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.
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 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.
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.
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.
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.
An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.
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.
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.
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 GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
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).
A hemeprotein from leukocytes. Deficiency of this enzyme leads to a hereditary disorder coupled with disseminated moniliasis. It catalyzes the conversion of a donor and peroxide to an oxidized donor and water. EC 1.11.1.7.
Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.
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 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.
The dialdehyde of malonic acid.
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 hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC 1.11.1.5.
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.
Peroxidases that utilize ASCORBIC ACID as an electron donor to reduce HYDROGEN PEROXIDE to WATER. The reaction results in the production of monodehydroascorbic acid and DEHYDROASCORBIC ACID.
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.
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 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).
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.
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 hemeprotein that catalyzes the oxidation of the iodide radical to iodine with the subsequent iodination of many organic compounds, particularly proteins. EC 1.11.1.8.
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)
Diagnostic aid in pancreas function determination.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A 66-kDa peroxidase found in EOSINOPHIL granules. Eosinophil peroxidase is a cationic protein with a pI of 10.8 and is comprised of a heavy chain subunit and a light chain subunit. It possesses cytotoxic activity towards BACTERIA and other organisms, which is attributed to its peroxidase activity.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
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.
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 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 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.
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.
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.
Organic compounds which contain selenium as an integral part of the molecule.
Compounds containing the -SH radical.
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 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 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.
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.
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.
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
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Inorganic compounds that contain selenium as an integral part of the molecule.
A contact herbicide used also to produce desiccation and defoliation. (From Merck Index, 11th ed)
Electron-accepting molecules in chemical reactions in which electrons are transferred from one molecule to another (OXIDATION-REDUCTION).
Thiomalates are medicinal compounds, such as dimethylamine thiomalate, that contain a thiomalic acid structure and are used in the treatment of conditions like rheumatoid arthritis and ankylosing spondylitis due to their anti-inflammatory and analgesic properties.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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.
The rate dynamics in chemical or physical systems.
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)
A nutritional condition produced by a deficiency of VITAMIN E in the diet, characterized by posterior column and spinocerebellar tract abnormalities, areflexia, ophthalmoplegia, and disturbances of gait, proprioception, and vibration. In premature infants vitamin E deficiency is associated with hemolytic anemia, thrombocytosis, edema, intraventricular hemorrhage, and increasing risk of retrolental fibroplasia and bronchopulmonary dysplasia. An apparent inborn error of vitamin E metabolism, named familial isolated vitamin E deficiency, has recently been identified. (Cecil Textbook of Medicine, 19th ed, p1181)
'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 peroxiredoxin that is a cytosolic bifunctional enzyme. It functions as a peroxiredoxin via a single redox-active cysteine and also contains a Ca2+-independent acidic phospholipase A2 activity.
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.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A strong dibasic acid with the molecular formula H2SeO4. Included under this heading is the acid form, and inorganic salts of dihydrogen selenium tetraoxide.
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 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.
An agent thought to have disinfectant properties and used as an expectorant. (From Martindale, The Extra Pharmacopoeia, 30th ed, p747)
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.
A THIOREDOXIN-dependent hydroperoxidase that is localized in the mitochondrial matrix. The enzyme plays a crucial role in protecting mitochondrial components from elevated levels of HYDROGEN PEROXIDE.
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.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
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.
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.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A single SELENOCYSTEINE containing protein that binds reduced GLUTATHIONE and can act as an antioxidant.
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.
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.
A thioglucose derivative used as an antirheumatic and experimentally to produce obesity in animals.
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.
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.
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.
A myodegeneration most frequent in calves and lambs whose dams have been fed during gestation or longer on feeds, especially legumes (FABACEAE), grown in certain areas where selenium is either deficient or unavailable in the soil. It has been recorded in many countries. It has been produced experimentally in several species of animals on low-selenium intake. A similar myopathy occurs naturally in goats, deer, foals, and dogs but proof of the etiology is lacking. (Merck Veterinary Manual, 5th ed)
Inorganic compounds formed through the oxidation of selenium.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An enzyme derived from cow's milk. It catalyzes the radioiodination of tyrosine and its derivatives and of peptides containing tyrosine.
Regular course of eating and drinking adopted by a person or animal.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A subtype of thioredoxin reductase found primarily in the CYTOSOL.
A flour made of pulverized, dried fish or fish parts.
Unstable isotopes of selenium that decay or disintegrate emitting radiation. Se atoms with atomic weights 70-73, 75, 79, 81, and 83-85 are radioactive selenium isotopes.
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)
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.
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.
Organic compounds containing a carbonyl group in the form -CHO.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Elements of limited time intervals, contributing to particular results or situations.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A natural tocopherol and one of the most potent antioxidant tocopherols. It exhibits antioxidant activity by virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus. It has four methyl groups on the 6-chromanol nucleus. The natural d form of alpha-tocopherol is more active than its synthetic dl-alpha-tocopherol racemic mixture.
A group of proteins that covalently attach to selenium or SELENIUM-containing compounds.
Five membered rings containing a NITROGEN atom.
The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
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.
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.
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)
Compounds in which one or more of the ketone groups on the pyrimidine ring of barbituric acid are replaced by thione groups.
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.
A process involving chance used in therapeutic trials or other research endeavor for allocating experimental subjects, human or animal, between treatment and control groups, or among treatment groups. It may also apply to experiments on inanimate objects.
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.
**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.
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.
Established cell cultures that have the potential to propagate indefinitely.
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.
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.
Highly reactive compounds produced when oxygen is reduced by a single electron. In biological systems, they may be generated during the normal catalytic function of a number of enzymes and during the oxidation of hemoglobin to METHEMOGLOBIN. In living organisms, SUPEROXIDE DISMUTASE protects the cell from the deleterious effects of superoxides.
Use of plants or herbs to treat diseases or to alleviate pain.
A phylum of fungi that produce their sexual spores (basidiospores) on the outside of the basidium. It includes forms commonly known as mushrooms, boletes, puffballs, earthstars, stinkhorns, bird's-nest fungi, jelly fungi, bracket or shelf fungi, and rust and smut fungi.
An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria.
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.
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.
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.
An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. EC 1.11.1.10.
Products in capsule, tablet or liquid form that provide dietary ingredients, and that are intended to be taken by mouth to increase the intake of nutrients. Dietary supplements can include macronutrients, such as proteins, carbohydrates, and fats; and/or MICRONUTRIENTS, such as VITAMINS; MINERALS; and PHYTOCHEMICALS.
A rare autosomal recessive disorder resulting from the absence of CATALASE activity. Though usually asymptomatic, a syndrome of oral ulcerations and gangrene may be present.
A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.
The mass or quantity of heaviness of an individual. It is expressed by units of pounds or kilograms.
The convoluted cordlike structure attached to the posterior of the TESTIS. Epididymis consists of the head (caput), the body (corpus), and the tail (cauda). A network of ducts leaving the testis joins into a common epididymal tubule proper which provides the transport, storage, and maturation of SPERMATOZOA.
Proteins prepared by recombinant DNA technology.
Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.
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.
A subtype of thioredoxin reductase found primarily in MITOCHONDRIA.
An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
A plant genus of the family BRASSICACEAE known for its peppery red root.
Alcohols derived from the aryl radical (C6H5CH2-) and defined by C6H5CHOH. The concept includes derivatives with any substituents on the benzene ring.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
Organic derivatives of thiocyanic acid which contain the general formula R-SCN.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.
Inbred C57BL mice are a strain of laboratory mice that have been produced by many generations of brother-sister matings, resulting in a high degree of genetic uniformity and homozygosity, making them widely used for biomedical research, including studies on genetics, immunology, cancer, and neuroscience.
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.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
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.
The male gonad containing two functional parts: the SEMINIFEROUS TUBULES for the production and transport of male germ cells (SPERMATOGENESIS) and the interstitial compartment containing LEYDIG CELLS that produce ANDROGENS.
Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.
A series of prostaglandin-like compounds that are produced by the attack of free-radical species on unsaturated fatty acids, especially ARACHIDONIC ACID, of cellular MEMBRANES. Once cleaved from the lipid membrane by the action of phospholipases they can circulate into various bodily fluids and eventually be excreted. Although these compounds resemble enzymatically synthesized prostaglandins their stereoisometric arrangement is usually different than the "naturally occurring" compounds.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Alloxan is a chemical compound, specifically an organic compound, that is used in scientific research to induce diabetes in laboratory animals by destroying their insulin-producing cells in the pancreas.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The process by which chemical compounds provide protection to cells against harmful agents.
An enzyme that catalyzes the HYDROXYLATION of gamma-butyrobetaine to L-CARNITINE. It is the last enzyme in the biosynthetic pathway of L-CARNITINE and is dependent on alpha-ketoglutarate; IRON; ASCORBIC ACID; and OXYGEN.
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
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.
Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.
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)
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
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.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Antibodies that can catalyze a wide variety of chemical reactions. They are characterized by high substrate specificity and share many mechanistic features with enzymes.
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.
Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.
A group of chemical elements that are needed in minute quantities for the proper growth, development, and physiology of an organism. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.
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.
Chinese herbal or plant extracts which are used as drugs to treat diseases or promote general well-being. The concept does not include synthesized compounds manufactured in China.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Mature male germ cells derived from SPERMATIDS. As spermatids move toward the lumen of the SEMINIFEROUS TUBULES, they undergo extensive structural changes including the loss of cytoplasm, condensation of CHROMATIN into the SPERM HEAD, formation of the ACROSOME cap, the SPERM MIDPIECE and the SPERM TAIL that provides motility.
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.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
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.
The measurement of an organ in volume, mass, or heaviness.

Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. (1/2775)

In the yeast Saccharomyces cerevisiae, the non-Mendelian inherited genetic element [URE3] behaves as a prion. A hypothesis has been put forward which states that [URE3] arises spontaneously from its cellular isoform Ure2p (the product of the URE2 gene), and propagates through interactions of the N-terminal domain of the protein, thus leading to its aggregation and loss of function. In the present study, various N- and C-terminal deletion mutants of Ure2p were constructed and their cross-interactions were tested in vitro and in vivo using affinity binding and a two-hybrid analysis. We show that the self-interaction of the protein is mediated by at least two domains, corresponding to the first third of the protein (the so-called prion-forming domain) and the C-terminal catalytic domain.  (+info)

Inflammatory cell-mediated tumour progression and minisatellite mutation correlate with the decrease of antioxidative enzymes in murine fibrosarcoma cells. (2/2775)

We isolated six clones of weakly tumorigenic fibrosarcoma (QR) from the tumorigenic clone BMT-11 cl-9. The QR clones were unable to grow in normal C57BL/6 mice when injected s.c. (1x10(5) cells). However, they formed aggressive tumours upon co-implantation with a 'foreign body', i.e. a gelatin sponge, and the rate of tumour take ranged from 8% to 58% among QR clones. The enhanced tumorigenicity was due to host cell-mediated reaction to the gelatin sponge (inflammation). Immunoblot analysis and enzyme activity assay revealed a significant inverse correlation between the frequencies of tumour formation by QR clones and the levels of manganese superoxide dismutase (Mn-SOD, P<0.005) and glutathione peroxidase (GPchi, P<0.01) in the respective tumour clones. Electron spin resonance (ESR) revealed that superoxide-scavenging ability of cell lysates of the QR clone with high level of Mn-SOD was significantly higher than that with low level of the antioxidative enzyme in the presence of potassium cyanide, an inhibitor for copper-zinc superoxide dismutase (CuZn-SOD) (P<0.001). Minisatellite mutation (MSM) induced by the inflammatory cells in tumour cells were investigated by DNA fingerprint analysis after QR clones had been co-cultured with gelatin-sponge-reactive cells. The MSM rate was significantly higher in the subclones with low levels of Mn-SOD and GPchi (P<0.05) than in the subclones with high levels of both enzymes. The MSM of the subclones with low levels of both enzymes was inhibited in the presence of mannitol, a hydroxyl radical scavenger. The content of 8-hydroxydeoxyguanosine (8-OHdG) by which the cellular DNA damage caused by active oxygen species can be assessed was significantly low in the tumours arising from the QR clone with high levels of Mn-SOD and GPchi even if the clone had been co-implanted with gelatin sponge, compared with the arising tumour from the QR clone with low levels of those antioxidative enzymes (P<0.001). In contrast, CuZn-SOD and catalase levels in the six QR clones did not have any correlation with tumour progression parameters. These results suggest that tumour progression is accelerated by inflammation-induced active oxygen species particularly accompanied with declined levels of intracellular antioxidative enzymes in tumour cells.  (+info)

Prion domain initiation of amyloid formation in vitro from native Ure2p. (3/2775)

The [URE3] non-Mendelian genetic element of Saccharomyces cerevisiae is an infectious protein (prion) form of Ure2p, a regulator of nitrogen catabolism. Here, synthetic Ure2p1-65 were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent beta sheet. Ure2p1-65 specifically induced full-length native Ure2p to copolymerize under conditions where native Ure2p alone did not polymerize. Like Ure2p in extracts of [URE3] strains, these 180- to 220-angstrom-diameter filaments were protease resistant. The Ure2p1-65-Ure2p cofilaments could seed polymerization of native Ure2p to form thicker, less regular filaments. All filaments stained with Congo Red to produce the green birefringence typical of amyloid. This self-propagating amyloid formation can explain the properties of [URE3].  (+info)

Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes. (4/2775)

Selenium has been increasingly recognized as an essential element in biology and medicine. Its biochemistry resembles that of sulfur, yet differs from it by virtue of both redox potentials and stabilities of its oxidation states. Selenium can substitute for the more ubiquitous sulfur of cysteine and as such plays an important role in more than a dozen selenoproteins. We have chosen to examine zinc-sulfur centers as possible targets of selenium redox biochemistry. Selenium compounds release zinc from zinc/thiolate-coordination environments, thereby affecting the cellular thiol redox state and the distribution of zinc and likely of other metal ions. Aromatic selenium compounds are excellent spectroscopic probes of the otherwise relatively unstable functional selenium groups. Zinc-coordinated thiolates, e.g., metallothionein (MT), and uncoordinated thiolates, e.g., glutathione, react with benzeneseleninic acid (oxidation state +2), benzeneselenenyl chloride (oxidation state 0) and selenocystamine (oxidation state -1). Benzeneseleninic acid and benzeneselenenyl chloride react very rapidly with MT and titrate substoichiometrically and with a 1:1 stoichiometry, respectively. Selenium compounds also catalyze the release of zinc from MT in peroxidation and thiol/disulfide-interchange reactions. The selenoenzyme glutathione peroxidase catalytically oxidizes MT and releases zinc in the presence of t-butyl hydroperoxide, suggesting that this type of redox chemistry may be employed in biology for the control of metal metabolism. Moreover, selenium compounds are likely targets for zinc/thiolate coordination centers in vivo, because the reactions are only partially suppressed by excess glutathione. This specificity and the potential to undergo catalytic reactions at low concentrations suggests that zinc release is a significant aspect of the therapeutic antioxidant actions of selenium compounds in antiinflammatory and anticarcinogenic agents.  (+info)

Alloxan in vivo does not only exert deleterious effects on pancreatic B cells. (5/2775)

The aim of the experiment was to investigate the mechanism of harmful alloxan action in vivo. 75 mg/kg b.w. of this diabetogenic agent were administered to fasting rats. Two minutes later the animals were decapitated. It was observed that alloxan caused a distinct rise in blood insulin and glucose levels with a concomitant drop of free fatty acids. The amount of sulfhydryl groups in the liver of alloxan-treated rats was decreased and glutathione peroxidase activity was substantially higher. These results indicate that some changes observed in alloxan-induced diabetes can not only be the consequence of B cells damage by alloxan but may also be the result of its direct influence on other tissues. It was also observed that glucose given 20 min before alloxan injection only partially protected against the deleterious effects of alloxan.  (+info)

Effects of pre- or postpartum selenium supplementation on selenium status in beef cows and their calves. (6/2775)

The effect of Se supplementation before or after calving on Se status in deficient cows and their calves was studied using 72 beef cows in two experiments. In Exp. 1, cows calving in February or March 1997 were supplemented orally for 15 d in late pregnancy with 13.0, 32.5, or 45.5 mg of Se/d as sodium selenite. Glutathione peroxidase (GSH-Px) activities were measured in red blood cells (RBC) or plasma of cows and calves at d 15 and between d 17 and 88 after calving. In Exp. 2, cows calving in January 1997 were supplemented orally with .0, 13.0, or 32.5 mg of Se/d for 15 d postpartum, and calves were injected with 1.38 mg of Se when 2 d old and at an average age of 49 d. The GSH-Px activities were measured in 30-d-old calves and in cows and calves between d 77 and 115 after calving. In both experiments, Se supplementation resulted in adequate Se status for the dams. The increase in RBC GSH-Px activity was faster with 45.5 mg of Se/d, and GSH-Px activities remained high for up to 98 d after the end of supplementation. The improvement in Se status in calves as a result of maternal supplementation was greater in Exp. 1 than in Exp. 2, suggesting that the placental transfer of Se is more efficient than milk transfer. Prepartum oral Se supplementation of deficient beef cows with 13.0 mg of Se/d for 15 d allowed adequate Se status of dams and calves, and 45.5 mg of Se/d resulted in a faster improvement of Se status. Parenteral administration of 1.38 mg of Se to newborn calves did not sustain normal Se status in calves issued from deficient cows.  (+info)

Age-related changes in antioxidant enzyme activities in the small intestine and liver from Wistar rats. (7/2775)

The present study was designed to determine age-related changes in intestinal and hepatic antioxidant enzymes including superoxide dismutase (SOD), glutathione peroxidase (GSH-PX), and glutathione-S-transferase (GST), and lipid peroxidation in male Wistar rats (n = 8) aged 2 wk, 2.5 mon, 5 mon, 10 mon, and 23 mon. In the small intestine, cytosolic SOD, GSH-PX activities and lipid peroxidation were not affected by age, but intestinal GST activity was noticeably enhanced as age increased. In particular, intestinal GST activity in 23 mon old rats was 3 times as strong as that in 2 wk old rats. In the liver, the activity of hepatic cytosolic SOD was not affected by age, whereas GSH-PX and GST activities in rats aged 10 mon and 23 mon were much stronger than those in rats aged 2 wk, 2.5 mon, and 5 mon. The increased lipid peroxidation in 2.5 mon and 5 mon old rats was observed when compared with that of other groups. It is therefore concluded from the results presented here that age greatly increases GST activity in the small intestinal mucosae and increasing GSH-PX, GST activities and lipid peroxidation in the liver from male Wistar rats.  (+info)

Granulomatous inflammatory response to recombinant filarial proteins of Brugia species. (8/2775)

The lymphatic inflammatory response in Brugia-infected jirds peaks early during primary infections and then decreases in severity as judged by the numbers of lymph thrombi present within these vessels. Antigen-specific hypersensitivity reactions in these animals was measured by a pulmonary granulomatous inflammatory response (PGRN) induced by somatic adult worm antigen (SAWA)-coated beads, and by cellular proliferative responses of renal lymph node cells. The kinetics of these responses temporally correspond to lymphatic lesion formation. The importance of any single antigen to the induction of this inflammatory response has not been elucidated. In this study, the PGRN was used to measure the cellular immune response to four recombinant filarial proteins during the course of a primary B. pahangi infection. These proteins were BpL4, glycoprotein (glutathione peroxidase) gp29, heat shock protein (hsp) 70, and filarial chitinase. All were fusion proteins of maltose-binding protein (MBP). Control beads included those coated with diethanolamine (DEA), SAWA, or MBP. The measurements of PRGN were made at 14, 28, 56, and > 150 days postinfection (PI) in infected jirds, in jirds sensitized with SAWA, and in uninfected jirds. The secretory homolog of glutathione peroxidase gp29 was the only recombinant protein tested that induced a significantly greater PGRN (P < 0.05) than controls. This was seen at 28 days PI. These observations indicate that gp29 may be part of the worm antigen complex that induces an early inflammatory response, a response similar to that observed with SAWA. These studies indicate that this approach is useful in investigating the functional ability of specific proteins in the induction and down-regulation of immune-mediated inflammatory responses elicited by filarial parasites. Absence of a granulomatous response to the other recombinant proteins used may be related to the nature and sensitivity of the assay used or the character of recombinant proteins tested.  (+info)

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.

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.

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.

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.

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 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.

Horseradish peroxidase (HRP) is not a medical term, but a type of enzyme that is derived from the horseradish plant. In biological terms, HRP is defined as a heme-containing enzyme isolated from the roots of the horseradish plant (Armoracia rusticana). It is widely used in molecular biology and diagnostic applications due to its ability to catalyze various oxidative reactions, particularly in immunological techniques such as Western blotting and ELISA.

HRP catalyzes the conversion of hydrogen peroxide into water and oxygen, while simultaneously converting a variety of substrates into colored or fluorescent products that can be easily detected. This enzymatic activity makes HRP a valuable tool in detecting and quantifying specific biomolecules, such as proteins and nucleic acids, in biological samples.

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.

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.

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.

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.

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.

Peroxidase is a type of enzyme that catalyzes the chemical reaction in which hydrogen peroxide (H2O2) is broken down into water (H2O) and oxygen (O2). This enzymatic reaction also involves the oxidation of various organic and inorganic compounds, which can serve as electron donors.

Peroxidases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in various biological processes, such as defense against oxidative stress, breakdown of toxic substances, and participation in metabolic pathways.

The peroxidase-catalyzed reaction can be represented by the following chemical equation:

H2O2 + 2e- + 2H+ → 2H2O

In this reaction, hydrogen peroxide is reduced to water, and the electron donor is oxidized. The peroxidase enzyme facilitates the transfer of electrons between the substrate (hydrogen peroxide) and the electron donor, making the reaction more efficient and specific.

Peroxidases have various applications in medicine, industry, and research. For example, they can be used for diagnostic purposes, as biosensors, and in the treatment of wastewater and medical wastes. Additionally, peroxidases are involved in several pathological conditions, such as inflammation, cancer, and neurodegenerative diseases, making them potential targets for therapeutic interventions.

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.

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.

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.

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.

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.

Cytochrome-c peroxidase is an enzyme found in the inner membrane of mitochondria, which are the energy-producing structures in cells. It plays a crucial role in the electron transport chain, a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.

The enzyme's primary function is to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect the cell from the harmful effects of hydrogen peroxide, which can damage proteins, lipids, and DNA if left unchecked.

Cytochrome-c peroxidase contains a heme group, which is a prosthetic group consisting of an iron atom surrounded by a porphyrin ring. This heme group is responsible for the enzyme's ability to undergo redox reactions, where it cycles between its oxidized and reduced states during the catalytic cycle.

The medical relevance of cytochrome-c peroxidase lies in its role in cellular metabolism and energy production. Dysfunctions in the electron transport chain or oxidative phosphorylation processes, including those involving cytochrome-c peroxidase, can lead to various mitochondrial disorders and diseases, such as neurodegenerative conditions, muscle weakness, and metabolic abnormalities. However, it is essential to note that the study of this enzyme and its role in health and disease is still an active area of research.

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.

Ascorbate peroxidases (AHPX) are a group of enzymes that use ascorbic acid (vitamin C) as a reducing cofactor to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from oxidative damage caused by the accumulation of H2O2, a byproduct of various metabolic processes. Ascorbate peroxidases are primarily found in plants, algae, and cyanobacteria, where they play a crucial role in the detoxification of reactive oxygen species generated during photosynthesis.

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.

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.

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.

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.

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.

Iodide peroxidase, also known as iodide:hydrogen peroxide oxidoreductase, is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a peroxidase that uses iodide as its physiological reducing substrate. This enzyme catalyzes the oxidation of iodide by hydrogen peroxide to produce iodine, which plays a crucial role in thyroid hormone biosynthesis.

The systematic name for this enzyme is iodide:hydrogen-peroxide oxidoreductase (iodinating). It is most commonly found in the thyroid gland, where it helps to produce and regulate thyroid hormones by facilitating the iodination of tyrosine residues on thyroglobulin, a protein produced by the thyroid gland.

Iodide peroxidase requires a heme cofactor for its enzymatic activity, which is responsible for the oxidation-reduction reactions it catalyzes. The enzyme's ability to iodinate tyrosine residues on thyroglobulin is essential for the production of triiodothyronine (T3) and thyroxine (T4), two critical hormones that regulate metabolism, growth, and development in mammals.

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.

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.

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.

Eosinophil peroxidase (EPO) is an enzyme that is primarily found in the granules of eosinophils, which are a type of white blood cell that plays a role in the immune response. EPO is involved in the destruction of certain types of parasites and also contributes to the inflammatory response in allergic reactions and other diseases.

EPO catalyzes the conversion of hydrogen peroxide to hypochlorous acid, which is a potent oxidizing agent that can kill or inhibit the growth of microorganisms. EPO also plays a role in the production of other reactive oxygen species, which can contribute to tissue damage and inflammation in certain conditions.

Elevated levels of EPO in tissues or bodily fluids may be indicative of eosinophil activation and degranulation, which can occur in various diseases such as asthma, allergies, parasitic infections, and some types of cancer. Measuring EPO levels can be useful in the diagnosis and monitoring of these conditions.

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.

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.

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.

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.

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.

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).

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.

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.

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.

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.

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.

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.

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.

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.

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.

"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.

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.

Diquat is a herbicide that is used to control the growth of weeds and unwanted vegetation in various settings, such as agricultural land, aquatic environments, and industrial sites. It is a type of chemical known as a contact herbicide, which means that it kills plants on contact rather than being absorbed through the plant's roots and transported throughout its tissues.

Diquat works by disrupting the plant's ability to photosynthesize, or convert light energy into chemical energy. When applied to plant leaves, diquat causes the formation of free radicals, which are highly reactive molecules that can damage cell membranes and other cell structures. This leads to the death of the plant cells and ultimately the death of the entire plant.

Diquat is a fast-acting herbicide that is often used to control weeds in aquatic environments, such as ponds and lakes. It is also used in agriculture to desiccate crops before harvest, which can make them easier to harvest and reduce post-harvest losses. However, diquat can be harmful to non-target organisms, including fish, aquatic invertebrates, and beneficial insects, so it must be used carefully and in accordance with label instructions to minimize off-target impacts.

Like all pesticides, diquat is subject to regulation by government agencies such as the Environmental Protection Agency (EPA) in the United States. The EPA sets limits on the amount of diquat that can be applied to crops and other surfaces, and requires manufacturers to provide information about the potential risks and hazards associated with its use. It is important to follow all safety precautions and guidelines when using diquat or any other pesticide to protect yourself, others, and the environment.

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.

Thiomalates are not a medical term per se, but they refer to a group of chemical compounds that contain a sulfur atom (thio-) and a malic acid component (-malate). In the medical context, thiomalates are primarily known for their use in the preparation of certain medications. Specifically, potassium or sodium salt of thiomalic acid is used as an active ingredient in some types of disease-modifying antirheumatic drugs (DMARDs), such as rheumatoid arthritis treatments. These medications, known as thiomalate drugs, work by reducing inflammation and slowing down the progression of the disease.

Examples of thiomalate drugs include:

* Sodium thiomalate (brand name: Thiosal)
* Potassium thiomalate (brand name: Thiomal-K)

It is important to note that these medications can have side effects and potential risks, so they should only be used under the supervision of a healthcare professional.

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.

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.

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.

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.

Vitamin E deficiency is a condition that occurs when there is a lack of sufficient vitamin E in the body. Vitamin E is a fat-soluble antioxidant that plays an essential role in maintaining the health of cell membranes, protecting them from damage caused by free radicals. It also helps to support the immune system and promotes healthy blood vessels and nerves.

Vitamin E deficiency can occur due to several reasons, including malnutrition, malabsorption disorders such as cystic fibrosis or celiac disease, premature birth, or genetic defects affecting the alpha-tocopherol transfer protein (alpha-TTP), which is responsible for transporting vitamin E from the liver to other tissues.

Symptoms of vitamin E deficiency may include:

* Neurological problems such as peripheral neuropathy, ataxia (loss of coordination), and muscle weakness
* Retinopathy (damage to the retina) leading to vision loss
* Increased susceptibility to oxidative stress and inflammation
* Impaired immune function

Vitamin E deficiency is rare in healthy individuals who consume a balanced diet, but it can occur in people with certain medical conditions or those who have undergone bariatric surgery. In these cases, supplementation may be necessary to prevent or treat vitamin E deficiency.

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.

Peroxiredoxin VI (Prdx6) is an antioxidant enzyme that belongs to the peroxiredoxin family. It plays a crucial role in reducing and regulating the levels of hydrogen peroxide, lipid peroxides, and other reactive oxygen species (ROS) within cells. Prdx6 has both peroxidase and phospholipase A2 activities, which makes it unique among the peroxiredoxins. It is widely expressed in various tissues, including the lungs, liver, kidneys, and brain. In addition to its antioxidant function, Prdx6 also contributes to cellular signaling pathways, inflammation regulation, and membrane repair processes. Dysregulation of Prdx6 has been implicated in several diseases, such as cancer, neurodegenerative disorders, and lung injury.

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.

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.

I'm sorry for any confusion, but "Selenic Acid" is not a recognized term in medicine or physiology. Selenium, however, is an essential trace element that is important for proper immune function, antioxidant activity, and thyroid hormone metabolism. Selenious acid (H2SeO3) is a compound of selenium, but it's more commonly used in the context of chemistry or industrial processes rather than medicine or biology. If you have any questions related to medicine or health, I'd be happy to try and help with those!

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.

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.

Guaiacol is not a medical term per se, but it is a chemical compound with potential applications in the medical field. Here's a general definition:

Guaiacol (also known as 2-methoxyphenol) is an organic compound that belongs to the class of phenols. It is a colorless or slightly yellow oily liquid with a characteristic smoky odor, and it is soluble in alcohol and ether but only sparingly soluble in water. Guaiacol occurs naturally in the smoke of wood fires and is also found in certain plants, such as guaiacum and creosote bush. It has antimicrobial properties and is used in some medical and industrial applications, including as a precursor for the synthesis of other chemicals.

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.

Peroxiredoxin III (PrxIII) is an antioxidant enzyme that belongs to the peroxiredoxin family. It plays a crucial role in maintaining the redox balance within cells by reducing hydrogen peroxide and other organic peroxides into water and alcohol, respectively. PrxIII is primarily located in the mitochondrial matrix, where it protects against oxidative damage to proteins, lipids, and DNA caused by reactive oxygen species (ROS). It functions as a homodimer and contains a conserved catalytic cysteine residue that gets oxidized during the reduction of peroxides. This oxidized form can be reduced back to its active state by thioredoxin or other reducing agents, allowing PrxIII to continue scavenging ROS. Mutations in the PRDX3 gene, which encodes Peroxiredoxin III, have been associated with various pathological conditions, including neurodegenerative diseases and cancer.

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.

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.

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.

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.

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.

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.

Selenoprotein W is a protein that contains selenocysteine, an amino acid containing selenium. It is primarily found in muscle tissue and plays a role in protecting muscles from oxidative damage and maintaining the proper function of calcium channels. Selenoprotein W has been studied for its potential role in various health conditions related to muscle function and oxidative stress, such as muscular dystrophy and inflammation.

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.

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.

Aurothioglucose is a gold-containing medication that has been used in the treatment of rheumatoid arthritis. It works by modulating the immune system and reducing inflammation in the joints. The medication is administered via injection, usually into a muscle (intramuscularly).

The use of aurothioglucose has declined in recent years due to the availability of newer and more effective medications for rheumatoid arthritis. Additionally, aurothioglucose can have significant side effects, including kidney damage, skin reactions, and blood disorders. It is important to be monitored by a healthcare provider while taking this medication to ensure that it is safe and effective for use.

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.

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.

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.

White muscle disease is not a formal medical term, but it is a condition commonly referred to in veterinary medicine, particularly in the context of livestock and wildlife. It's also known as nutritional muscular dystrophy or enzootic muscular dystrophy.

The term "white muscle disease" refers to a group of conditions characterized by degeneration and necrosis (death) of skeletal and cardiac muscle tissue, primarily caused by deficiencies in certain nutrients, particularly selenium and vitamin E. These nutrients play crucial roles in the antioxidant defense system within the body, protecting cells from oxidative damage.

In affected animals, the lack of these essential nutrients leads to muscle damage, which can result in various clinical signs, such as:

1. Weakness
2. Stiffness
3. Reluctance to move
4. Difficulty swallowing or breathing (in severe cases)
5. Sudden death (often due to heart failure)

White muscle disease is most commonly observed in ruminants like cattle, sheep, and goats, as well as certain species of swine, poultry, and wild animals. It can be prevented through dietary supplementation with selenium and vitamin E or by providing these nutrients through mineral-rich soil and forage. In some cases, treatment may involve administering selenium and vitamin E injections to help support muscle recovery and prevent further damage.

Selenium oxides are inorganic compounds that contain selenium in an oxidized state combined with oxygen. The most common forms of selenium oxides include:

1. Selenium dioxide (SeO2): A red or yellow crystalline solid, selenium dioxide is formed by the oxidation of elemental selenium or by the burning of selenium in air. It is soluble in water and alcohol, forming selenous acid.

2. Selenium trioxide (SeO3): A white crystalline solid, selenium trioxide is a strong oxidizing agent that can react violently with reducing agents. It is used as a catalyst in the industrial production of certain chemicals and as a reagent in organic synthesis.

Selenium oxides have been studied for their potential use in various medical applications, such as antimicrobial agents and drug delivery systems. However, they are not currently used as therapeutic agents in clinical medicine due to their toxicity and potential health hazards.

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.

Lactoperoxidase is a type of peroxidase enzyme that is present in various secretory fluids, including milk, saliva, and tears. In milk, lactoperoxidase plays an important role in the natural defense system by helping to protect against microbial growth. It does this by catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which is a potent antimicrobial agent.

Lactoperoxidase is a glycoprotein with a molecular weight of approximately 78 kDa, and it is composed of four identical subunits, each containing a heme group that binds to the hydrogen peroxide molecule during the enzymatic reaction. Lactoperoxidase has been studied for its potential therapeutic applications in various fields, including oral health, food preservation, and wound healing.

A diet, in medical terms, refers to the planned and regular consumption of food and drinks. It is a balanced selection of nutrient-rich foods that an individual eats on a daily or periodic basis to meet their energy needs and maintain good health. A well-balanced diet typically includes a variety of fruits, vegetables, whole grains, lean proteins, and low-fat dairy products.

A diet may also be prescribed for therapeutic purposes, such as in the management of certain medical conditions like diabetes, hypertension, or obesity. In these cases, a healthcare professional may recommend specific restrictions or modifications to an individual's regular diet to help manage their condition and improve their overall health.

It is important to note that a healthy and balanced diet should be tailored to an individual's age, gender, body size, activity level, and any underlying medical conditions. Consulting with a healthcare professional, such as a registered dietitian or nutritionist, can help ensure that an individual's dietary needs are being met in a safe and effective way.

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.

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.

I'm sorry for any confusion, but "Fish Flour" is not a recognized term in medical terminology. It is possible that you may be referring to "fish meal," which is a product made from ground-up fish and is used as a protein source in animal feeds. However, it is not typically used in human food or medicine. If you have any concerns about the use of this substance or any other unusual substances in human health, I would recommend consulting with a healthcare professional for accurate information.

Selenium radioisotopes are unstable forms of the element selenium that emit radiation as they decay into more stable forms. These isotopes can be produced through various nuclear reactions, such as irradiating a stable selenium target with protons or alpha particles. Some examples of selenium radioisotopes include selenium-75, selenium-79, and selenium-81.

Selenium-75 is commonly used in medical imaging to study the function of the thyroid gland, as it accumulates in this gland and can be detected using a gamma camera. Selenium-79 and selenium-81 have potential uses in cancer treatment, as they can be incorporated into compounds that selectively target and destroy cancer cells. However, more research is needed to fully understand the potential benefits and risks of using these radioisotopes in medical treatments.

It's important to note that handling and using radioisotopes requires special training and precautions, as they can be dangerous if not handled properly. Exposure to radiation from radioisotopes can increase the risk of cancer and other health problems, so it's essential to use them only under controlled conditions and with appropriate safety measures in place.

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.

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.

"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.

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.

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.

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.

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.

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.

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.

Alpha-tocopherol is the most active form of vitamin E in humans and is a fat-soluble antioxidant that helps protect cells from damage caused by free radicals. It plays a role in immune function, cell signaling, and metabolic processes. Alpha-tocopherol is found naturally in foods such as nuts, seeds, leafy green vegetables, and vegetable oils, and it is also available as a dietary supplement.

Selenium-binding proteins (Se-binding proteins) are a group of proteins that contain selenocysteine, an amino acid containing selenium. Selenocysteine is incorporated into these proteins at specific positions during protein synthesis, and it plays a crucial role in the function of Se-binding proteins.

One of the most well-known Se-binding proteins is glutathione peroxidase (GPx), an antioxidant enzyme that protects cells from oxidative damage by reducing hydrogen peroxide and lipid peroxides to water and alcohols, respectively. Other Se-binding proteins include thioredoxin reductase, which plays a role in redox regulation, and iodothyronine deiodinases, which are involved in thyroid hormone metabolism.

Se-binding proteins have been identified in various organisms, including bacteria, archaea, and eukaryotes. In humans, Se-binding proteins are found in a variety of tissues, including the liver, kidney, and brain. The expression and activity of Se-binding proteins can be influenced by factors such as selenium status, oxidative stress, and inflammation.

"Azoles" is a class of antifungal medications that have a similar chemical structure, specifically a five-membered ring containing nitrogen and two carbon atoms (a "azole ring"). The most common azoles used in medicine include:

1. Imidazoles: These include drugs such as clotrimazole, miconazole, and ketoconazole. They are used to treat a variety of fungal infections, including vaginal yeast infections, thrush, and skin infections.
2. Triazoles: These include drugs such as fluconazole, itraconazole, and voriconazole. They are also used to treat fungal infections, but have a broader spectrum of activity than imidazoles and are often used for more serious or systemic infections.

Azoles work by inhibiting the synthesis of ergosterol, an essential component of fungal cell membranes. This leads to increased permeability of the cell membrane, which ultimately results in fungal cell death.

While azoles are generally well-tolerated, they can cause side effects such as nausea, vomiting, and abdominal pain. In addition, some azoles can interact with other medications and affect liver function, so it's important to inform your healthcare provider of all medications you are taking before starting an azole regimen.

I'm sorry for any confusion, but "Lignin" is not a medical term. It is a term used in the field of biology and chemistry, particularly in botany and wood science. Lignin is a complex organic polymer that binds cellulose fibers together, providing strength and rigidity to the cell walls of plants. It is a major component of wood and bark.

If you have any medical terms you would like defined or any other questions, please let me know!

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.

"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.

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.

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.

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.

Thiobarbiturates are a class of barbiturates that contain a sulfur atom in place of the oxygen atom in the urea-like structure. They are central nervous system depressants, which means they can cause decreased heart rate, blood pressure, and breathing. These properties make them useful for anesthesia and sedation, but also contribute to their potential for abuse and dependence.

Thiobarbiturates have been largely replaced by other classes of drugs due to their narrow therapeutic index (the difference between the effective dose and a toxic dose is small) and high potential for overdose. Examples of thiobarbiturates include thiopental, used for induction of anesthesia, and pentobarbital, which has been used for both anesthesia and as a treatment for seizures.

It's important to note that barbiturates and thiobarbiturates are controlled substances in many countries due to their potential for abuse and dependence. They should only be prescribed and administered by trained medical professionals.

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.

"Random allocation," also known as "random assignment" or "randomization," is a process used in clinical trials and other research studies to distribute participants into different intervention groups (such as experimental group vs. control group) in a way that minimizes selection bias and ensures the groups are comparable at the start of the study.

In random allocation, each participant has an equal chance of being assigned to any group, and the assignment is typically made using a computer-generated randomization schedule or other objective methods. This process helps to ensure that any differences between the groups are due to the intervention being tested rather than pre-existing differences in the participants' characteristics.

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.

"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.

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.

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.

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.

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.

Superoxides are partially reduced derivatives of oxygen that contain one extra electron, giving them an overall charge of -1. They are highly reactive and unstable, with the most common superoxide being the hydroxyl radical (•OH-) and the superoxide anion (O2-). Superoxides are produced naturally in the body during metabolic processes, particularly within the mitochondria during cellular respiration. They play a role in various physiological processes, but when produced in excess or not properly neutralized, they can contribute to oxidative stress and damage to cells and tissues, potentially leading to the development of various diseases such as cancer, atherosclerosis, and neurodegenerative disorders.

Phytotherapy is the use of extracts of natural origin, especially plants or plant parts, for therapeutic purposes. It is also known as herbal medicine and is a traditional practice in many cultures. The active compounds in these plant extracts are believed to have various medicinal properties, such as anti-inflammatory, analgesic, or sedative effects. Practitioners of phytotherapy may use the whole plant, dried parts, or concentrated extracts to prepare teas, capsules, tinctures, or ointments for therapeutic use. It is important to note that the effectiveness and safety of phytotherapy are not always supported by scientific evidence, and it should be used with caution and preferably under the guidance of a healthcare professional.

Basidiomycota is a phylum in the kingdom Fungi that consists of organisms commonly known as club fungi or club mushrooms. The name Basidiomycota is derived from the presence of a characteristic reproductive structure called a basidium, which is where spores are produced.

The basidiomycetes include many familiar forms such as mushrooms, toadstools, bracket fungi, and other types of polypores. They have a complex life cycle that involves both sexual and asexual reproduction. The sexual reproductive stage produces a characteristic fruiting body, which may be microscopic or highly visible, depending on the species.

Basidiomycota fungi play important ecological roles in decomposing organic matter, forming mutualistic relationships with plants, and acting as parasites on other organisms. Some species are economically important, such as edible mushrooms, while others can be harmful or even deadly to humans and animals.

Xanthine oxidase is an enzyme that catalyzes the oxidation of xanthine to uric acid, which is the last step in purine metabolism. It's a type of molybdenum-containing oxidoreductase that generates reactive oxygen species (ROS) during its reaction mechanism.

The enzyme exists in two interconvertible forms: an oxidized state and a reduced state. The oxidized form, called xanthine oxidase, reduces molecular oxygen to superoxide and hydrogen peroxide, while the reduced form, called xanthine dehydrogenase, reduces NAD+ to NADH.

Xanthine oxidase is found in various tissues, including the liver, intestines, and milk. An overproduction of uric acid due to increased activity of xanthine oxidase can lead to hyperuricemia, which may result in gout or kidney stones. Some medications and natural compounds are known to inhibit xanthine oxidase, such as allopurinol and febuxostat, which are used to treat gout and prevent the formation of uric acid stones in the kidneys.

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.

"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.

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.

Chloride peroxidase is an enzyme that contains heme as a cofactor and is responsible for catalyzing the oxidation of chloride ions (Cl-) to hypochlorous acid (HOCl) using hydrogen peroxide (H2O2) as a substrate. This reaction plays a crucial role in the microbial defense system of certain organisms, such as the halophilic archaea. The enzyme is also known as chloroperoxidase or CPO.

The chemical reaction catalyzed by chloride peroxidase can be represented as follows:

Cl- + H2O2 → HOCl + H2O

Hypochlorous acid is a powerful oxidizing agent that can kill or inhibit the growth of various microorganisms, making it an important component of the immune system in some organisms. Chloride peroxidase has attracted significant interest from researchers due to its potential applications in biotechnology and environmental protection, such as in the development of new disinfection methods and the removal of pollutants from water.

A dietary supplement is a product that contains nutrients, such as vitamins, minerals, amino acids, herbs or other botanicals, and is intended to be taken by mouth, to supplement the diet. Dietary supplements can include a wide range of products, such as vitamin and mineral supplements, herbal supplements, and sports nutrition products.

Dietary supplements are not intended to treat, diagnose, cure, or alleviate the effects of diseases. They are intended to be used as a way to add extra nutrients to the diet or to support specific health functions. It is important to note that dietary supplements are not subject to the same rigorous testing and regulations as drugs, so it is important to choose products carefully and consult with a healthcare provider if you have any questions or concerns about using them.

Acatalasia is a very rare inherited disorder that affects the body's ability to break down and remove hydrogen peroxide, a byproduct produced during normal cellular metabolism. This condition is caused by a deficiency or complete lack of the enzyme catalase, which is responsible for converting hydrogen peroxide into water and oxygen.

The medical definition of Acatalasia can be described as:

1. An autosomal recessive genetic disorder: Acatalasia is inherited in an autosomal recessive pattern, meaning that an individual must inherit two copies of the defective gene (one from each parent) to develop the condition. Individuals who inherit only one copy of the defective gene are carriers and do not typically show symptoms themselves.

2. Absence or deficiency of catalase enzyme: Acatalasia is characterized by a near-complete absence or significantly reduced levels of the catalase enzyme in the body, primarily in red blood cells and certain tissues such as the liver and spleen. This deficiency leads to an accumulation of hydrogen peroxide within cells.

3. Accumulation of hydrogen peroxide: The buildup of hydrogen peroxide can cause damage to cellular components, including proteins, lipids, and DNA, potentially leading to various health issues over time.

4. Clinical manifestations: Although Acatalasia is a rare condition, when it does occur, it can lead to several health problems, such as chronic granulomatous disease (CGD), which is characterized by recurrent bacterial and fungal infections due to impaired immune function. Additionally, individuals with Acatalasia may have an increased risk of developing certain types of cancer, particularly those related to the hematopoietic system (blood cells and bone marrow).

5. Diagnosis: Acatalasia can be diagnosed through various methods, including blood tests that measure catalase enzyme activity, genetic testing to identify mutations in the CAT gene (which encodes for the catalase enzyme), and clinical evaluation of symptoms and medical history.

6. Treatment and management: Currently, there is no specific treatment or cure for Acatalasia. Management typically focuses on addressing individual symptoms as they arise and implementing strategies to reduce the risk of complications. This may include antibiotics or antifungal medications to treat infections, cancer surveillance and prevention measures, and regular monitoring of overall health.

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.

Body weight is the measure of the force exerted on a scale or balance by an object's mass, most commonly expressed in units such as pounds (lb) or kilograms (kg). In the context of medical definitions, body weight typically refers to an individual's total weight, which includes their skeletal muscle, fat, organs, and bodily fluids.

Healthcare professionals often use body weight as a basic indicator of overall health status, as it can provide insights into various aspects of a person's health, such as nutritional status, metabolic function, and risk factors for certain diseases. For example, being significantly underweight or overweight can increase the risk of developing conditions like malnutrition, diabetes, heart disease, and certain types of cancer.

It is important to note that body weight alone may not provide a complete picture of an individual's health, as it does not account for factors such as muscle mass, bone density, or body composition. Therefore, healthcare professionals often use additional measures, such as body mass index (BMI), waist circumference, and blood tests, to assess overall health status more comprehensively.

The epididymis is a tightly coiled tube located on the upper and posterior portion of the testicle that serves as the site for sperm maturation and storage. It is an essential component of the male reproductive system. The epididymis can be divided into three parts: the head (where newly produced sperm enter from the testicle), the body, and the tail (where mature sperm exit and are stored). Any abnormalities or inflammation in the epididymis may lead to discomfort, pain, or infertility.

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.

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.

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).

Thioredoxin Reductase 2 (Txnrd2) is an antioxidant enzyme that plays a crucial role in maintaining the redox balance within cells, particularly in the mitochondria. It is a member of the thioredoxin reductase family, which are selenium-containing proteins that catalyze the reduction of various substrates through the use of NADPH as an electron donor.

Txnrd2 specifically reduces the disulfide bond in mitochondrial thioredoxin 2 (Trx2), regenerating its active form and allowing it to neutralize reactive oxygen species (ROS) and maintain the redox state of proteins within the mitochondria. This enzyme is essential for protecting cells against oxidative stress, which can damage cellular components such as DNA, proteins, and lipids. Dysregulation of Txnrd2 has been implicated in various pathological conditions, including neurodegenerative diseases, cancer, and aging.

Glucose oxidase (GOD) is an enzyme that catalyzes the oxidation of D-glucose to D-glucono-1,5-lactone, while reducing oxygen to hydrogen peroxide in the process. This reaction is a part of the metabolic pathway in some organisms that convert glucose into energy. The systematic name for this enzyme is D-glucose:oxygen 1-oxidoreductase.

Glucose oxidase is commonly found in certain fungi, such as Aspergillus niger, and it has various applications in industry, medicine, and research. For instance, it's used in the production of glucose sensors for monitoring blood sugar levels, in the detection and quantification of glucose in food and beverages, and in the development of biosensors for environmental monitoring.

It's worth noting that while glucose oxidase has many applications, it should not be confused with glutathione peroxidase, another enzyme involved in the reduction of hydrogen peroxide to water.

Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.

In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.

It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.

"Raphanus" is the genus name for a group of plants that include the common radish. The black radish (*Raphanus sativus* var. *niger*) and the white radish (also known as daikon or *Raphanus sativus* var. *longipinnatus*) are examples of species within this genus. These plants belong to the family Brassicaceae, which also includes vegetables such as broccoli, cabbage, and kale. The roots, leaves, and seeds of Raphanus plants have been used in traditional medicine for various purposes, including as a digestive aid and to treat respiratory conditions. However, it is essential to consult with a healthcare professional before using these plants or their extracts for medicinal purposes, as they can interact with certain medications and may cause side effects.

Benzyl alcohol is an aromatic alcohol with the chemical formula C6H5CH2OH. It is a colorless liquid with a mild, pleasant odor and is used as a solvent and preservative in cosmetics, medications, and other products. Benzyl alcohol can also be found as a natural component of some essential oils, fruits, and teas.

Benzyl alcohol is not typically considered a "drug" or a medication, but it may have various pharmacological effects when used in certain medical contexts. For example, it has antimicrobial properties and is sometimes used as a preservative in injectable medications to prevent the growth of bacteria and fungi. It can also be used as a local anesthetic or analgesic in some topical creams and ointments.

It's important to note that benzyl alcohol can be harmful or fatal to infants and young children, especially when it is used in high concentrations or when it is introduced into the body through intravenous (IV) routes. Therefore, it should be used with caution in these populations and only under the guidance of a healthcare professional.

The myocardium is the middle layer of the heart wall, composed of specialized cardiac muscle cells that are responsible for pumping blood throughout the body. It forms the thickest part of the heart wall and is divided into two sections: the left ventricle, which pumps oxygenated blood to the rest of the body, and the right ventricle, which pumps deoxygenated blood to the lungs.

The myocardium contains several types of cells, including cardiac muscle fibers, connective tissue, nerves, and blood vessels. The muscle fibers are arranged in a highly organized pattern that allows them to contract in a coordinated manner, generating the force necessary to pump blood through the heart and circulatory system.

Damage to the myocardium can occur due to various factors such as ischemia (reduced blood flow), infection, inflammation, or genetic disorders. This damage can lead to several cardiac conditions, including heart failure, arrhythmias, and cardiomyopathy.

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.

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.

Tissue distribution, in the context of pharmacology and toxicology, refers to the way that a drug or xenobiotic (a chemical substance found within an organism that is not naturally produced by or expected to be present within that organism) is distributed throughout the body's tissues after administration. It describes how much of the drug or xenobiotic can be found in various tissues and organs, and is influenced by factors such as blood flow, lipid solubility, protein binding, and the permeability of cell membranes. Understanding tissue distribution is important for predicting the potential effects of a drug or toxin on different parts of the body, and for designing drugs with improved safety and efficacy profiles.

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

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.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

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.

The testis, also known as the testicle, is a male reproductive organ that is part of the endocrine system. It is located in the scrotum, outside of the abdominal cavity. The main function of the testis is to produce sperm and testosterone, the primary male sex hormone.

The testis is composed of many tiny tubules called seminiferous tubules, where sperm are produced. These tubules are surrounded by a network of blood vessels, nerves, and supportive tissues. The sperm then travel through a series of ducts to the epididymis, where they mature and become capable of fertilization.

Testosterone is produced in the Leydig cells, which are located in the interstitial tissue between the seminiferous tubules. Testosterone plays a crucial role in the development and maintenance of male secondary sexual characteristics, such as facial hair, deep voice, and muscle mass. It also supports sperm production and sexual function.

Abnormalities in testicular function can lead to infertility, hormonal imbalances, and other health problems. Regular self-examinations and medical check-ups are recommended for early detection and treatment of any potential issues.

A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.

In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:

1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.

It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Aging is a complex, progressive and inevitable process of bodily changes over time, characterized by the accumulation of cellular damage and degenerative changes that eventually lead to increased vulnerability to disease and death. It involves various biological, genetic, environmental, and lifestyle factors that contribute to the decline in physical and mental functions. The medical field studies aging through the discipline of gerontology, which aims to understand the underlying mechanisms of aging and develop interventions to promote healthy aging and extend the human healthspan.

Isoprostanes are a type of prostaglandin-like compounds that are produced in the body through the free radical-catalyzed peroxidation of arachidonic acid, a polyunsaturated fatty acid found in cell membranes. They are formed in situ on phospholipids and then released as free isoprostanes by the action of phospholipases.

Isoprostanes are chemically stable and can be measured in various biological fluids such as urine, blood, and breath to assess oxidative stress in the body. They have been used as biomarkers for lipid peroxidation and oxidative damage in several diseases, including atherosclerosis, cancer, neurodegenerative disorders, and respiratory diseases.

Isoprostanes can also activate various signaling pathways and contribute to the development of inflammation, vasoconstriction, platelet aggregation, and other physiological responses. Therefore, they play a significant role in the pathogenesis of several diseases associated with oxidative stress and inflammation.

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.

Alloxan is a chemical compound that is primarily used in laboratory research. Its medical definition is:

A toxic, crystalline substance, C6H4O6, derived from uric acid, and used experimentally to produce diabetes in animals by destroying their insulin-producing cells (beta cells) in the pancreas. Alloxan monohydrate is a white crystalline powder that is soluble in water and alcohol. It is used as a reagent in analytical chemistry and in photography.

In scientific research, alloxan is often used to induce diabetes in laboratory animals (like rats and mice) in order to study the disease and potential treatments. The compound is toxic to the insulin-producing beta cells in the pancreas, leading to a decrease in insulin production and an increase in blood glucose levels, similar to what occurs in type 1 diabetes in humans. However, it's important to note that alloxan-induced diabetes does not perfectly mimic the human form of the disease, and results from such studies may not always translate directly to human treatments.

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.

Cytoprotection refers to the protection of cells, particularly from harmful agents or damaging conditions. This can be achieved through various mechanisms, such as:

1. Activation of cellular defense pathways that help cells resist damage.
2. Inhibition of oxidative stress and inflammation, which can cause cellular damage.
3. Enhancement of cell repair processes, enabling cells to recover from damage more effectively.
4. Prevention of apoptosis (programmed cell death) or promotion of cell survival signals.

In the medical context, cytoprotective agents are often used to protect tissues and organs from injury due to various factors like chemotherapy, radiation therapy, ischemia-reperfusion injury, or inflammation. These agents can include antioxidants, anti-inflammatory drugs, growth factors, and other compounds that help maintain cellular integrity and function.

Gamma-Butyrobetaine Dioxygenase (GBD, or also known as ETHE1) is an enzyme that catalyzes the conversion of gamma-butyrobetaine to succinate and hydrogen peroxide in the final step of L-carnitine biosynthesis. This mitochondrial matrix enzyme requires iron (Fe2+) as a cofactor for its activity. Deficiency or mutations in this enzyme can lead to a rare genetic disorder called "ethylmalonic aciduria and combined oxidative phosphorylation deficiency type 6" (ETHE1), which is characterized by the accumulation of ethylmalonic acid, gamma-butyrobetaine, and other organic acids in body fluids.

Copper is a chemical element with the symbol Cu (from Latin: *cuprum*) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. Copper is found as a free element in nature, and it is also a constituent of many minerals such as chalcopyrite and bornite.

In the human body, copper is an essential trace element that plays a role in various physiological processes, including iron metabolism, energy production, antioxidant defense, and connective tissue synthesis. Copper is found in a variety of foods, such as shellfish, nuts, seeds, whole grains, and organ meats. The recommended daily intake of copper for adults is 900 micrograms (mcg) per day.

Copper deficiency can lead to anemia, neutropenia, impaired immune function, and abnormal bone development. Copper toxicity, on the other hand, can cause nausea, vomiting, abdominal pain, diarrhea, and in severe cases, liver damage and neurological symptoms. Therefore, it is important to maintain a balanced copper intake through diet and supplements if necessary.

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.

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.

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.

Animal disease models are specialized animals, typically rodents such as mice or rats, that have been genetically engineered or exposed to certain conditions to develop symptoms and physiological changes similar to those seen in human diseases. These models are used in medical research to study the pathophysiology of diseases, identify potential therapeutic targets, test drug efficacy and safety, and understand disease mechanisms.

The genetic modifications can include knockout or knock-in mutations, transgenic expression of specific genes, or RNA interference techniques. The animals may also be exposed to environmental factors such as chemicals, radiation, or infectious agents to induce the disease state.

Examples of animal disease models include:

1. Mouse models of cancer: Genetically engineered mice that develop various types of tumors, allowing researchers to study cancer initiation, progression, and metastasis.
2. Alzheimer's disease models: Transgenic mice expressing mutant human genes associated with Alzheimer's disease, which exhibit amyloid plaque formation and cognitive decline.
3. Diabetes models: Obese and diabetic mouse strains like the NOD (non-obese diabetic) or db/db mice, used to study the development of type 1 and type 2 diabetes, respectively.
4. Cardiovascular disease models: Atherosclerosis-prone mice, such as ApoE-deficient or LDLR-deficient mice, that develop plaque buildup in their arteries when fed a high-fat diet.
5. Inflammatory bowel disease models: Mice with genetic mutations affecting intestinal barrier function and immune response, such as IL-10 knockout or SAMP1/YitFc mice, which develop colitis.

Animal disease models are essential tools in preclinical research, but it is important to recognize their limitations. Differences between species can affect the translatability of results from animal studies to human patients. Therefore, researchers must carefully consider the choice of model and interpret findings cautiously when applying them to human diseases.

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.

Alanine transaminase (ALT) is a type of enzyme found primarily in the cells of the liver and, to a lesser extent, in the cells of other tissues such as the heart, muscles, and kidneys. Its primary function is to catalyze the reversible transfer of an amino group from alanine to another alpha-keto acid, usually pyruvate, to form pyruvate and another amino acid, usually glutamate. This process is known as the transamination reaction.

When liver cells are damaged or destroyed due to various reasons such as hepatitis, alcohol abuse, nonalcoholic fatty liver disease, or drug-induced liver injury, ALT is released into the bloodstream. Therefore, measuring the level of ALT in the blood is a useful diagnostic tool for evaluating liver function and detecting liver damage. Normal ALT levels vary depending on the laboratory, but typically range from 7 to 56 units per liter (U/L) for men and 6 to 45 U/L for women. Elevated ALT levels may indicate liver injury or disease, although other factors such as muscle damage or heart disease can also cause elevations in ALT.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Catalytic antibodies, also known as abzymes or catalytic immune proteins, are a type of antibody that possesses enzymatic activity. They are capable of accelerating specific chemical reactions in a manner similar to traditional enzymes. This unique property arises from the ability of certain antibodies to bind substrates and promote their conversion into products through a series of chemical transformations.

Catalytic antibodies are generated by immunizing an organism with a transition state analogue, a molecule that mimics the high-energy, transient structure of a substrate during a chemical reaction. The immune system recognizes this analogue as foreign and produces antibodies against it. Some of these antibodies will bind to the transition state analogue in a way that stabilizes its geometry and lowers the energy barrier for the conversion of the substrate into the product. This results in the formation of a catalytic antibody, which can then accelerate this specific chemical reaction when presented with the appropriate substrate.

These specialized antibodies have attracted significant interest in the fields of chemistry, biochemistry, and immunology due to their potential applications in various areas, including drug design, diagnostics, and environmental monitoring. However, it is important to note that catalytic antibodies are still a subject of ongoing research, and their use as practical tools in these applications is not yet widespread.

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.

Enzymes are complex proteins that act as catalysts to speed up chemical reactions in the body. They help to lower activation energy required for reactions to occur, thereby enabling the reaction to happen faster and at lower temperatures. Enzymes work by binding to specific molecules, called substrates, and converting them into different molecules, called products. This process is known as catalysis.

Enzymes are highly specific and will only catalyze one particular reaction with a specific substrate. The shape of the enzyme's active site, where the substrate binds, determines this specificity. Enzymes can be regulated by various factors such as temperature, pH, and the presence of inhibitors or activators. They play a crucial role in many biological processes, including digestion, metabolism, and DNA replication.

Trace elements are essential minerals that the body needs in very small or tiny amounts, usually less than 100 milligrams per day, for various biological processes. These include elements like iron, zinc, copper, manganese, fluoride, selenium, and iodine. They are vital for maintaining good health and proper functioning of the human body, but they are required in such minute quantities that even a slight excess or deficiency can lead to significant health issues.

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.

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.

Chinese herbal drugs, also known as traditional Chinese medicine (TCM), refer to a system of medicine that has been practiced in China for thousands of years. It is based on the belief that the body's vital energy, called Qi, must be balanced and flowing freely for good health. TCM uses various techniques such as herbal therapy, acupuncture, dietary therapy, and exercise to restore balance and promote healing.

Chinese herbal drugs are usually prescribed in the form of teas, powders, pills, or tinctures and may contain one or a combination of herbs. The herbs used in Chinese medicine are typically derived from plants, minerals, or animal products. Some commonly used Chinese herbs include ginseng, astragalus, licorice root, and cinnamon bark.

It is important to note that the use of Chinese herbal drugs should be under the guidance of a qualified practitioner, as some herbs can interact with prescription medications or have side effects. Additionally, the quality and safety of Chinese herbal products can vary widely depending on the source and manufacturing process.

Northern blotting is a laboratory technique used in molecular biology to detect and analyze specific RNA molecules (such as mRNA) in a mixture of total RNA extracted from cells or tissues. This technique is called "Northern" blotting because it is analogous to the Southern blotting method, which is used for DNA detection.

The Northern blotting procedure involves several steps:

1. Electrophoresis: The total RNA mixture is first separated based on size by running it through an agarose gel using electrical current. This separates the RNA molecules according to their length, with smaller RNA fragments migrating faster than larger ones.

2. Transfer: After electrophoresis, the RNA bands are denatured (made single-stranded) and transferred from the gel onto a nitrocellulose or nylon membrane using a technique called capillary transfer or vacuum blotting. This step ensures that the order and relative positions of the RNA fragments are preserved on the membrane, similar to how they appear in the gel.

3. Cross-linking: The RNA is then chemically cross-linked to the membrane using UV light or heat treatment, which helps to immobilize the RNA onto the membrane and prevent it from washing off during subsequent steps.

4. Prehybridization: Before adding the labeled probe, the membrane is prehybridized in a solution containing blocking agents (such as salmon sperm DNA or yeast tRNA) to minimize non-specific binding of the probe to the membrane.

5. Hybridization: A labeled nucleic acid probe, specific to the RNA of interest, is added to the prehybridization solution and allowed to hybridize (form base pairs) with its complementary RNA sequence on the membrane. The probe can be either a DNA or an RNA molecule, and it is typically labeled with a radioactive isotope (such as ³²P) or a non-radioactive label (such as digoxigenin).

6. Washing: After hybridization, the membrane is washed to remove unbound probe and reduce background noise. The washing conditions (temperature, salt concentration, and detergent concentration) are optimized based on the stringency required for specific hybridization.

7. Detection: The presence of the labeled probe is then detected using an appropriate method, depending on the type of label used. For radioactive probes, this typically involves exposing the membrane to X-ray film or a phosphorimager screen and analyzing the resulting image. For non-radioactive probes, detection can be performed using colorimetric, chemiluminescent, or fluorescent methods.

8. Data analysis: The intensity of the signal is quantified and compared to controls (such as housekeeping genes) to determine the relative expression level of the RNA of interest. This information can be used for various purposes, such as identifying differentially expressed genes in response to a specific treatment or comparing gene expression levels across different samples or conditions.

Spermatozoa are the male reproductive cells, or gametes, that are produced in the testes. They are microscopic, flagellated (tail-equipped) cells that are highly specialized for fertilization. A spermatozoon consists of a head, neck, and tail. The head contains the genetic material within the nucleus, covered by a cap-like structure called the acrosome which contains enzymes to help the sperm penetrate the female's egg (ovum). The long, thin tail propels the sperm forward through fluid, such as semen, enabling its journey towards the egg for fertilization.

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.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

'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.

Organ size refers to the volume or physical measurement of an organ in the body of an individual. It can be described in terms of length, width, and height or by using specialized techniques such as imaging studies (like CT scans or MRIs) to determine the volume. The size of an organ can vary depending on factors such as age, sex, body size, and overall health status. Changes in organ size may indicate various medical conditions, including growths, inflammation, or atrophy.

Glutathione peroxidase 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 ... Glutathione peroxidase (GPx) (EC 1.11.1.9) is the general name of an enzyme family with peroxidase activity whose main ... eight different isoforms of glutathione peroxidase (GPx1-8) have been identified in humans. The main reaction that glutathione ...
In this context, the extracellular antioxidant system, comprised primarily of glutathione and glutathione peroxidase, is ... The regulation and role of extracellular glutathione peroxidase Antioxid Redox Signal. 2005 Jan-Feb;7(1-2):72-9. doi: 10.1089/ ... Induction of extracellular glutathione peroxidase occurs in airway inflammation and undoubtedly plays an important defense ...
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 ... GSH peroxidase contains one selenocysteine residue per .... * NM_001329455.2 → NP_001316384.1 glutathione peroxidase 1 isoform ... GSH_Peroxidase; Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of ...
Protein target information for Glutathione peroxidase (pig). Find diseases associated with this biological target and compounds ...
Peroxidase 4/GPX4 products for your research including Glutathione Peroxidase 4/GPX4 Small Molecules and Glutathione Peroxidase ... Glutathione Peroxidase 4/GPX4: Products. Glutathione Peroxidase 4 (GPX4; also known as PHGPx) is a monomeric, 21 kDa member of ... the glutathione peroxidase family of proteins. It is widely expressed and serves to both protect cell membranes from ...
Selenium and glutathione peroxidase (EC 1.11.1.9) in blood components of New Zealand women - Volume 69 Issue 2 ... Antihuman plasma glutathione peroxidase antibodies: immunologic investigations to determine plasma glutathione peroxidase ... Tarp, U., Hansen, J. C., Overvad, K., Thorling, E. B., Tarp, B. D. & Graudal, H. (1987). Glutathione peroxidase activity in ... Whanger, P. D., Beilstein, M. A., Thomson, C. D., Robinson, M. F. & Howe, M. (1988). Blood selenium and glutathione peroxidase ...
Protein target information for Glutathione peroxidase (Bacteroides thetaiotaomicron VPI-5482). Find diseases associated with ...
"Glutathione Peroxidase" by people in this website by year, and whether "Glutathione Peroxidase" was a major or minor topic of ... "Glutathione Peroxidase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? An ... Below are the most recent publications written about "Glutathione Peroxidase" by people in Profiles. ...
Glutathione may be useful for monitoring melatonins protective role on cell damage. ... Results: Melatonin caused an increase in glutathione level, the activity of glutathione peroxidase as well as glutathione ... The effect of melatonin on glutathione and glutathione transferase and glutathione peroxidase activities in the mouse liver and ... Objectives: The changes in reduced glutathione (GSH), activity of glutathione transferase (GST) and glutathione peroxidase ( ...
piR-31470 epigenetically suppresses the expression of glutathione S-transferase pi 1 in prostate cancer via DNA methylation.. ... Glucose metabolism and pyruvate carboxylase enhance glutathione synthesis and restrict oxidative stress in pancreatic islets.. ...
Glutathione peroxidase 4 (GPX4) is an essential regulator of ferroptotic cancer cell death by virtue of its ability to scavenge ... Activity of glutathione peroxidase (GPx). For measuring GPx activity, we used the conventional spectrophotometry method (Cayman ... paired with oxidized glutathione (GSSG) recovery by consumption of NADPH and glutathione reductase activity. The oxidation of ... Immunohistochemistry was performed on deparaffinized sections using the avidin-biotin-peroxidase complex methods (ABC-Elite kit ...
Involved in glutathione peroxidase activity. Specific Function. May constitute a glutathione peroxidase-like protective system ... Avery, A. M., Avery, S. V. (2001). "Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases ...
Glutathione peroxidase is the catalyst for glutathione (GSH) converting hydrogen peroxide (H2O2). to water (H2O). ... Colorimetric assay kit used to test for glutathione peroxidase (GPX) activity in multiple species and sample types. ... Can Glutathione Peroxidase (GPX) be detected in cell culture supernatant? Can Glutathione Peroxidase (GPX) be detected in cell ... Human Cellular Glutathione Peroxidase (cGPx or GPX1) ELISA Kit. Glutathione Reductase (GR) Assay Kit: 192 Tests. Glutathione ( ...
The Effect Of Temperature On Glutathione Peroxidase From Fish. Project Material in PDF & Doc ... 2.3 GLUTATHIONE PEROXIDASE (GPX) AND FISH …………………...14. 2.4 THE EFFECT OF TEMPERATURE ON GLUTATHIONE PEROXIDASE (GPX) ACTIVITY ... Glutathione peroxidase was extracted and purified from the liver of the fish using the purification method of Ezeet al(2010). ... Glutathione Peroxidase (GPx) family of enzymes plays important roles in the protection of organisms from oxidative damage. GPx ...
Mouse GPX1(Glutathione Peroxidase 1) ELISA Kit. Mouse GPX1(Glutathione Peroxidase 1) ELISA Kit ... Description: A sandwich ELISA kit for detection of Glutathione Peroxidase 1 from Mouse in samples from blood, serum, plasma, ... Description: A sandwich ELISA kit for quantitative measurement of Mouse GPX1 (Glutathione Peroxidase 1) in samples from Serum, ... Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Glutathione Peroxidase 1 ...
Glutathione Peroxidase (RANSEL). Glutathione Peroxidase is an antioxidant enzyme that helps protect the body from free radicals ... such as glutathione peroxidase, to function correctly.. The Randox Ransel test is used to measure glutathione peroxidase ... Glutathione Peroxidase (Ransel). Total Protein. Aspartate Aminotransferase (AST). Cholinesterase (Butyryl). Iron. Triglycerides ...
Glutathione reductase activity (p=0.05) and glutathione peroxidase activity (p=0 065) were significantly associated with ARMD ... The relation of glutathione reductase and glutathione peroxidase activity to ARMD merits further study. ... Low Glutathione Reductase and Peroxidase Activity in Age-Related Macular Degeneration. *Post author:2by2host ... The activities of glutathione peroxidase (p=018) and erythrocyte superoxide dismutase (p=029) were similar between the two ...
Its major role is its integration into the important enzyme called "Glutathione Peroxidase". ... Cellular glutathione production still requires the precursors found in Immunocal. Once produced by the cell, the glutathione ... It is the best glutathione solution; Immunocal provides the building blocks for the production of glutathione and the Booster ... The Nrf2 gene is a gene (piece of DNA code) that enhances glutathione and antioxidant metabolism. ...
Its major role is its integration into the important enzyme called "Glutathione Peroxidase". ... Cellular glutathione production still requires the precursors found in Immunocal. Once produced by the cell, the glutathione ... It is the best glutathione solution; Immunocal provides the building blocks for the production of glutathione and the Booster ... The Nrf2 gene is a gene (piece of DNA code) that enhances glutathione and antioxidant metabolism. ...
Native specific activity of glutathione peroxidase (GPx-1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and ... Phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis nuclei is bound to chromatin. Biochem Mol Meed. 1996 ; ... Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid ... The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of ...
... glutathione peroxidase 1; HMGCS/HMGCR, hydroxymethylglutaryl-CoA synthase/reductase; LDLR, low-density lipoprotein receptor; ... Hepatocyte glutathione peroxidase-1 deficiency improves hepatic glucose metabolism and decreases steatohepatitis in mice. ... glutathione peroxidase 1; LPIN, lipin; MTTP, microsomal triglyceride transfer protein; PPARg2, peroxisome proliferator- ... High-fat-fed obese glutathione peroxidase 1-deficient mice exhibit defective insulin secretion but protection from hepatic ...
... glutathione peroxidase (GPx), glutathione reductase, glutathione S-transferase (GST), superoxide dismutase (SOD), catalase, ... Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon ... glutathione, ubiquinone, thioredoxin and urate) that work synergically. The human body also has proteins (transferrin, ferritin ...
Synthesis and glutathione peroxidase (GPx)-like activity of selenocystine (SeC) bioconjugates of biotin and lipoic acid Authors ...
K00432 E1.11.1.9; glutathione peroxidase. 1.00. 1.37. 1.32. evm.model.LG03.168. K00026 MDH2; malate dehydrogenase. 1.00. 1.10. ... including upregulated expression of ascorbate peroxidase, superoxide dismutase, and glutathione reductase (Table 3), which are ... K00383 GSR, gor; glutathione reductase (NADPH). 1.00. 1.22. 1.48. evm.model.LG03.1372. K01919 gshA; glutamate-cysteine ligase. ... Li, K.; Pang, C.H.; Ding, F.; Sui, N.; Feng, Z.T.; Wang, B.S. Overexpression of Suaeda salsa stroma ascorbate peroxidase in ...
... glutathione peroxidase (GSH-PX), and malondialdehyde (MDA) in blood were determined.,i, Results,/i,. While an increased time to ... versus the PEO group; EOM: essential oil mixture; PEO: peppermint essential oil; GSH-PX: glutathione peroxidase. ... glutathione peroxidase (GSH-PX), and malondialdehyde (MDA) in blood were determined. Results. While an increased time to ... glutathione peroxidase (GSH-PX) kit, and malondialdehyde (MDA) kit were from Nanjing Jiancheng Biotechnology Institute (Nanjing ...
... and glutathione peroxidase (GPx) activities), and prooxidant enzymes (NADPH oxidase and xanthine oxidase (XO) activities, ... Glutathione peroxidase (GPx) activity was significantly higher in the HIIT (. ) than in the MICT (2.14 ± 0.45 μmol·min-1g-1) ... and glutathione peroxidase (GPx) activities), and prooxidant enzymes (NADPH oxidase and xanthine oxidase (XO) activities, ... "Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase," The Journal of Laboratory ...

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