. Liver function tests, imaging studies, and sometimes liver biopsies may be necessary to confirm the diagnosis. Treatment typically involves discontinuing the offending drug and providing supportive care until the liver recovers. In some cases, medications that protect the liver or promote its healing may be used.

Xenobiotics are substances that are foreign to a living organism and usually originate outside of the body. This term is often used in the context of pharmacology and toxicology to refer to drugs, chemicals, or other agents that are not naturally produced by or expected to be found within the body.

When xenobiotics enter the body, they undergo a series of biotransformation processes, which involve metabolic reactions that convert them into forms that can be more easily excreted from the body. These processes are primarily carried out by enzymes in the liver and other organs.

It's worth noting that some xenobiotics can have beneficial effects on the body when used as medications or therapeutic agents, while others can be harmful or toxic. Therefore, understanding how the body metabolizes and eliminates xenobiotics is important for developing safe and effective drugs, as well as for assessing the potential health risks associated with exposure to environmental chemicals and pollutants.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Bromobenzenes are a group of chemical compounds that consist of a benzene ring (a cyclic structure with six carbon atoms and alternating double bonds) substituted with one or more bromine atoms. The simplest and most common member of this group is bromobenzene itself, which contains a single bromine atom attached to a benzene ring.

Other members of the bromobenzenes family include dibromobenzene (with two bromine atoms), tribromobenzene (with three bromine atoms), and tetrabromobenzene (with four bromine atoms). These compounds are used in various industrial applications, such as in the production of flame retardants, dyes, pharmaceuticals, and agrochemicals.

It is important to note that bromobenzenes can be harmful or toxic to humans and other organisms, and should be handled with care. Exposure to high levels of these compounds can cause a range of health effects, including irritation of the skin, eyes, and respiratory tract, headaches, dizziness, nausea, and damage to the liver and kidneys.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Mercaptoethanol, also known as β-mercaptoethanol or BME, is not a medical term itself but is commonly used in laboratories including medical research. It is a reducing agent and a powerful antioxidant with the chemical formula HOCH2CH2SH.

Medical Definition:
Mercaptoethanol (β-mercaptoethanol) is a colorless liquid with an unpleasant odor, used as a reducing agent in biochemical research and laboratory experiments. It functions by breaking disulfide bonds between cysteine residues in proteins, allowing them to unfold and denature. This property makes it useful for various applications such as protein purification, enzyme assays, and cell culture.

However, it is important to note that Mercaptoethanol has a high toxicity level and should be handled with caution in the laboratory setting.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

Benzene derivatives are chemical compounds that are derived from benzene, which is a simple aromatic hydrocarbon with the molecular formula C6H6. Benzene has a planar, hexagonal ring structure, and its derivatives are formed by replacing one or more of the hydrogen atoms in the benzene molecule with other functional groups.

Benzene derivatives have a wide range of applications in various industries, including pharmaceuticals, dyes, plastics, and explosives. Some common examples of benzene derivatives include toluene, xylene, phenol, aniline, and nitrobenzene. These compounds can have different physical and chemical properties depending on the nature and position of the substituents attached to the benzene ring.

It is important to note that some benzene derivatives are known to be toxic or carcinogenic, and their production, use, and disposal must be carefully regulated to ensure safety and protect public health.

Sulfobromophthalein (BSP or bromsulphthalein) is not typically defined in a medical dictionary as it is a chemical compound. However, I can provide you with some information about its use in a medical context:

Sulfobromophthalein is a chemical compound primarily used for liver function tests. It is a dye that is injected into the patient's bloodstream, and then its clearance rate from the blood is measured to evaluate liver function. A healthy liver should quickly remove the dye from the blood and excrete it through the bile ducts into the digestive system. If the liver is not functioning properly, the clearance of sulfobromophthalein will be slower, leading to higher levels of the dye remaining in the bloodstream over time.

The test using sulfobromophthalein has largely been replaced by more modern and specific liver function tests; however, it was once widely used for assessing overall liver health and diagnosing conditions such as hepatitis, cirrhosis, and liver damage due to various causes.

Multidrug Resistance-Associated Proteins (MRPs) are a subfamily of ATP-binding cassette (ABC) transporter proteins that play a crucial role in the efflux of various substrates, including drugs and organic anions, out of cells. They are located in the plasma membrane of many cell types, including epithelial cells in the liver, intestine, kidney, and blood-brain barrier.

MRPs are known to transport a wide range of molecules, such as glutathione conjugates, bilirubin, bile acids, and various clinical drugs. One of the most well-known MRPs is MRP1 (ABCC1), which was initially identified in drug-resistant tumor cells. MRP1 can confer resistance to chemotherapeutic agents by actively pumping them out of cancer cells, thereby reducing their intracellular concentration and effectiveness.

The activity of MRPs can have significant implications for the pharmacokinetics and pharmacodynamics of drugs, as they can affect drug absorption, distribution, metabolism, and excretion (ADME). Understanding the function and regulation of MRPs is essential for developing strategies to overcome multidrug resistance in cancer therapy and optimizing drug dosing regimens in various clinical settings.

F344 is a strain code used to designate an outbred stock of rats that has been inbreeded for over 100 generations. The F344 rats, also known as Fischer 344 rats, were originally developed at the National Institutes of Health (NIH) and are now widely used in biomedical research due to their consistent and reliable genetic background.

Inbred strains, like the F344, are created by mating genetically identical individuals (siblings or parents and offspring) for many generations until a state of complete homozygosity is reached, meaning that all members of the strain have identical genomes. This genetic uniformity makes inbred strains ideal for use in studies where consistent and reproducible results are important.

F344 rats are known for their longevity, with a median lifespan of around 27-31 months, making them useful for aging research. They also have a relatively low incidence of spontaneous tumors compared to other rat strains. However, they may be more susceptible to certain types of cancer and other diseases due to their inbred status.

It's important to note that while F344 rats are often used as a standard laboratory rat strain, there can still be some genetic variation between individual animals within the same strain, particularly if they come from different suppliers or breeding colonies. Therefore, it's always important to consider the source and history of any animal model when designing experiments and interpreting results.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

Sulfur-containing amino acids are a type of amino acid that contain sulfur atoms in their side chains. There are three sulfur-containing amino acids that are considered essential for human health: methionine, cysteine, and homocysteine.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It contains a sulfur atom in its side chain and plays important roles in various biological processes, including methylation reactions, protein synthesis, and detoxification.

Cysteine is a semi-essential amino acid, which means that it can be synthesized by the human body under normal conditions but may become essential during periods of growth or illness. It contains a sulfhydryl group (-SH) in its side chain, which allows it to form disulfide bonds with other cysteine residues and contribute to the stability and structure of proteins.

Homocysteine is a non-proteinogenic amino acid that is derived from methionine metabolism. It contains a sulfur atom in its side chain and has been linked to various health problems, including cardiovascular disease, when present at elevated levels in the blood.

Other sulfur-containing amino acids include taurine, which is not incorporated into proteins but plays important roles in bile acid conjugation, antioxidant defense, and neuromodulation, and cystathionine, which is an intermediate in methionine metabolism.

A plant extract is a preparation containing chemical constituents that have been extracted from a plant using a solvent. The resulting extract may contain a single compound or a mixture of several compounds, depending on the extraction process and the specific plant material used. These extracts are often used in various industries including pharmaceuticals, nutraceuticals, cosmetics, and food and beverage, due to their potential therapeutic or beneficial properties. The composition of plant extracts can vary widely, and it is important to ensure their quality, safety, and efficacy before use in any application.

Peroxiredoxins (Prx) are a family of peroxidases that play a crucial role in cellular defense against oxidative stress. They catalyze the reduction of hydrogen peroxide, organic hydroperoxides, and peroxynitrite, thereby protecting cells from potentially harmful effects of these reactive oxygen and nitrogen species.

Peroxiredoxins are ubiquitously expressed in various cellular compartments, including the cytosol, mitochondria, and nucleus. They contain a conserved catalytic cysteine residue that gets oxidized during the reduction of peroxides, which is then reduced back to its active form by thioredoxins or other reducing agents.

Dysregulation of peroxiredoxin function has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders. Therefore, understanding the role of peroxiredoxins in cellular redox homeostasis is essential for developing novel therapeutic strategies to treat oxidative stress-related diseases.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Phytochelatins are low molecular weight, heavy metal-binding peptides that are synthesized by plants and some other organisms in response to exposure to toxic metals. They are composed of repeating units of the amino acids glutamic acid, cysteine, and glycine, with the general structure (γ-Glu-Cys)n-Gly, where n typically ranges from 2 to 5.

Phytochelatins are produced by the enzyme phytochelatin synthase, which is activated in the presence of heavy metals such as cadmium, mercury, and lead. Once synthesized, phytochelatins bind to these metals, forming metal-phytochelatin complexes that are then transported to the vacuole for sequestration and detoxification.

In addition to their role in heavy metal detoxification, phytochelatins have been shown to have antioxidant properties and may play a role in protecting plants against oxidative stress. They have also attracted interest as potential therapeutic agents for heavy metal poisoning in humans and other animals.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.

Isoxazoles are not a medical term, but a chemical compound. They are organic compounds containing a five-membered ring consisting of one nitrogen atom, one oxygen atom, and three carbon atoms. Isoxazoles have various applications in the pharmaceutical industry as they can be used to synthesize different drugs. Some isoxazole derivatives have been studied for their potential medicinal properties, such as anti-inflammatory, analgesic, and antipyretic effects. However, isoxazoles themselves are not a medical diagnosis or treatment.

Amitrole is a non-selective herbicide that is used to control broadleaf weeds and some annual grasses. Its chemical name is 3-amino-1,2,4-triazole, and it works by inhibiting the enzyme responsible for the production of certain aromatic amino acids in plants, which are essential for their growth and development.

Amitrole is absorbed through the leaves and roots of plants and can be applied either before or after weed emergence. It is commonly used in agricultural settings, as well as in non-crop areas such as industrial sites, railways, and roadsides.

While amitrole is generally considered safe for use around humans and animals when used according to label instructions, it can cause eye and skin irritation, and may be harmful if swallowed or inhaled. It is important to follow all safety precautions when handling and applying this herbicide.

Sulfhydryl reagents are chemical compounds that react with sulfhydryl groups (-SH), which are found in certain amino acids such as cysteine. These reagents can be used to modify or inhibit the function of proteins by forming disulfide bonds or adding functional groups to the sulfur atom. Examples of sulfhydryl reagents include N-ethylmaleimide (NEM), p-chloromercuribenzoate (PCMB), and iodoacetamide. These reagents are widely used in biochemistry and molecular biology research to study protein structure and function, as well as in the development of drugs and therapeutic agents.

Cadmium is a toxic heavy metal that is a byproduct of the mining and smelting of zinc, lead, and copper. It has no taste or smell and can be found in small amounts in air, water, and soil. Cadmium can also be found in some foods, such as kidneys, liver, and shellfish.

Exposure to cadmium can cause a range of health effects, including kidney damage, lung disease, fragile bones, and cancer. Cadmium is classified as a known human carcinogen by the International Agency for Research on Cancer (IARC) and the National Toxicology Program (NTP).

Occupational exposure to cadmium can occur in industries that produce or use cadmium, such as battery manufacturing, metal plating, and pigment production. Workers in these industries may be exposed to cadmium through inhalation of cadmium-containing dusts or fumes, or through skin contact with cadmium-containing materials.

The general population can also be exposed to cadmium through the environment, such as by eating contaminated food or breathing secondhand smoke. Smoking is a major source of cadmium exposure for smokers and those exposed to secondhand smoke.

Prevention measures include reducing occupational exposure to cadmium, controlling emissions from industrial sources, and reducing the use of cadmium in consumer products. Regular monitoring of air, water, and soil for cadmium levels can also help identify potential sources of exposure and prevent health effects.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

Cytochrome P-450 CYP2E1 is a specific isoform of the cytochrome P-450 enzyme system, which is involved in the metabolism of various xenobiotics and endogenous compounds. This enzyme is primarily located in the liver and to some extent in other organs such as the lungs, brain, and kidneys.

CYP2E1 plays a significant role in the metabolic activation of several procarcinogens, including nitrosamines, polycyclic aromatic hydrocarbons, and certain solvents. It also contributes to the oxidation of various therapeutic drugs, such as acetaminophen, anesthetics, and anticonvulsants. Overexpression or induction of CYP2E1 has been linked to increased susceptibility to chemical-induced toxicity, carcinogenesis, and alcohol-related liver damage.

The activity of CYP2E1 can be influenced by various factors, including genetic polymorphisms, age, sex, smoking status, and exposure to certain chemicals or drugs. Understanding the regulation and function of this enzyme is crucial for predicting individual susceptibility to chemical-induced toxicities and diseases, as well as for optimizing drug therapy and minimizing adverse effects.

Drug resistance, also known as antimicrobial resistance, is the ability of a microorganism (such as bacteria, viruses, fungi, or parasites) to withstand the effects of a drug that was originally designed to inhibit or kill it. This occurs when the microorganism undergoes genetic changes that allow it to survive in the presence of the drug. As a result, the drug becomes less effective or even completely ineffective at treating infections caused by these resistant organisms.

Drug resistance can develop through various mechanisms, including mutations in the genes responsible for producing the target protein of the drug, alteration of the drug's target site, modification or destruction of the drug by enzymes produced by the microorganism, and active efflux of the drug from the cell.

The emergence and spread of drug-resistant microorganisms pose significant challenges in medical treatment, as they can lead to increased morbidity, mortality, and healthcare costs. The overuse and misuse of antimicrobial agents, as well as poor infection control practices, contribute to the development and dissemination of drug-resistant strains. To address this issue, it is crucial to promote prudent use of antimicrobials, enhance surveillance and monitoring of resistance patterns, invest in research and development of new antimicrobial agents, and strengthen infection prevention and control measures.

Thiazolidinediones (TZDs), also known as glitazones, are a class of drugs used in the management of type 2 diabetes. They function as insulin sensitizers, improving the body's response to insulin, particularly in muscle, fat, and liver tissues. This helps to lower blood sugar levels.

Examples of TZDs include pioglitazone (Actos) and rosiglitazone (Avandia). While effective at controlling blood sugar, these medications have been associated with serious side effects such as an increased risk of heart failure, fractures, and bladder cancer. Therefore, their use is typically reserved for patients who cannot achieve good glucose control with other medications and who do not have a history of heart failure or bladder cancer.

It's important to note that the medical community continues to evaluate and re-evaluate the risks and benefits of thiazolidinediones, and their use may change based on new research findings. As always, patients should consult with their healthcare providers for personalized medical advice regarding their diabetes treatment plan.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Vitamin K3 is not typically referred to as a medical definition, but it is a form of Vitamin K. Medically, Vitamins K are coagulation factors that play a crucial role in blood clotting. Specifically, Vitamin K3 is known as Menadione and it is a synthetic version of Vitamin K. Unlike other forms of Vitamin K (K1 and K2), which are found naturally in foods like leafy green vegetables and fermented products, Vitamin K3 is not found in food and must be synthetically produced in a laboratory. It is used in some dietary supplements and animal feed additives. However, the use of Vitamin K3 in human nutrition is limited due to its potential toxicity, especially when given in large doses or to infants.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:

1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.

Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.

Carcinogens are agents (substances or mixtures of substances) that can cause cancer. They may be naturally occurring or man-made. Carcinogens can increase the risk of cancer by altering cellular DNA, disrupting cellular function, or promoting cell growth. Examples of carcinogens include certain chemicals found in tobacco smoke, asbestos, UV radiation from the sun, and some viruses.

It's important to note that not all exposures to carcinogens will result in cancer, and the risk typically depends on factors such as the level and duration of exposure, individual genetic susceptibility, and lifestyle choices. The International Agency for Research on Cancer (IARC) classifies carcinogens into different groups based on the strength of evidence linking them to cancer:

Group 1: Carcinogenic to humans
Group 2A: Probably carcinogenic to humans
Group 2B: Possibly carcinogenic to humans
Group 3: Not classifiable as to its carcinogenicity to humans
Group 4: Probably not carcinogenic to humans

This information is based on medical research and may be subject to change as new studies become available. Always consult a healthcare professional for medical advice.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Pyroglutamate hydrolase, also known as glutamine cyclotransferase or 5-oxoprolinase, is an enzyme involved in the metabolism of certain amino acids. Specifically, it catalyzes the hydrolysis of pyroglutamate (also called 5-oxoproline) to form glutamate and water. Pyroglutamate is a cyclic derivative of glutamate that can be generated through various metabolic pathways, including the breakdown of certain proteins or as an intermediate in the synthesis of some neurotransmitters.

The reaction catalyzed by pyroglutamate hydrolase is:

pyroglutamate + H2O → glutamate

This enzyme plays a critical role in maintaining the proper balance of amino acids and preventing the accumulation of potentially toxic metabolites. Deficiencies or mutations in pyroglutamate hydrolase can lead to various metabolic disorders, such as 5-oxoprolinuria, which is characterized by an excessive accumulation of pyroglutamate in the body and the excretion of large amounts of it in the urine.

Thioredoxin Reductase 1 (TXNRD1) is an enzyme that belongs to the thioredoxin reductase family. It is a homodimeric flavoprotein that contains a selenocysteine residue at its active site, which is essential for its catalytic activity.

The primary function of TXNRD1 is to reduce and regenerate the oxidized form of thioredoxin (TXN) by using NADPH as an electron donor. Thioredoxin is a small protein that plays a crucial role in maintaining the redox balance within the cell by regulating various cellular processes, such as DNA synthesis, gene expression, and apoptosis.

TXNRD1 is widely expressed in various tissues and is localized in the cytosol of the cell. It has been implicated in several physiological and pathological processes, including inflammation, oxidative stress, cancer, and neurodegenerative diseases. Inhibition of TXNRD1 has been shown to have potential therapeutic benefits in various disease models, making it an attractive target for drug development.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Leukotriene C4 (LTC4) is a type of lipid mediator called a cysteinyl leukotriene, which is derived from arachidonic acid through the 5-lipoxygenase pathway. It is primarily produced by activated mast cells and basophils, and to a lesser extent by eosinophils, during an allergic response or inflammation.

LTC4 plays a crucial role in the pathogenesis of asthma and other allergic diseases by causing bronchoconstriction, increased vascular permeability, mucus secretion, and recruitment of inflammatory cells to the site of inflammation. It exerts its effects by binding to cysteinyl leukotriene receptors (CysLT1 and CysLT2) found on various cell types, including airway smooth muscle cells, bronchial epithelial cells, and immune cells.

LTC4 is rapidly metabolized to Leukotriene D4 (LTD4) and then to Leukotriene E4 (LTE4) by enzymes such as gamma-glutamyl transpeptidase and dipeptidases, which are present in the extracellular space. These metabolites also have biological activity and contribute to the inflammatory response.

Inhibitors of 5-lipoxygenase or leukotriene receptor antagonists are used as therapeutic agents for the treatment of asthma, allergies, and other inflammatory conditions.

Thiocyanates are chemical compounds that contain the thiocyanate ion (SCN-), which consists of a sulfur atom, a carbon atom, and a nitrogen atom. The thiocyanate ion is formed by the removal of a hydrogen ion from thiocyanic acid (HSCN). Thiocyanates are used in various applications, including pharmaceuticals, agrochemicals, and industrial chemicals. In medicine, thiocyanates have been studied for their potential effects on the thyroid gland and their use as a treatment for cyanide poisoning. However, excessive exposure to thiocyanates can be harmful and may cause symptoms such as irritation of the eyes, skin, and respiratory tract, as well as potential impacts on thyroid function.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Genotype, in genetics, refers to the complete heritable genetic makeup of an individual organism, including all of its genes. It is the set of instructions contained in an organism's DNA for the development and function of that organism. The genotype is the basis for an individual's inherited traits, and it can be contrasted with an individual's phenotype, which refers to the observable physical or biochemical characteristics of an organism that result from the expression of its genes in combination with environmental influences.

It is important to note that an individual's genotype is not necessarily identical to their genetic sequence. Some genes have multiple forms called alleles, and an individual may inherit different alleles for a given gene from each parent. The combination of alleles that an individual inherits for a particular gene is known as their genotype for that gene.

Understanding an individual's genotype can provide important information about their susceptibility to certain diseases, their response to drugs and other treatments, and their risk of passing on inherited genetic disorders to their offspring.

Experimental liver neoplasms refer to abnormal growths or tumors in the liver that are intentionally created or manipulated in a laboratory setting for the purpose of studying their development, progression, and potential treatment options. These experimental models can be established using various methods such as chemical induction, genetic modification, or transplantation of cancerous cells or tissues. The goal of this research is to advance our understanding of liver cancer biology and develop novel therapies for liver neoplasms in humans. It's important to note that these experiments are conducted under strict ethical guidelines and regulations to minimize harm and ensure the humane treatment of animals involved in such studies.

Riboflavin deficiency, also known as ariboflavinosis, is a condition that results from inadequate intake or absorption of riboflavin (vitamin B2). This vitamin plays a crucial role in energy production, cellular function, growth, and development.

The medical definition of riboflavin deficiency includes the following symptoms:

1. Fatigue and weakness due to impaired energy production
2. Swelling and inflammation of the mouth and tongue, which can lead to painful lesions, soreness, and a smooth red tongue (glossitis)
3. Angular cheilosis - cracks at the corners of the mouth
4. Skin disorders such as seborrheic dermatitis, characterized by scaly, itchy, or greasy skin around the nose, eyebrows, ears, and genital area
5. Anemia due to impaired synthesis of heme (the iron-containing component of hemoglobin)
6. Impaired vision, particularly in low light conditions, due to damage to the light-sensitive cells in the eyes (photosensitivity)
7. Nerve damage and degeneration leading to neurological symptoms such as numbness, tingling, or burning sensations in the hands and feet
8. Slowed growth and development in children
9. Increased susceptibility to infections due to impaired immune function

Riboflavin deficiency is usually seen in individuals with poor nutrition, alcoholism, or those who have conditions affecting nutrient absorption, such as celiac disease or inflammatory bowel disease. Additionally, certain medications and pregnancy may increase the risk of riboflavin deficiency.

Cysteamine is a medication and a naturally occurring aminothiol compound, which is composed of the amino acid cysteine and a sulfhydryl group. It has various uses in medicine, including as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs and tissues. Cysteamine works by reacting with cystine to form a compound that can be more easily eliminated from the body. It is available in oral and topical forms and may also be used for other indications, such as treating lung diseases and radiation-induced damage.

Acrolein is an unsaturated aldehyde with the chemical formula CH2CHCHO. It is a colorless liquid that has a distinct unpleasant odor and is highly reactive. Acrolein is produced by the partial oxidation of certain organic compounds, such as glycerol and fatty acids, and it is also found in small amounts in some foods, such as coffee and bread.

Acrolein is a potent irritant to the eyes, nose, and throat, and exposure to high levels can cause coughing, wheezing, and shortness of breath. It has been shown to have toxic effects on the lungs, heart, and nervous system, and prolonged exposure has been linked to an increased risk of cancer.

In the medical field, acrolein is sometimes used as a laboratory reagent or as a preservative for biological specimens. However, due to its potential health hazards, it must be handled with care and appropriate safety precautions should be taken when working with this compound.

Thioctic acid is also known as alpha-lipoic acid. It is a vitamin-like chemical compound that is made naturally in the body and is found in small amounts in some foods like spinach, broccoli, and potatoes. Thioctic acid is an antioxidant that helps to protect cells from damage caused by free radicals. It also plays a role in energy production in the cells and has been studied for its potential benefits in the treatment of diabetes and nerve-related symptoms of diabetes such as pain, burning, itching, and numbness. Thioctic acid is available as a dietary supplement.

Medical Definition: Thioctic acid (also known as alpha-lipoic acid) is a vitamin-like antioxidant that is made naturally in the body and is found in small amounts in some foods. It plays a role in energy production in the cells, and has been studied for its potential benefits in the treatment of diabetes and nerve-related symptoms of diabetes such as pain, burning, itching, and numbness. Thioctic acid is also available as a dietary supplement.

Ethylmaleimide is a chemical compound that is commonly used in research and scientific studies. Its chemical formula is C7H10N2S. It is known to modify proteins by forming covalent bonds with them, which can alter their function or structure. This property makes it a useful tool in the study of protein function and interactions.

In a medical context, Ethylmaleimide is not used as a therapeutic agent due to its reactivity and potential toxicity. However, it has been used in research to investigate various physiological processes, including the regulation of ion channels and the modulation of enzyme activity. It is important to note that the use of Ethylmaleimide in medical research should be carried out with appropriate precautions and safety measures due to its potential hazards.

Paraquat is a highly toxic herbicide that is used for controlling weeds and grasses in agricultural settings. It is a non-selective contact weed killer, meaning it kills any green plant it comes into contact with. Paraquat is a fast-acting chemical that causes rapid desiccation of plant tissues upon contact.

In a medical context, paraquat is classified as a toxicological emergency and can cause severe poisoning in humans if ingested, inhaled, or comes into contact with the skin or eyes. Paraquat poisoning can lead to multiple organ failure, including the lungs, kidneys, and liver, and can be fatal in severe cases. There is no specific antidote for paraquat poisoning, and treatment typically focuses on supportive care and managing symptoms.

It's important to note that paraquat is highly regulated and its use is restricted to licensed professionals due to its high toxicity. Proper protective equipment, including gloves, goggles, and respiratory protection, should be used when handling paraquat to minimize the risk of exposure.

Selenium compounds refer to chemical substances that contain the metalloid element selenium (Se) in its various oxidation states, combined with other elements. These compounds can be organic or inorganic and can exist in different forms, such as selenides, selenites, and selenates. Selenium is an essential trace element for human health, playing a crucial role in several biological processes, including antioxidant defense, immune function, and thyroid hormone metabolism. However, excessive exposure to certain selenium compounds can be toxic and cause serious health effects.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Dehydroascorbic acid (DHAA) is the oxidized form of ascorbic acid, which is more commonly known as vitamin C. It is the oxidation product of ascorbic acid that is formed when the vitamin C molecule loses two electrons and two protons. This conversion can occur naturally in the body or during the processing and storage of food.

DHAA still retains some vitamin C activity, but it is not as biologically active as ascorbic acid. However, DHAA can be reduced back to ascorbic acid in the body by certain enzymes, which allows it to still contribute to maintaining proper levels of this essential nutrient.

DHAA plays a role in various physiological processes, including collagen synthesis, immune function, and antioxidant defense. It is also involved in the metabolism of amino acids, carbohydrates, and lipids. A deficiency in vitamin C can lead to scurvy, a condition characterized by fatigue, joint pain, anemia, and skin changes.

Metabolic Detoxification, Phase II, also known as conjugation, is the second step in the body's process of neutralizing and eliminating potentially harmful substances. During this phase, the liver cells add a molecule, such as glucuronic acid, sulfuric acid, glycine, or glutathione, to the substance, which has been previously modified during Phase I. This conjugation makes the substance water-soluble, allowing it to be excreted from the body through urine or bile.

In this process, various enzymes, such as UDP-glucuronosyltransferases (UGTs), sulfotransferases (SULTs), N-acetyltransferases (NATs), glutathione S-transferases (GSTs), and methyltransferases, play a crucial role in the transfer of these molecules to the substrate. Proper functioning of Phase II detoxification is essential for the effective elimination of drugs, environmental toxins, endogenous waste products, and other harmful substances from the body.

The amino acid transport system y+ is a type of sodium-independent cationic amino acid transporter that is responsible for the uptake of positively charged amino acids, such as arginine and lysine, into cells. It is a part of a larger family of amino acid transporters that are involved in the transport of various types of amino acids across cell membranes.

The y+ system is composed of several different transporter proteins, including rBAT/4F2hc heteromeric amino acid transporter (Cat1), and light chains such as y+LAT1, y+LAT2, and y+LAT3. These transporters are widely expressed in various tissues, including the small intestine, kidney, liver, and brain.

The y+ system plays important roles in various physiological processes, including protein synthesis, immune function, and neurotransmitter metabolism. Dysregulation of this transport system has been implicated in several diseases, such as cancer, neurological disorders, and kidney disease.

Sulfur is not typically referred to in the context of a medical definition, as it is an element found in nature and not a specific medical condition or concept. However, sulfur does have some relevance to certain medical topics:

* Sulfur is an essential element that is a component of several amino acids (the building blocks of proteins) and is necessary for the proper functioning of enzymes and other biological processes in the body.
* Sulfur-containing compounds, such as glutathione, play important roles in antioxidant defense and detoxification in the body.
* Some medications and supplements contain sulfur or sulfur-containing compounds, such as dimethyl sulfoxide (DMSO), which is used topically for pain relief and inflammation.
* Sulfur baths and other forms of sulfur-based therapies have been used historically in alternative medicine to treat various conditions, although their effectiveness is not well-established by scientific research.

It's important to note that while sulfur itself is not a medical term, it can be relevant to certain medical topics and should be discussed with a healthcare professional if you have any questions or concerns about its use in medications, supplements, or therapies.

Selenomethionine is an organic form of selenium, which is an essential trace element in human nutrition. It is incorporated into proteins in place of methionine, one of the 20 standard amino acids, and functions as an antioxidant by helping to prevent cellular damage from free radicals. Selenomethionine can be found in a variety of foods, including brazil nuts, fish, meat, and whole grains, and is also available as a dietary supplement.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

A lung is a pair of spongy, elastic organs in the chest that work together to enable breathing. They are responsible for taking in oxygen and expelling carbon dioxide through the process of respiration. The left lung has two lobes, while the right lung has three lobes. The lungs are protected by the ribcage and are covered by a double-layered membrane called the pleura. The trachea divides into two bronchi, which further divide into smaller bronchioles, leading to millions of tiny air sacs called alveoli, where the exchange of gases occurs.

Hydroquinones are a type of chemical compound that belong to the group of phenols. In a medical context, hydroquinones are often used as topical agents for skin lightening and the treatment of hyperpigmentation disorders such as melasma, age spots, and freckles. They work by inhibiting the enzyme tyrosinase, which is necessary for the production of melanin, the pigment that gives skin its color.

It's important to note that hydroquinones can have side effects, including skin irritation, redness, and contact dermatitis. Prolonged use or high concentrations may also cause ochronosis, a condition characterized by blue-black discoloration of the skin. Therefore, they should be used under the supervision of a healthcare provider and for limited periods of time.

Nitric oxide (NO) is a molecule made up of one nitrogen atom and one oxygen atom. In the body, it is a crucial signaling molecule involved in various physiological processes such as vasodilation, immune response, neurotransmission, and inhibition of platelet aggregation. It is produced naturally by the enzyme nitric oxide synthase (NOS) from the amino acid L-arginine. Inhaled nitric oxide is used medically to treat pulmonary hypertension in newborns and adults, as it helps to relax and widen blood vessels, improving oxygenation and blood flow.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Herbicides are a type of pesticide used to control or kill unwanted plants, also known as weeds. They work by interfering with the growth processes of the plant, such as inhibiting photosynthesis, disrupting cell division, or preventing the plant from producing certain essential proteins.

Herbicides can be classified based on their mode of action, chemical composition, and the timing of their application. Some herbicides are selective, meaning they target specific types of weeds while leaving crops unharmed, while others are non-selective and will kill any plant they come into contact with.

It's important to use herbicides responsibly and according to the manufacturer's instructions, as they can have negative impacts on the environment and human health if not used properly.

Dithionitrobenzoic acid is not a medical term, as it is related to chemistry rather than medicine. It is an organic compound with the formula C6H4N2O4S2. This compound is a type of benzenediol that contains two sulfur atoms and two nitro groups. It is a white crystalline powder that is soluble in water and alcohol.

Dithionitrobenzoic acid is not used directly in medical applications, but it can be used as a reagent in chemical reactions that are relevant to medical research or analysis. For example, it can be used to determine the concentration of iron in biological samples through a reaction that produces a colored complex. However, if you have any specific questions related to its use or application in a medical context, I would recommend consulting with a medical professional or a researcher in the relevant field.

Chloranil is the common name for 2,3,5,6-tetrachloro-1,4-benzoquinone, which is an organic compound with the formula C6Cl4O2. It is a light yellow to orange crystalline powder that is slightly soluble in water and more soluble in organic solvents.

Chloranil is used as a chemical intermediate in the synthesis of other organic compounds, including dyes and pigments. It is also used as a catalyst in some chemical reactions and has been studied for its potential use as a bactericide or fungicide.

Like many other halogenated aromatic compounds, chloranil can be harmful if swallowed, inhaled, or contacted on the skin. It can cause irritation to the eyes, skin, and respiratory tract, and prolonged exposure may lead to more serious health effects. Therefore, it is important to handle chloranil with care and follow appropriate safety precautions when working with this compound.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Oxygen is a colorless, odorless, tasteless gas that constitutes about 21% of the earth's atmosphere. It is a crucial element for human and most living organisms as it is vital for respiration. Inhaled oxygen enters the lungs and binds to hemoglobin in red blood cells, which carries it to tissues throughout the body where it is used to convert nutrients into energy and carbon dioxide, a waste product that is exhaled.

Medically, supplemental oxygen therapy may be provided to patients with conditions such as chronic obstructive pulmonary disease (COPD), pneumonia, heart failure, or other medical conditions that impair the body's ability to extract sufficient oxygen from the air. Oxygen can be administered through various devices, including nasal cannulas, face masks, and ventilators.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

In the context of medicine and toxicology, protective agents are substances that provide protection against harmful or damaging effects of other substances. They can work in several ways, such as:

1. Binding to toxic substances: Protective agents can bind to toxic substances, rendering them inactive or less active, and preventing them from causing harm. For example, activated charcoal is sometimes used in the emergency treatment of certain types of poisoning because it can bind to certain toxins in the stomach and intestines and prevent their absorption into the body.
2. Increasing elimination: Protective agents can increase the elimination of toxic substances from the body, for example by promoting urinary or biliary excretion.
3. Reducing oxidative stress: Antioxidants are a type of protective agent that can reduce oxidative stress caused by free radicals and reactive oxygen species (ROS). These agents can protect cells and tissues from damage caused by oxidation.
4. Supporting organ function: Protective agents can support the function of organs that have been damaged by toxic substances, for example by improving blood flow or reducing inflammation.

Examples of protective agents include chelating agents, antidotes, free radical scavengers, and anti-inflammatory drugs.

Carmustine is a chemotherapy drug used to treat various types of cancer, including brain tumors, multiple myeloma, and Hodgkin's lymphoma. It belongs to a class of drugs called alkylating agents, which work by damaging the DNA in cancer cells, preventing them from dividing and growing.

Carmustine is available as an injectable solution that is administered intravenously (into a vein) or as implantable wafers that are placed directly into the brain during surgery. The drug can cause side effects such as nausea, vomiting, hair loss, and low blood cell counts, among others. It may also increase the risk of certain infections and bleeding complications.

As with all chemotherapy drugs, carmustine can have serious and potentially life-threatening side effects, and it should only be administered under the close supervision of a qualified healthcare professional. Patients receiving carmustine treatment should be closely monitored for signs of toxicity and other adverse reactions.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Bile is a digestive fluid that is produced by the liver and stored in the gallbladder. It plays an essential role in the digestion and absorption of fats and fat-soluble vitamins in the small intestine. Bile consists of bile salts, bilirubin, cholesterol, phospholipids, electrolytes, and water.

Bile salts are amphipathic molecules that help to emulsify fats into smaller droplets, increasing their surface area and allowing for more efficient digestion by enzymes such as lipase. Bilirubin is a breakdown product of hemoglobin from red blood cells and gives bile its characteristic greenish-brown color.

Bile is released into the small intestine in response to food, particularly fats, entering the digestive tract. It helps to break down large fat molecules into smaller ones that can be absorbed through the walls of the intestines and transported to other parts of the body for energy or storage.

Phenobarbital is a barbiturate medication that is primarily used for the treatment of seizures and convulsions. It works by suppressing the abnormal electrical activity in the brain that leads to seizures. In addition to its anticonvulsant properties, phenobarbital also has sedative and hypnotic effects, which can be useful for treating anxiety, insomnia, and agitation.

Phenobarbital is available in various forms, including tablets, capsules, and elixirs, and it is typically taken orally. The medication works by binding to specific receptors in the brain called gamma-aminobutyric acid (GABA) receptors, which help to regulate nerve impulses in the brain. By increasing the activity of GABA, phenobarbital can help to reduce excessive neural activity and prevent seizures.

While phenobarbital is an effective medication for treating seizures and other conditions, it can also be habit-forming and carries a risk of dependence and addiction. Long-term use of the medication can lead to tolerance, meaning that higher doses may be needed to achieve the same effects. Abruptly stopping the medication can also lead to withdrawal symptoms, such as anxiety, restlessness, and seizures.

Like all medications, phenobarbital can have side effects, including dizziness, drowsiness, and impaired coordination. It can also interact with other medications, such as certain antidepressants and sedatives, so it is important to inform your healthcare provider of all medications you are taking before starting phenobarbital.

In summary, phenobarbital is a barbiturate medication used primarily for the treatment of seizures and convulsions. It works by binding to GABA receptors in the brain and increasing their activity, which helps to reduce excessive neural activity and prevent seizures. While phenobarbital can be effective, it carries a risk of dependence and addiction and can have side effects and drug interactions.

Hepatocytes are the predominant type of cells in the liver, accounting for about 80% of its cytoplasmic mass. They play a key role in protein synthesis, protein storage, transformation of carbohydrates, synthesis of cholesterol, bile salts and phospholipids, detoxification, modification, and excretion of exogenous and endogenous substances, initiation of formation and secretion of bile, and enzyme production. Hepatocytes are essential for the maintenance of homeostasis in the body.

... exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within ... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ... Glutathione enhances the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione ... In plants, glutathione is involved in stress management. It is a component of the glutathione-ascorbate cycle, a system that ...
... (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the ... For instance, glutathione peroxidases catalyze the oxidation of GSH to glutathione disulfide (GSSG) by reducing free radicals ... Glutathione synthetase deficiency Glutathione Liver Sulfur Metabolism Gogos A, Shapiro L (Dec 2002). "Large conformational ... such as H2O2 or Glutathione S-transferases in the detoxification of xenobiotics. Glutathione synthetase is important for a ...
It is also called citryl-glutathione thioesterhydrolase. Kielley WW, Bradley LB (1954). "Glutathione thiolesterase". J. Biol. ... The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction S-acylglutathione + H2O ⇌ {\displaystyle \ ... rightleftharpoons } glutathione + a carboxylate This enzyme belongs to the family of hydrolases, specifically those acting on ...
... (GSSG) is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is ... Glutathione-ascorbate cycle Antioxidant Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711-60 ... This reaction is catalyzed by the enzyme glutathione reductase. Antioxidant enzymes, such as glutathione peroxidases and ... GSSG, along with glutathione and S-nitrosoglutathione (GSNO), have been found to bind to the glutamate recognition site of the ...
Glutathione+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.19). ... Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the ... "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24 ... a key enzyme in glutathione metabolism, and its reaction intermediate". Proceedings of the National Academy of Sciences of the ...
... was discovered in 1957 by Gordon C. Mills. Activity of glutathione peroxidase is measured ... Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially ... Zakowski JJ, Tappel AL (September 1978). "A semiautomated system for measurement of glutathione in the assay of glutathione ... RSeH Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS-SG + NADPH + H+ → 2 GSH + NADP+. ...
... (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione ( ... In plants, reduced glutathione participates in the glutathione-ascorbate cycle in which reduced glutathione reduces ... Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the ... In particular, glutathione reductase appears to be a good target for anti-malarials, as the glutathione reductase of the ...
In enzymology, a glutathione oxidase (EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction 2 glutathione + O2 ⇌ {\ ... The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione ... displaystyle \rightleftharpoons } glutathione disulfide + H2O2 Thus, the two substrates of this enzyme are glutathione and O2, ... Kusakabe H, Kuninaka A, Yoshino H (1982). "Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp ...
"Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also to glutathione-S-transferase deficiency". ... Glutathione synthetase deficiency can be classified into three types: mild, moderate and severe. Mild glutathione synthetase ... Glutathione helps prevent damage to cells by neutralizing harmful molecules generated during energy production. Glutathione ... This cycle is necessary for producing a molecule called glutathione. Glutathione protects cells from damage caused by unstable ...
Since glutathione, ascorbate and NADPH are present in high concentrations in plant cells it is assumed that the glutathione- ... yielding oxidized glutathione (GSSG). Finally GSSG is reduced by glutathione reductase (GR) using NADPH as the electron donor. ... such as glutathione S-transferase omega 1 or glutaredoxins. In plants, the glutathione-ascorbate cycle operates in the cytosol ... Thus ascorbate and glutathione are not consumed; the net electron flow is from NADPH to H2O2. The reduction of dehydroascorbate ...
In enzymology, a glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase. Other ... the two substrates of this enzyme are glutathione and [Glu(-Cys)]n-Gly, whereas its two products are Gly and [Glu(-Cys)]n+1-Gly ... are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)". Proc ...
NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione ... In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction CoA + glutathione + ... glutathione, and NADP+, whereas its 3 products are CoA-glutathione, NADPH, and H+. This enzyme belongs to the family of ... The systematic name of this enzyme class is glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include ...
... (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This ... glutathione amide disulfide + NADH + H+ Glutathione amide reductase is a dimeric flavoprotein (FAD). Vergauwen B, Pauwels F, ... Glutathione+amide+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.8.1) ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ...
This enzyme participates in methionine metabolism and glutathione metabolism. Racker E (December 1955). "Glutathione- ... glutathione disulfide + 2 homocysteine Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two ... In enzymology, a glutathione-homocystine transhydrogenase (EC 1.8.4.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. ...
... glutathione disulfide + ascorbate Thus, the two substrates of this enzyme are glutathione and dehydroascorbate, whereas its two ... In enzymology, a glutathione dehydrogenase (ascorbate) (EC 1.8.5.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:dehydroascorbate oxidoreductase. Other names in common use include ... Crook EM (March 1941). "The system dehydroascorbic acid-glutathione". The Biochemical Journal. 35 (3): 226-36. doi:10.1042/ ...
Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions ... Glutathione transferases play a key role in catalyzing such reactions. Bacterial glutathione transferases of all classes are ... A GST monomer binds a glutathione molecule to its N-terminal glutathione-binding site. On the adjacent hydrophobic alpha- ... After completion of this reaction, glutathione reductase recycles oxidized glutathione back to the reduced form so that it ...
Affinity chromatography Bacterial glutathione transferase Glutathione S-transferase Mu 1 Glutathione S-transferase, C-terminal ... Overview of Glutathione S-Transferases Glutathione+S-Transferase at the U.S. National Library of Medicine Medical Subject ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles ... "Glutathione S-transferase pull-down assays using dehydrated immobilized glutathione resin". Analytical Biochemistry. 322 (2): ...
... glutathione disulfide + 2 cysteine Thus, the two substrates of this enzyme are glutathione and cystine, whereas its two ... In enzymology, a glutathione-cystine transhydrogenase (EC 1.8.4.4) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine ... This enzyme participates in cysteine metabolism and glutathione metabolism. Nagai S, Black S (1968). "A thiol-disulfide ...
... (EC 1.11.1.17) is an enzyme with systematic name glutathione amide:hydrogen-peroxide ... Glutathione+amide-dependent+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ... This enzyme catalyses the following chemical reaction 2 glutathione amide + H2O2 ⇌ {\displaystyle \rightleftharpoons } ...
... glutathione-coenzyme A glutathione disulfide transhydrogenase, glutathione coenzyme A-glutathione transhydrogenase, glutathione ... CoA-glutathione + glutathione Thus, the two substrates of this enzyme are CoA and glutathione disulfide, whereas its two ... a glutathione-CoA-glutathione transhydrogenase (EC 1.8.4.3) is an enzyme that catalyzes the chemical reaction CoA + glutathione ... coenzyme A-glutathione transhydrogenase, coenzyme A:oxidized-glutathione oxidoreductase, and coenzyme A:glutathione-disulfide ...
... hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). This enzyme participates in glutathione metabolism. ... glutathione disulfide + lipid + 2 H2O Thus, the two substrates of this enzyme are glutathione and lipid hydroperoxide, whereas ... glutathione, (phospholipid hydroperoxide-reducing), phospholipid hydroperoxide glutathione peroxidase, ... In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical ...
... is an enzyme that in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTA1 glutathione S-transferase A1". Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA ... This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped ... 1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate ...
... glutathione disulfide + protein-dithiol Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas ... glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein- ... This enzyme participates in glutathione metabolism. As of late 2007, only one structure has been solved for this class of ... In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction 2 ...
The systematic name of this enzyme class is S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming). Other names ... The enzyme S-(hydroxymethyl)glutathione synthase (EC 4.4.1.22) catalyzes the reaction S-(hydroxymethyl)glutathione ⇌ {\ ... Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA (February 2002). "A glutathione-dependent formaldehyde- ... in common use include glutathione-dependent formaldehyde-activating enzyme, Gfa, and S-(hydroxymethyl)glutathione formaldehyde- ...
... and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione. This enzyme belongs to the family of ... glutathione disulfide ⇌ {\displaystyle \rightleftharpoons } adenylyl sulfate + 2 glutathione The 3 substrates of this enzyme ... Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction AMP + sulfite + ... The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate- ...
... glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent ... In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction S ... The systematic name of this enzyme class is S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include ... Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF (2000). "Kinetic mechanism of human glutathione-dependent ...
2 glutathione Thus, the two substrates of this enzyme are xanthine dehydrogenase and glutathione disulfide, whereas its two ... oxidized-glutathione), glutathione-dependent thiol:disulfide oxidoreductase, and thiol:disulfide oxidoreductase. This enzyme ... In enzymology, an enzyme-thiol transhydrogenase (glutathione-disulfide) (EC 1.8.4.7) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase. Other names in ...
... (gene name GSTM1) is a human glutathione S-transferase. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTM1 glutathione S-transferase M1". Engel LS, Taioli E, Pfeiffer R, Garcia-Closas M, Marcus PM, Lan Q, et al. ( ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 v t ... This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in ...
... is an enzyme that in humans is encoded by the MGST1 gene. The MAPEG family (Membrane- ... Cholon A, Giaccia AJ, Lewis AD (1992). "What role do glutathione S-transferases play in the cellular response to ionizing ... DeJong JL, Mohandas T, Tu CP (1990). "The gene for the microsomal glutathione S-transferase is on human chromosome 12". ... This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid ...
... is a structural domain of glutathione S-transferase (GST). GST conjugates reduced ... GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol. Glutathione S- ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles ... The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed ...
Glutathione exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within ... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ... Glutathione enhances the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione ... In plants, glutathione is involved in stress management. It is a component of the glutathione-ascorbate cycle, a system that ...
... shown that certain GST isozymes can regulate mitogen-activated protein kinases or can facilitate the addition of glutathione to ... The super family of glutathione S-transferases (GSTs) is composed of multiple isozymes with significant evidence of functional ... Glutathione S-transferase polymorphisms: cancer incidence and therapy. *C C McIlwain1, ... Glutathione S-transferase Mu 2 inhibits hepatic steatosis via ASK1 suppression *Yi Jin ...
... is a rare inborn error of glutathione metabolism characterized by severe metabolic acidosis, hemolytic anemia, and neurological ... Glutathione synthetase (GS) deficiency, first described in 1970, is a rare autosomal-recessive inborn error of glutathione ... encoded search term (Glutathione Synthetase Deficiency) and Glutathione Synthetase Deficiency What to Read Next on Medscape ... Multiple mutations that cause glutathione synthetase deficiency have been described in the glutathione synthetase gene, GSS. ...
GlutamicGlutathioneGovt,Heart,Humans,IonLine,Magnesium,Mice,Microscopy,MuscleMutation,Non-U.S.P.H.S.,PointProteinProteins, ... GlutamicGlutathioneGovt,Heart,Humans,InhibitoryIonIsoforms,Kinetics,Line,MagnesiumMagnesium,Mice,Microscopy,Molecular,Muscle ... GlutathioneGovt,Histamine,Humans,HydrostaticInInositolIsoforms,Line,Mammals,Mechanical,MembraneMuscle,MyocardialMyocardium, ...
glutathione peroxidase 1. Names. GSHPx-1. cellular glutathione peroxidase. selenoprotein GPX1. NP_000572.2. *EC 1.11.1.9 ... GPX1 glutathione peroxidase 1 [Homo sapiens] GPX1 glutathione peroxidase 1 [Homo sapiens]. Gene ID:2876 ... glutathione peroxidase 1provided by HGNC. Primary source. HGNC:HGNC:4553 See related. Ensembl:ENSG00000233276 MIM:138320; ... involved_in glutathione metabolic process IBA Inferred from Biological aspect of Ancestor. more info ...
OZ Glutathione - Carrie April 11, 2013, 6:34 pm *Re: Dr. OZ Glutathione - Hope April 16, 2013, 8:57 pm *CF - Carrie March 5, ... New website about glutathione in cystic fibrosis - Lucy October 18, 2012, 8:13 pm *Re: New website about glutathione in cystic ... Blood test for glutathione level - received results - Denise October 31, 2014, 11:42 am *Re: Blood test for glutathione level ... Cystic Fibrosis and Glutathione. [ Post a Message , Cystic Fibrosis and Glutathione Stories ]. CYSTIC FIBROSIS (CF) AND ...
Do glutathione supplements help with aging or other conditions such as cancer and diabetes? ... Tests have shown that some glutathione supplements contain little glutathione, less glutathione than listed, and/or are ... and whether S-acetyl-glutathione (SAG) is any better than regular glutathione at raising glutathione levels, sign in as a ... Levels of glutathione in the brain appear to be lower in people with Alzheimers disease, but it is unknown if glutathione ...
OZ Glutathione - Carrie April 11, 2013, 6:34 pm *Re: Dr. OZ Glutathione - Hope April 16, 2013, 8:57 pm *CF - Carrie March 5, ... New website about glutathione in cystic fibrosis - Lucy October 18, 2012, 8:13 pm *Re: New website about glutathione in cystic ... Blood test for glutathione level - received results - Denise October 31, 2014, 11:42 am *Re: Blood test for glutathione level ... Cystic Fibrosis and Glutathione. [ Post a Message , Cystic Fibrosis and Glutathione Stories ]. CYSTIC FIBROSIS (CF) AND ...
Rhieu, S. , Urbas, A. , Bearden, D. , Marino, J. , Reipa, V. and Lippa, K. (2014), Probing the intracellular glutathione redox ... Here we describe an in-cell nuclear magnetic resonance (NMR)-based method for measuring the intracellular glutathione redox ... Using this approach, perturbations in the cellular glutathione redox homeostasis were also monitored as yeast cells were ... potential by direct and quantitative measurement of isotopically labeled glutathione introduced exogenously into living yeast. ...
... membrane associated proteins in eicosanoid and glutathione metabolism), defined according to enzymatic activities, sequence ... Microsomal glutathione transferase 1 (MGST1) is a member of the MAPEG family ( ... Microsomal glutathione transferase 1 in cancer and the regulation of ferroptosis Adv Cancer Res. 2023:160:107-132. doi: 10.1016 ... MGST1 has both glutathione transferase and peroxidase activities. Each is based on stabilizing the GSH thiolate in the same ...
Glutathione is a small molecule found in almost every cell. It cannot enter most cells directly and therefore must be made ... Glutathione. Glutathione is a small molecule found in almost every cell. It cannot enter most cells directly and therefore must ... the necessity for glutathione becomes increasingly evident. Glutathione values decline with age and higher values in older ... Fourthly, glutathione is required in many of the intricate steps needed to carry out an immune response. For example, it is ...
Protein target information for Glutathione peroxidase (pig). Find diseases associated with this biological target and compounds ...
Glutathione can be taken as a pill or powder. It can also be inhaled through the nose as a nasal spray. It can also be injected ... Glutathione is a protein in the body that mainly works in the liver. It has been used as an antioxidant to slow damage to cells ... It is likely safe to take glutathione in small doses for a short time. Not enough studies have been done to say whether it is ... Eight weeks of resistance training in conjugation with glutathione and L-Citrulline supplementation increases lean mass and has ...
Shop for Glutathione online with Swanson Health Products, where unparalleled quality meets unbeatable prices. ...
Crystal structure of glutathione transferase F7 from Populus trichocarpa ... Glutathione S-transferase family protein. A, B. 216. Populus trichocarpa. Mutation(s): 0 Gene Names: POPTR_0002s20900g, POPTR_ ... GLUTATHIONE. C10 H17 N3 O6 S. RWSXRVCMGQZWBV-WDSKDSINSA-N. Ligand Interaction. ... The glutathione transferase (GST) gene family is divided into 14 classes in photosynthetic organisms. Among them, the Phi class ...
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Glutathione is an endogenously produced compound that protects the body against the bombardment of free radicals. Free radicals ... have lower levels of glutathione and elevated levels of glutathione disulphide. Elevated levels of glutathione disulfide are ... Glutathione disulphide, the oxidized form of glutathione that has already reacted with a free radical, is also present in the ... Elevated levels of glutathione disulphide are an indication of a large utilization of glutathione and are often observed in ...
A Liposomal Complex Glutathione (GSH) is a short string of amino acids called a peptide. It is composed of three amino acids: ... Lipoceutical Glutathione is a liposomal glutathione supplement in liquid form. Glutathione. is not well absorbed when taken by ... In LipoCeutical Glutathione, the glutathione. is contained in tiny nanosize. spheres called liposomes. Liposomes. are tiny ... The glutathione does have an unpleasant smell so just dont sniff it as you drink it. I was disappointed to learn the vitamin B ...
Re: Updated Notice to Registrants - Glutathione On October 30, 2020, the College issued a communication to all Registrants that ... Registrants were advised on November 4, 2020 to cease using any IV L-Glutathione received from Galena Pharmacy, regardless of ... Therefore, registrants are advised to cease using any IV L-Glutathione from any source until further notice. ... In this case, it is believed that the L-Glutathione was from a different source. ...
The global glutathione resin market size was valued at USD 407.60 million in 2020 and is expected to grow at a compound annual ... 5 Glutathione Resin market Snapshot. Fig. 6 Glutathione Resin Segmental Outlook. Fig. 7 Glutathione Resin market volume and ... Glutathione Resin Market Size & Share Report, 2021-2028 Glutathione Resin Market Size, Share & Trends Analysis Report By ... Chapter 5 Glutathione Resin Market: Regional Estimates & Trend Analysis. 5.1 Glutathione Resin regional movement analysis & ...
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In short, glutathione has shown benefit among cystic fibrosis and AIDS patients who have decreased glutathione in the intestine ... Glutathione has also been studied in cystic fibrosis patients. Decreased glutathione in their intestines can lead to ... Mice unable to form glutathione will die before birth. Mice that have been genetically altered to not produce glutathione in ... People with AIDS have reduced production of glutathione in the intestine, and supplementation with glutathione could help in ...
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Abundant biochemical data support a direct causal link between low glutathione (GSH), impaired defenses and cellular ... ATLANTAAbundant biochemical data support a direct causal link between low glutathione (GSH), impaired defenses and cellular ...
... ... GLUTATHIONE S-TRANSFERASE1-Menaphthyl Glutathione ConjugateSulfate Ion ...
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... glutathione is found in every tissue and fluid throughout the body-and has a number of key health benefits.* ... What is glutathione - and what does it do in the body?. Glutathione is an antioxidant thats made up of the three amino acids- ... Sources of glutathione.. There are two primary ways to make sure youre getting enough glutathione, and theyre complementary. ... In these cases, incorporating a glutathione supplement (or a targeted multi-ingredient supplement that optimizes glutathiones ...
  • Although glutathione plays an important role in the body as an antioxidant, supplementing with glutathione has not been shown to slow aging or benefit most people with conditions associated with reduced levels of glutathione, such as cancer, cataracts, HIV infection, and diabetes (although there may be a modest benefit among older people with type 2 diabetes). (consumerlab.com)
  • Levels of glutathione in the brain appear to be lower in people with Alzheimer's disease, but it is unknown if glutathione supplements are beneficial. (consumerlab.com)
  • The liver and kidneys contain high levels of glutathione as they have the greatest exposure to toxins. (life-enthusiast.com)
  • Research has observed lower levels of glutathione in adults over 45 years old, in comparison to younger people. (preparedfoods.com)
  • Elevated levels of glutathione disulphide are an indication of a large utilization of glutathione and are often observed in individuals over the age of 45. (preparedfoods.com)
  • People that are under oxidative stress, such as smokers, alcoholics and diabetics, have lower levels of glutathione and elevated levels of glutathione disulphide. (preparedfoods.com)
  • Elevated levels of glutathione disulfide are associated with increased carotid intima media thickness, a measurement of the thickness of artery walls and an indication of cardiovascular disease risk. (preparedfoods.com)
  • There is debate about whether oral glutathione supplements actually raise blood and tissue levels of glutathione. (allstarhealth.com)
  • In animal models, levels of glutathione remain constant in females who have suffered a brain injury, but drop by as much as 80 percent in males with the same injury. (ambafrance-do.org)
  • However, intravenous glutathione therapy and glutathione precursors or dietary supplements are effective in boosting intracellular levels of glutathione. (ambafrance-do.org)
  • ABSTRACT Serum levels of glutathione reductase (GR), glutathione S-transferase- (GST-) and malondialdehyde (MDA) were determined to evaluate their use in diagnosing hepatocellular damage in 75 children with liver disease. (who.int)
  • Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, peroxides, lipid peroxides, and heavy metals. (wikipedia.org)
  • Glutathione is involved in several important biologic functions, including membrane transport, detoxification of xenobiotics, and protection of cells from free radicals. (medscape.com)
  • Firstly , glutathione is the major antioxidant produced by the cell, protecting it from free radicals (oxygen radicals, oxyradicals). (life-enthusiast.com)
  • March 2011 -Glutathione is an endogenously produced compound that protects the body against the bombardment of free radicals. (preparedfoods.com)
  • Now Foods Glutathione contains 500mg of Glutathione along with Milk Thistle and Alpha Lipoic Acid to help strengthen immune system function and to fight free radicals. (bestpricenutrition.com)
  • Glutathione is responsible for disarming free radicals, recycling other antioxidants, and encouraging cell turnover and collagen production. (skininc.com)
  • Glutathione is an antioxidant produced throughout the body that plays many important roles, including neutralizing unstable oxygen molecules called free radicals , which cause damage to DNA and cells if left unchecked. (fightaging.org)
  • According to functional medicine doctor and mbg Collective member Mark Hyman, M.D., the sticky, flypaper-like nature of the sulfur in glutathione is what allows it to essentially grab on to free radicals and toxins (like mercury and other heavy metals) in order to usher them out of the body. (mindbodygreen.com)
  • No surprise here considering all that talk earlier about glutathione being like flypaper for free radicals and toxins, right? (mindbodygreen.com)
  • Glutathione biosynthesis involves two adenosine triphosphate-dependent steps: First, γ-glutamylcysteine is synthesized from L-glutamate and cysteine. (wikipedia.org)
  • In addition to the well-characterized catalytic activity, recent evidence has shown that certain GST isozymes can regulate mitogen-activated protein kinases or can facilitate the addition of glutathione to cysteine residues in target proteins ( S -glutathionylation). (nature.com)
  • Glutathione is produced from the amino acids cysteine, glycine, and glutamine via the consecutive actions of gamma-glutamylcysteine synthetase and glutathione synthetase. (medscape.com)
  • The rate at which glutathione can be made depends on the availability of cysteine, which is relatively scarce in foodstuffs. (life-enthusiast.com)
  • Owing to the presence of a cysteine with a pK a value around 5 in their active site, GSTF3, F7, and F8 displayed a thiol transferase activity in addition to the usual glutathione transferase and peroxidase activities. (rcsb.org)
  • Glutathione is an antioxidant produced in the body through enzymatic reactions, using the amino acids cysteine, L-glutamic acid and glycine. (uclahealth.org)
  • Some nutritionists recommend increasing the intake of the amino acids cysteine and glutamate, which make glutathione, but this hasn't been studied either. (uclahealth.org)
  • Glutathione is a peptide molecule comprised of the amino acids glycine, glutamic acid and cysteine. (bestpricenutrition.com)
  • Now Foods Glutathione 250mg 60 Capsules Glutathione is made from the amino acids glycine, cysteine and glutamic acid and is produced by the liver. (bestpricenutrition.com)
  • Reduced glutathione supplements such as NOW Foods' Glutathione have only become available recently, and are welcome additions to the short list of legitimate liver-support substances such as milk thistle extracts, n-acetyl-cysteine and alpha lipoic acid. (allstarhealth.com)
  • Glutathione is an antioxidant that's made up of the three amino acids- glutamine, glycine, and cysteine 2 -all of which are rich in the mineral sulfur. (mindbodygreen.com)
  • N-acetyl-cysteine (NAC), a precursor of glutathione, already approved for use by the U.S. Food and Drug Administration to treat people who have overdosed on acetaminophen, may be an effective treatment for brain injury in boys whose brains are deprived of oxygen. (ambafrance-do.org)
  • Atkuri KR, Mantovani JJ, Herzenberg LA, Herzenberg LA. N-Acetylcysteine--a safe antidote for cysteine/glutathione deficiency. (medscape.com)
  • Clickable Glutathione-Based Identification of Cysteine Glutathionylation. (bvsalud.org)
  • According to one review, the oldest reported survivor with the severe form of glutathione synthetase deficiency was aged 24 years and had experienced significant neurological deterioration over the previous few years. (medscape.com)
  • Glutathione disulphide, the oxidized form of glutathione that has already reacted with a free radical, is also present in the body. (preparedfoods.com)
  • There is no debate, however, about the reduced form of glutathione being the most desirable form. (allstarhealth.com)
  • Glutathione is used to produce S-sulfanylglutathione, which is part of hydrogen sulfide metabolism. (wikipedia.org)
  • Glutathione facilitates metabolism of xenobiotics. (wikipedia.org)
  • Glutathione S-transferase enzymes catalyze its conjugation to lipophilic xenobiotics, facilitating their excretion or further metabolism. (wikipedia.org)
  • Glutathione synthetase (GS) deficiency, first described in 1970, is a rare autosomal-recessive inborn error of glutathione metabolism characterized by severe metabolic acidosis , hemolytic anemia, and neurological problems. (medscape.com)
  • Microsomal glutathione transferase 1 (MGST1) is a member of the MAPEG family (membrane associated proteins in eicosanoid and glutathione metabolism), defined according to enzymatic activities, sequence motifs, and structural properties. (nih.gov)
  • A number of enzymes in carbohydrate and lipid metabolism depend upon glutathione and other sulfhydryl compounds such as coenzyme A for their activity. (erowid.org)
  • abnormalities in glutathione metabolism and antioxidant defenses. (ambafrance-do.org)
  • Acrylonitrile (ACN), one of the top 50 chemicals produced in the world, is a very powerful pro-oxidant compound whose metabolism leads to a profound glutathione (GSH) depletion and to a production of cyanide (CN) which, in turn, can inhibit superoxide dismutase (SOD). (cdc.gov)
  • Glutathione is a small molecule found in almost every cell. (life-enthusiast.com)
  • This allows positioning of several active site residues at proximity of the glutathione molecule, which itself remains unchanged in GSTF three-dimensional structures. (rcsb.org)
  • Glutathione is a molecule that is present in every cell, where it works as a potent detoxifier and protector of cellular function. (skininc.com)
  • This type of glutathione uses sub-nanotechnology to deliver a highly absorbable form of reduced L-glutathione, which enables the glutathione molecule to absorb intact into the skin. (skininc.com)
  • The College has not received any information that oral glutathione has been affected. (cnpbc.bc.ca)
  • This condensation is catalyzed by glutathione synthetase. (wikipedia.org)
  • In mild glutathione synthetase deficiency, which is characterized by hemolytic anemia , enzyme deficiency primarily occurs in erythrocytes. (medscape.com)
  • Biochemical pathway of glutathione synthetase. (medscape.com)
  • Multiple mutations that cause glutathione synthetase deficiency have been described in the glutathione synthetase gene, GSS . (medscape.com)
  • Thirteen different missense mutations in GSS have been identified in individuals with severe glutathione synthetase deficiency. (medscape.com)
  • The frequency of glutathione synthetase deficiency is unknown. (medscape.com)
  • Glutathione synthetase deficiency is very rare. (medscape.com)
  • It is believed that some cases of glutathione synthetase deficiency may go undiagnosed or misdiagnosed, complicating a determination of its true frequency. (medscape.com)
  • Recently, authors have recommended that 3 forms of glutathione synthetase deficiency be identified: mild, moderate, and severe (see History). (medscape.com)
  • No race predilection is observed in glutathione synthetase deficiency. (medscape.com)
  • Most individuals with systemic glutathione synthetase deficiency are diagnosed in the newborn period. (medscape.com)
  • Available at https://rarediseases.org/rare-diseases/glutathione-synthetase-deficiency/ . (medscape.com)
  • Available at https://rarediseases.info.nih.gov/diseases/10047/glutathione-synthetase-deficiency . (medscape.com)
  • The biosynthesis pathway for GSH, consisting of γ-glutamylcysteine synthetase (γGCS) and glutathione synthetase (GS) is present in malaria parasites as well as in their host cells. (gla.ac.uk)
  • Diagnosis of glutathione synthetase deficiency in newborn screening. (medscape.com)
  • Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. (medscape.com)
  • The Recommended Dietary Allowance (RDA) for sulphur-containing amino acids (precursors to glutathione) is 1.1 g/day for women and 1.4 g/day for men, which is equivalent to 2.7 and 3.3g of glutathione/day. (preparedfoods.com)
  • Although most Americans consume an adequate supply of dietary precursors for GSH {glutathione} synthesis, there is a gap between the amount synthesized and the amount needed (i.e., a decline in GSH is associated with disease risk). (preparedfoods.com)
  • You might recall recent small human trials of high dose supplementation of glutathione precursors in order to achieve upregulation of glutathione, and corresponding studies in mice . (fightaging.org)
  • if any glutathione is broken down during digestion, it will be broken down into glutathione precursors, which can then be used to make more glutathione. (allstarhealth.com)
  • Glutathione (GSH) precursors can prevent death of brain cells induced by amyloid plaques in Alzhiemer's disease, while substances that deplete GSH increase cell death. (ambafrance-do.org)
  • The ratio of reduced glutathione to oxidized glutathione within cells is a measure of cellular oxidative stress where increased GSSG-to-GSH ratio is indicative of greater oxidative stress. (wikipedia.org)
  • 1/2 GSSG + RH Aside from deactivating radicals and reactive oxidants, glutathione participates in thiol protection and redox regulation of cellular thiol proteins under oxidative stress by protein S-glutathionylation, a redox-regulated post-translational thiol modification. (wikipedia.org)
  • Using this approach, perturbations in the cellular glutathione redox homeostasis were also monitored as yeast cells were subjected to oxidative stress. (nist.gov)
  • A major advancement in Glutathione supplementation, Results RNA® has developed Advanced Cellular Glutathione (ACG). (positivehealth.com)
  • Jarrow Formulas Reduced Glutathione 500mg 60 Caps Glutathione Reduced is an ubiquitous antioxidant involved in many cellular functions such as detoxification, amino acid transport, production of. (bestpricenutrition.com)
  • ATLANTAAbundant biochemical data support a direct causal link between low glutathione (GSH), impaired defenses and cellular susceptibility in model systems, according to a study published in Natural Journal Medicine (Feb. 1, 2011). (naturalproductsinsider.com)
  • Glutathione, a powerful antioxidant essential for the functioning of the immune system, also protects against environmental damage and helps repair skin cells at the cellular level. (skininc.com)
  • Glutathione is an interesting cellular antioxidant , as increased levels can improve health in humans and slow aging in animal models. (fightaging.org)
  • 1,4] Many factors can increase cellular exposure to oxidative insult, and therefore increase cellular consumption of nutrients - such as glutathione - that provide antioxidant activity. (prohealth.com)
  • Taking glutathione itself as a supplement does not boost cellular glutathione levels, since it breaks down in the digestive tract before it reaches the cells. (ambafrance-do.org)
  • Do glutathione supplements work to prevent aging or for other conditions? (consumerlab.com)
  • Tests have shown that some 'glutathione' supplements contain little glutathione, less glutathione than listed, and/or are contaminated with lead. (consumerlab.com)
  • What do glutathione supplements do? (uclahealth.org)
  • Ask the Doctors - What do glutathione supplements do? (uclahealth.org)
  • As a result, glutathione supplements have become increasingly popular as an over-the-counter approach to wellness. (fightaging.org)
  • Therefore I feel comfortable that it supplements the body's additional need for glutathione when it is under stress. (prohealth.com)
  • The general reaction involves formation of an unsymmetrical disulfide from the protectable protein (RSH) and GSH: RSH + GSH + [O] → GSSR + H2O Glutathione is also employed for the detoxification of methylglyoxal and formaldehyde, toxic metabolites produced under oxidative stress. (wikipedia.org)
  • As an antioxidant, Glutathione supports the livers detoxification process, and helps to support healthy ageing and vitality. (healthpost.co.nz)
  • Glutathione is important for a healthy immune system and is necessary for the bodies detoxification processes. (bestpricenutrition.com)
  • And a key factor in the liver's detoxification processes is the tripeptide glutathione . (allstarhealth.com)
  • Glutathione is so important because it forms the basis of a key antioxidant and detoxification enzyme, glutathione peroxidase. (allstarhealth.com)
  • So increasing glutathione production would be a great way to increase detoxification. (allstarhealth.com)
  • NOW's Glutathione is a reduced glutathione supplement and with NOW's reputation for purity and potency, this would be a good choice for anyone looking to support their liver's detoxification functions. (allstarhealth.com)
  • Glutathione is critical for healthy immune system function and is necessary for proper detoxification processes. (allstarhealth.com)
  • It's worth restating, though: According to Hyman, glutathione 5 is a critical and integral part of the body's intrinsic detoxification system. (mindbodygreen.com)
  • Also unsurprising given its role in detoxification: The highest concentrations of glutathione in the body are found in the liver and kidneys . (mindbodygreen.com)
  • L Glutathione is a potent antioxidant and plays an important role in the liver's detoxification pathways. (vitasprings.com)
  • The tripeptide glutathione (GSH) or γ-glutamylcysteinyl-glycine is the most abundant low molecular weight thiol in most eukaryotic organisms and serves a number of important functions as sulfhydryl-buffer, cofactor for enzymes and for the detoxification of xenobiotics and drugs. (gla.ac.uk)
  • Glutathione S-transferase (GST) is a search Centre (NRC), Cairo, Egypt from detoxification enzyme that catalyses the 2001 to 2004, in accordance with the ethical addition of glutathione to various xeno- principles of the NRC, in collaboration with biotics [ 4 ]. (who.int)
  • Additionally, items such as milk, blueberries, bottled apple juice and tea contain glutathione-reactive compounds that reduce the amount of glutathione present in food or lining of the small intestine. (preparedfoods.com)
  • Here, researchers find a mechanism that regulates the amount of glutathione that enters the mitochondria, and thus a possible target to increase this level without the need for global upregulation. (fightaging.org)
  • It also appeared to regulate the amount of glutathione. (fightaging.org)
  • 5 Human research has shown that glutathione from raw fruits and vegetables is associated with a reduced risk of oral cancer 6 and supplementation with glutathione can prevent nephrotoxicity associated with cancer treatment. (preparedfoods.com)
  • People with AIDS have reduced production of glutathione in the intestine, and supplementation with glutathione could help in the ability to digest food. (uclahealth.org)
  • A 2015 study published in the Journal of Pediatric Gastroenterology and Nutrition found that, for them, supplementation with glutathione three times per day with meals has been shown to decrease intestinal inflammation and improve growth in children. (uclahealth.org)
  • Research shows that the naturally occurring, master antioxidant glutathione is a critical component of longevity and good health. (skininc.com)
  • With a nickname like " the master antioxidant 1 ," glutathione is a one-of-a-kind bioactive that deserves your attention. (mindbodygreen.com)
  • Glutathione is the brain's master antioxidant and plays an important protective role in the brain. (ambafrance-do.org)
  • also known as PHGPx) is a monomeric, 21 kDa member of the glutathione peroxidase family of proteins. (rndsystems.com)
  • In this study, these data have been analyzed to find all human proteins containing (or predicted to contain) the cytosolic glutathione transferase (cGST) fold. (edu.au)
  • The only known archaea that make glutathione are halobacteria. (wikipedia.org)
  • Studies have found that the mood stabilizing drug, valproate, used to treat epilepsy and bi-polar disorder, regulates expression of the genes that make glutathione-S-transferase (GST). (ambafrance-do.org)
  • The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. (nih.gov)
  • Research has indicated that supplemental glutathione results in increased plasma glutathione levels in humans, despite an expected degradation that may occur in the intestine. (preparedfoods.com)
  • Acetyl-Glutathione 300 mg is a novel oral acetyl-glutathione formulation that is stable in the stomach and gastrointestinal tract, well absorbed, and able to enter the cells directly and present to the cytosol for mitochondrial entry. (allergyresearchgroup.com)
  • Acetyl-Glutathione 300 mg uses pure Emothion® glutathione as the starting material. (allergyresearchgroup.com)
  • Laboratory data showed that S-acetyl glutathione increased intracellular glutathione and had a positive effect on many oxidative stress biomarkers. (prohealth.com)
  • I'm in my gut healing journey and S Acetyl Glutathione is one of the must have to achieve my goal! (prohealth.com)
  • The oxido-reductase enzyme glutathione peroxidase 4 (GPX4) governs Salmonella Typhimurium-induced neutrophil transepithelial migration. (umassmed.edu)
  • Lipoceutical Glutathione is a liposomal glutathione supplement in liquid form. (brainchildnutritionals.com)
  • description':'Liposomal Glutathione is more bioavailable than other forms, making it a great choice for those looking for superior absorption. (healthpost.co.nz)
  • Liposomal Glutathione is a supplement that is encapsulated in a fatty layer (phospholipid) that is absorbed by our bodies very effectively because they are similar to our own cell membrane structure. (healthpost.co.nz)
  • we are so happy to be able to offer another potent antioxidant in the form of Liposomal Glutathione. (healthpost.co.nz)
  • When should I take a Liposomal Glutathione supplement? (healthpost.co.nz)
  • Due to its powerful antioxidant activity in the body, Liposomal Glutathione can support youth and vitality for healthy ageing. (healthpost.co.nz)
  • The tripeptide glutathione (l-y-glutamyl-l-cysteinyl-glycine, GSH) plays a pivotal role in metabolic and cell-cycle related functions in virtually all cells. (ersjournals.com)
  • Here we describe an in-cell nuclear magnetic resonance (NMR)-based method for measuring the intracellular glutathione redox potential by direct and quantitative measurement of isotopically labeled glutathione introduced exogenously into living yeast. (nist.gov)
  • People with mutations in the enzymes that form glutathione are more susceptible to oxidative stress. (uclahealth.org)
  • In addition, glutathione recycles other well-known antioxidants such as vitamin C and vitamin E, keeping them in their active state. (life-enthusiast.com)
  • This high-tech skin solution captures the three peptides found in Glutathione, one of the most powerful antioxidants, to transform the appearance of your skin to a youthful, supple touch. (suzannesomers.com)
  • The deficiency in the production of glutathione leads to break down of red blood cells, enlargement of the spleen, gall stones and after many years can lead to mental deterioration. (uclahealth.org)
  • Because you're presumably healthy, you're unlikely to have any deficiency in the production of glutathione. (uclahealth.org)
  • Increased oxidant burden and antioxidant, e.g. glutathione (GSH), deficiency in the lower respiratory tract have been thought to play a role in the progression of IPF. (ersjournals.com)
  • Prenatal diagnosis of glutathione synthase deficiency. (medscape.com)
  • This work led to the discovery of an undenatured whey protein concentrate that regulated glutathione levels and promoted immune enhancing and anti-carcinogenic activity. (life-enthusiast.com)
  • Glutathione is a protein in the body that mainly works in the liver. (epnet.com)
  • How glutathione actually enters mitochondria was unknown until 2021, when researchers discovered that a transporter protein called SLC25A39 delivers the package. (fightaging.org)
  • Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? (umassmed.edu)
  • It is a component of the glutathione-ascorbate cycle, a system that reduces poisonous hydrogen peroxide. (wikipedia.org)
  • An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. (umassmed.edu)
  • This conversion is catalyzed by glutathione reductase: NADPH + GSSG + H2O → 2 GSH + NADP+ + OH− GSH protects cells by neutralising (reducing) reactive oxygen species. (wikipedia.org)
  • Adenylyl-sulfate reductase, an enzyme of the sulfur assimilation pathway, uses glutathione as an electron donor. (wikipedia.org)
  • Comprised of 3 amino acids, glutathione is the body's main antioxidant and as part of a comprehensive skincare regimen can help to reduce the look of wrinkles and creases by replenishing fragile skin. (perriconemd.com)
  • Since it's one of the body's main detoxifiers, glutathione plays an important role in creating an overall smoother and brighter appearance for the skin. (skininc.com)
  • Above this message you will find a link for "Cystic Fibrosis and Glutathione Stories," where you can add longer accounts of your experiences with GSH. (boardhost.com)
  • Glutathione has also been studied in cystic fibrosis patients. (uclahealth.org)
  • In short, glutathione has shown benefit among cystic fibrosis and AIDS patients who have decreased glutathione in the intestine, and it may show benefit in inflammatory conditions of the intestine, such as ulcerative colitis and Crohn's disease, but this needs to be studied as well. (uclahealth.org)
  • The glutathione transferase (GST) gene family is divided into 14 classes in photosynthetic organisms. (rcsb.org)
  • Genetics researchers have found that the glutathione S-transferase gene controls the onset of Alzheimer's, Parkinson's disease and determines, not if we get these diseases, but when. (ambafrance-do.org)
  • The glutathione S-transferase gene has previously been linked to the risk for Parkinson's disease among people who used pesticides. (ambafrance-do.org)
  • Glutathione is the most abundant thiol in animal cells, ranging from 0.5 to 10 mmol/L. It is present in the cytosol and the organelles. (wikipedia.org)
  • It is thought that glutathione upregulation may largely improve health via mitochondrial function, as mitochondria are a prominent source of oxidative stress in aging cells. (fightaging.org)
  • Delivers Glutathione which is a very important and powerful antioxidant. (suzannesomers.com)
  • Glutathione is a powerful antioxidant that is produced naturally in the body, however there are times in life when the body may need more support. (healthpost.co.nz)
  • Glutathione conjugates to NAPQI, and the resulting ensemble is excreted. (wikipedia.org)
  • L-Glutathione binds and conjugates toxins, promoting their excretion. (vitasprings.com)
  • therefore, by limiting H2O2 accumulation, glutathione peroxidases are also involved in modulating these processes. (nih.gov)
  • Fourthly , glutathione is required in many of the intricate steps needed to carry out an immune response. (life-enthusiast.com)
  • Animal research with glutathione supplementation has indicated improvements in immune function, 2 protection against oxidant injury in newborn lungs, 3 reduction in the uptake of oxidized lipids 4 and protection against other toxic chemicals. (preparedfoods.com)
  • One Frontiers in Immunology study suggests that glutathione helps "fine-tune" our immune response 6 , helping the body to respond effectively when needed without kicking into unhelpful overdrive. (mindbodygreen.com)
  • In addition to this role in daily immune function, Hyman also suggests that ample glutathione is crucial for long-term immunity, as well. (mindbodygreen.com)
  • Glutathione also works to maintain the epithelial tissues (the lining found in organs like the intestines), which act as barriers between compounds ingested by the body and the bloodstream and are crucial for maintaining immune balance. (mindbodygreen.com)
  • Glutathione supports liver and kidney function, brightens skin, can help to reduce fatigue, and supports immune health. (veganessentials.com)
  • In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH), with the remainder in the disulfide form (GSSG). (wikipedia.org)
  • After 1 or 7 days, histopathology of selected organs was performed, and tissue reduced glutathione (GSH) levels were measured as an indicator of oxidative stress. (cdc.gov)
  • Secondly, glutathione is a very important detoxifying agent, enabling the body to get rid of undesirable toxins and pollutants. (life-enthusiast.com)
  • You can't do much about toxins in the environment but you can better protect yourself from any potential harm by using NOW Glutathione whenever you need or want liver support. (allstarhealth.com)
  • Toxins stick onto glutathione, which then carries them into bile and the stool to discard,"* he told mbg. (mindbodygreen.com)
  • Glutathione is naturally produced by the liver and works in that organ to combat toxins and turn them into bile ,"* explains Toronto-based dietitian Abby Langer, R.D. This pungent stuff then plays a role of its own: It's actually a must-have for the optimal digestion of fat, she explains. (mindbodygreen.com)
  • Glutathione Peroxidase 4/GPX4 " has 7 results in Products. (rndsystems.com)
  • The unusual gamma amide linkage in glutathione protects it from hydrolysis by peptidases. (wikipedia.org)
  • Glutathione donates electrons to oxidants to sequester, or squelch, their free radical activity, helping to prevent DNA damage and subsequent chronic disease. (preparedfoods.com)
  • Current in vitro studies were undertaken to probe the cytochrome P450 (P450)-mediated bioactivation of flutamide and identify the possible reactive species using reduced glutathione (GSH) as a trapping agent. (unboundmedicine.com)
  • NOW Glutathione is actually more thanjust gltathione, it's a complete liver support complex with alpha lipoic acid as well as the documented liver support herb milk thistle extract. (allstarhealth.com)
  • Among the many metabolic processes in which it participates, glutathione is required for the biosynthesis of leukotrienes and prostaglandins. (wikipedia.org)
  • Glutathione enhances the function of citrulline as part of the nitric oxide cycle. (wikipedia.org)
  • Dear Doctor: I've been seeing advertisements for glutathione, saying the supplement enhances the body's cells. (uclahealth.org)
  • LivOn Labs has developed this lypo-spheric glutathione supplement offers the purest and safest delivery of glutathione outside of intravenous methods. (veganessentials.com)
  • Glutathione exists in reduced (GSH) and oxidized (GSSG) states. (wikipedia.org)
  • Glutathione disulfide (GSSG) is thereby generated. (wikipedia.org)
  • however, a tentative bioactivation mechanism involving a P450-catalyzed abstraction of hydrogen atom from the amide nitrogen of flutamide and the subsequent trapping of the nitrogen-centered radical by GSH or oxidized glutathione (GSSG) was proposed. (unboundmedicine.com)