Glutathione. Medical search

A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9.

Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.

A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.

One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.

A synthetic amino acid that depletes glutathione by irreversibly inhibiting gamma-glutamylcysteine synthetase. Inhibition of this enzyme is a critical step in glutathione biosynthesis. It has been shown to inhibit the proliferative response in human T-lymphocytes and inhibit macrophage activation. (J Biol Chem 1995;270(33):1945-7)

A glutathione transferase that catalyzes the conjugation of electrophilic substrates to GLUTATHIONE. This enzyme has been shown to provide cellular protection against redox-mediated damage by FREE RADICALS.

One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.

A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.

A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).

Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

Compounds containing the -SH radical.

An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of GLUTATHIONE PEROXIDASE.

An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.

The N-acetyl derivative of CYSTEINE. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates.

An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.

An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1.

A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.

A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.

The dialdehyde of malonic acid.

The rate dynamics in chemical or physical systems.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.

A cyclized derivative of L-GLUTAMIC ACID. Elevated blood levels may be associated with problems of GLUTAMINE or GLUTATHIONE metabolism.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.

Low-molecular-weight end products, probably malondialdehyde, that are formed during the decomposition of lipid peroxidation products. These compounds react with thiobarbituric acid to form a fluorescent red adduct.

Electron-accepting molecules in chemical reactions in which electrons are transferred from one molecule to another (OXIDATION-REDUCTION).

A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.

Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.

A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant.

A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed)

A compound that inhibits symport of sodium, potassium, and chloride primarily in the ascending limb of Henle, but also in the proximal and distal tubules. This pharmacological action results in excretion of these ions, increased urinary output, and reduction in extracellular fluid. This compound has been classified as a loop or high ceiling diuretic.

Peroxides produced in the presence of a free radical by the oxidation of unsaturated fatty acids in the cell in the presence of molecular oxygen. The formation of lipid peroxides results in the destruction of the original lipid leading to the loss of integrity of the membranes. They therefore cause a variety of toxic effects in vivo and their formation is considered a pathological process in biological systems. Their formation can be inhibited by antioxidants, such as vitamin E, structural separation or low oxygen tension.

A direct-acting oxidative stress-inducing agent used to examine the effects of oxidant stress on Ca(2+)-dependent signal transduction in vascular endothelial cells. It is also used as a catalyst in polymerization reactions and to introduce peroxy groups into organic molecules.

A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.

Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

An enzyme that catalyzes the interconversion of methylglyoxal and lactate, with glutathione serving as a coenzyme. EC 4.4.1.5.

A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5

Organic compounds containing a carbonyl group in the form -CHO.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.

Analgesic antipyretic derivative of acetanilide. It has weak anti-inflammatory properties and is used as a common analgesic, but may cause liver, blood cell, and kidney damage.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.

The relationship between the dose of an administered drug and the response of the organism to the drug.

Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.

A selenium compound with the molecular formula H2SO3. It used as a source of SELENIUM, especially for patients that develop selenium deficiency following prolonged PARENTERAL NUTRITION.

A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.

Substances that influence the course of a chemical reaction by ready combination with free radicals. Among other effects, this combining activity protects pancreatic islets against damage by cytokines and prevents myocardial and pulmonary perfusion injuries.

Drugs that are chemically similar to naturally occurring metabolites, but differ enough to interfere with normal metabolic pathways. (From AMA Drug Evaluations Annual, 1994, p2033)

Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Organic compounds which contain selenium as an integral part of the molecule.

Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.

The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.

Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

Established cell cultures that have the potential to propagate indefinitely.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

A basic-leucine zipper transcription factor that was originally described as a transcriptional regulator controlling expression of the BETA-GLOBIN gene. It may regulate the expression of a wide variety of genes that play a role in protecting cells from oxidative damage.

Organic compounds with the general formula R-NCS.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

A generic descriptor for all TOCOPHEROLS and TOCOTRIENOLS that exhibit ALPHA-TOCOPHEROL activity. By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

An effective soil fumigant, insecticide, and nematocide. In humans, it causes severe burning of skin and irritation of the eyes and respiratory tract. Prolonged inhalation may cause liver necrosis. It is also used in gasoline. Members of this group have caused liver and lung cancers in rodents. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), 1,2-dibromoethane may reasonably be anticipated to be a carcinogen.

The disodium salt of selenious acid. It is used therapeutically to supply the trace element selenium and is prepared by the reaction of SELENIUM DIOXIDE with SODIUM HYDROXIDE.

Mixture of 2- and 3-tert-butyl-4-methoxyphenols that is used as an antioxidant in foods, cosmetics, and pharmaceuticals.

A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.

Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.

Proteins prepared by recombinant DNA technology.

A chlorinated hydrocarbon that has been used as an inhalation anesthetic and acts as a narcotic in high concentrations. Its primary use is as a solvent in manufacturing and food technology.

Elements of limited time intervals, contributing to particular results or situations.

An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.

A potent hepatotoxic and hepatocarcinogenic mycotoxin produced by the Aspergillus flavus group of fungi. It is also mutagenic, teratogenic, and causes immunosuppression in animals. It is found as a contaminant in peanuts, cottonseed meal, corn, and other grains. The mycotoxin requires epoxidation to aflatoxin B1 2,3-oxide for activation. Microsomal monooxygenases biotransform the toxin to the less toxic metabolites aflatoxin M1 and Q1.

Peptides composed of two amino acid units.

An extracellular selenoprotein that contains most of the SELENIUM in PLASMA. Selenoprotein P functions as an antioxidant and appears to transport selenium from the LIVER to peripheral tissues.

The appearance of carbonyl groups (such as aldehyde or ketone groups) in PROTEINS as the result of several oxidative modification reactions. It is a standard marker for OXIDATIVE STRESS. Carbonylated proteins tend to be more hydrophobic and resistant to proteolysis.

A spectrum of clinical liver diseases ranging from mild biochemical abnormalities to ACUTE LIVER FAILURE, caused by drugs, drug metabolites, and chemicals from the environment.

Chemical substances that are foreign to the biological system. They include naturally occurring compounds, drugs, environmental agents, carcinogens, insecticides, etc.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

Derivatives of benzene in which one or more hydrogen atoms on the benzene ring are replaced by bromine atoms.

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.

A phenolphthalein that is used as a diagnostic aid in hepatic function determination.

A sequence-related subfamily of ATP-BINDING CASSETTE TRANSPORTERS that actively transport organic substrates. Although considered organic anion transporters, a subset of proteins in this family have also been shown to convey drug resistance to neutral organic drugs. Their cellular function may have clinical significance for CHEMOTHERAPY in that they transport a variety of ANTINEOPLASTIC AGENTS. Overexpression of proteins in this class by NEOPLASMS is considered a possible mechanism in the development of multidrug resistance (DRUG RESISTANCE, MULTIPLE). Although similar in function to P-GLYCOPROTEINS, the proteins in this class share little sequence homology to the p-glycoprotein family of proteins.

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.

Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard.

A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.

Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.

Poly-glutathione peptides composed of (Glu-Cys)n-Gly where n is two to seven. They are biosynthesized by glutathione gamma-glutamylcysteinyltransferase and are found in many PLANTS; YEASTS; and algae. They sequester HEAVY METALS.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

The regular and simultaneous occurrence in a single interbreeding population of two or more discontinuous genotypes. The concept includes differences in genotypes ranging in size from a single nucleotide site (POLYMORPHISM, SINGLE NUCLEOTIDE) to large nucleotide sequences visible at a chromosomal level.

Azoles with an OXYGEN and a NITROGEN next to each other at the 1,2 positions, in contrast to OXAZOLES that have nitrogens at the 1,3 positions.

A non-selective post-emergence, translocated herbicide. According to the Seventh Annual Report on Carcinogens (PB95-109781, 1994) this substance may reasonably be anticipated to be a carcinogen. (From Merck Index, 12th ed) It is an irreversible inhibitor of CATALASE, and thus impairs activity of peroxisomes.

Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.

An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.

Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.

An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse.

Diminished or failed response of an organism, disease or tissue to the intended effectiveness of a chemical or drug. It should be differentiated from DRUG TOLERANCE which is the progressive diminution of the susceptibility of a human or animal to the effects of a drug, as a result of continued administration.

Reduced (protonated) form of THIAZOLES. They can be oxidized to THIAZOLIDINEDIONES.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A synthetic naphthoquinone without the isoprenoid side chain and biological activity, but can be converted to active vitamin K2, menaquinone, after alkylation in vivo.

A sulfur-containing essential L-amino acid that is important in many body functions.

Substances that increase the risk of NEOPLASMS in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Hydrolyzes pyroglutamic acid in the presence of ATP to glutamate plus ADP and inorganic phosphate. Deficiency leads to pyroglutamic acidurea.

A subtype of thioredoxin reductase found primarily in the CYTOSOL.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

The conjugation product of LEUKOTRIENE A4 and glutathione. It is the major arachidonic acid metabolite in macrophages and human mast cells as well as in antigen-sensitized lung tissue. It stimulates mucus secretion in the lung, and produces contractions of nonvascular and some VASCULAR SMOOTH MUSCLE. (From Dictionary of Prostaglandins and Related Compounds, 1990)

Organic derivatives of thiocyanic acid which contain the general formula R-SCN.

An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.

Experimentally induced tumors of the LIVER.

A dietary deficiency of riboflavin causing a syndrome chiefly marked by cheilitis, angular stomatitis, glossitis associated with a purplish red or magenta-colored tongue that may show fissures, corneal vascularization, dyssebacia, and anemia. (Dorland, 27th ed)

A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.

An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.

A sulfhydryl reagent that is widely used in experimental biochemical studies.

A poisonous dipyridilium compound used as contact herbicide. Contact with concentrated solutions causes irritation of the skin, cracking and shedding of the nails, and delayed healing of cuts and wounds.

Inorganic compounds that contain selenium as an integral part of the molecule.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

The reversibly oxidized form of ascorbic acid. It is the lactone of 2,3-DIKETOGULONIC ACID and has antiscorbutic activity in man on oral ingestion.

The conjugation of exogenous substances with various hydrophilic substituents to form water soluble products that are excretable in URINE. Phase II modifications include GLUTATHIONE conjugation; ACYLATION; and AMINATION. Phase II enzymes include GLUTATHIONE TRANSFERASE and GLUCURONOSYLTRANSFERASE. In a sense these reactions detoxify phase I reaction products.

An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.

Diagnostic aid in pancreas function determination.

Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.

Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.

Either of the pair of organs occupying the cavity of the thorax that effect the aeration of the blood.

A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.

A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.

A quinone fungicide used for treatment of seeds and foliage.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

Synthetic or natural substances which are given to prevent a disease or disorder or are used in the process of treating a disease or injury due to a poisonous agent.

A cell-cycle phase nonspecific alkylating antineoplastic agent. It is used in the treatment of brain tumors and various other malignant neoplasms. (From Martindale, The Extra Pharmacopoeia, 30th ed, p462) This substance may reasonably be anticipated to be a carcinogen according to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985). (From Merck Index, 11th ed)

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

Transport proteins that carry specific substances in the blood or across cell membranes.

An emulsifying agent produced in the LIVER and secreted into the DUODENUM. Its composition includes BILE ACIDS AND SALTS; CHOLESTEROL; and ELECTROLYTES. It aids DIGESTION of fats in the duodenum.

A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.

The main structural component of the LIVER. They are specialized EPITHELIAL CELLS that are organized into interconnected plates called lobules.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

The definition of DILI has been revised several times over the years, but the most recent definition was published in 2013 by the International Consortium for DILI Research (ICDCR). According to this definition, DILI is defined as:

"A clinically significant alteration in liver function that is caused by a medication or other exogenous substance, and is not related to underlying liver disease. The alteration may be biochemical, morphological, or both, and may be acute or chronic."

The ICDCR definition includes several key features of DILI, including:

1. Clinically significant alteration in liver function: This means that the liver damage must be severe enough to cause symptoms or signs of liver dysfunction, such as jaundice, nausea, vomiting, or abdominal pain.
2. Caused by a medication or other exogenous substance: DILI is triggered by exposure to certain drugs or substances that are not related to underlying liver disease.
3. Not related to underlying liver disease: This means that the liver damage must not be caused by an underlying condition such as hepatitis B or C, alcoholic liver disease, or other genetic or metabolic disorders.
4. May be acute or chronic: DILI can occur as a sudden and severe injury (acute DILI) or as a slower and more insidious process (chronic DILI).

The ICDCR definition provides a standardized way of defining and diagnosing DILI, which is important for clinicians and researchers to better understand the cause of liver damage in patients who are taking medications. It also helps to identify the drugs or substances that are most likely to cause liver injury and to develop strategies for preventing or treating DILI.

Examples of experimental liver neoplasms include:

1. Hepatocellular carcinoma (HCC): This is the most common type of primary liver cancer and can be induced experimentally by injecting carcinogens such as diethylnitrosamine (DEN) or dimethylbenz(a)anthracene (DMBA) into the liver tissue of animals.
2. Cholangiocarcinoma: This type of cancer originates in the bile ducts within the liver and can be induced experimentally by injecting chemical carcinogens such as DEN or DMBA into the bile ducts of animals.
3. Hepatoblastoma: This is a rare type of liver cancer that primarily affects children and can be induced experimentally by administering chemotherapy drugs to newborn mice or rats.
4. Metastatic tumors: These are tumors that originate in other parts of the body and spread to the liver through the bloodstream or lymphatic system. Experimental models of metastatic tumors can be studied by injecting cancer cells into the liver tissue of animals.

The study of experimental liver neoplasms is important for understanding the underlying mechanisms of liver cancer development and progression, as well as identifying potential therapeutic targets for the treatment of this disease. Animal models can be used to test the efficacy of new drugs or therapies before they are tested in humans, which can help to accelerate the development of new treatments for liver cancer.

Causes and risk factors:

1. Poor diet: A diet that is deficient in riboflavin can lead to a deficiency. Common culprits include a lack of dairy products, eggs, and leafy green vegetables.
2. Malabsorption: Certain medical conditions, such as celiac disease, Crohn's disease, and pancreatic insufficiency, can lead to malabsorption of riboflavin and other nutrients.
3. Alcoholism: Alcohol can interfere with the absorption of riboflavin and other B vitamins.
4. Pregnancy and lactation: Pregnant and breastfeeding women have a higher demand for riboflavin, and may be at risk for deficiency if their diet does not provide enough.
5. Genetic disorders: Certain genetic disorders, such as fibroblastosis, can lead to riboflavin deficiency.

Symptoms of riboflavin deficiency can include:

1. Cracks in the corners of the mouth (cheilosis)
2. Redness and swelling of the tongue
3. Dry, itchy skin
4. Fatigue
5. Headaches
6. Dizziness
7. Muscle weakness
8. Seizures (in severe cases)

Diagnosis of riboflavin deficiency is typically made based on a combination of symptoms, physical examination findings, and laboratory tests. Treatment involves supplementation with riboflavin, which can help to resolve symptoms and prevent complications.

In summary, riboflavin deficiency is a condition where the body does not have enough riboflavin, leading to a range of symptoms and potential health complications. It is important for individuals at risk for deficiency to be aware of the signs and symptoms, and to seek medical attention if they suspect they may have a deficiency.

... exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within ... It is a cofactor and acts on glutathione peroxidase. Glutathione facilitates metabolism of xenobiotics. Glutathione S- ... Glutathione conjugates to NAPQI, and the resulting ensemble is excreted. Glutathione, along with oxidized glutathione (GSSG) ... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ...

https://en.wikipedia.org/wiki/Glutathione

... (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the ... For instance, glutathione peroxidases catalyze the oxidation of GSH to glutathione disulfide (GSSG) by reducing free radicals ... Glutathione synthetase deficiency Glutathione Liver Sulfur Metabolism Gogos A, Shapiro L (Dec 2002). "Large conformational ... such as H2O2 or Glutathione S-transferases in the detoxification of xenobiotics. Glutathione synthetase is important for a ...

https://en.wikipedia.org/wiki/Glutathione_synthetase

It is also called citryl-glutathione thioesterhydrolase. Kielley WW, Bradley LB (1954). "Glutathione thiolesterase". J. Biol. ... The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction S-acylglutathione + H2O ⇌ {\displaystyle \ ... rightleftharpoons } glutathione + a carboxylate This enzyme belongs to the family of hydrolases, specifically those acting on ...

https://en.wikipedia.org/wiki/Glutathione_thiolesterase

... (GSSG) is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is ... Glutathione-ascorbate cycle Antioxidant Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711-60 ... This reaction is catalyzed by the enzyme glutathione reductase. Antioxidant enzymes, such as glutathione peroxidases and ... GSSG, along with glutathione and S-nitrosoglutathione (GSNO), have been found to bind to the glutamate recognition site of the ...

https://en.wikipedia.org/wiki/Glutathione_disulfide

Glutathione+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.19). ... Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the ... "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24 ... a key enzyme in glutathione metabolism, and its reaction intermediate". Proceedings of the National Academy of Sciences of the ...

https://en.wikipedia.org/wiki/Glutathione_hydrolase

... was discovered in 1957 by Gordon C. Mills. Activity of glutathione peroxidase is measured ... Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially ... Zakowski JJ, Tappel AL (September 1978). "A semiautomated system for measurement of glutathione in the assay of glutathione ... RSeH Glutathione reductase then reduces the oxidized glutathione to complete the cycle: GS-SG + NADPH + H+ → 2 GSH + NADP+. ...

https://en.wikipedia.org/wiki/Glutathione_peroxidase

... (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione ( ... In plants, reduced glutathione participates in the glutathione-ascorbate cycle in which reduced glutathione reduces ... Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the ... In particular, glutathione reductase appears to be a good target for anti-malarials, as the glutathione reductase of the ...

https://en.wikipedia.org/wiki/Glutathione_reductase

In enzymology, a glutathione oxidase (EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction 2 glutathione + O2 ⇌ {\ ... The systematic name of this enzyme class is glutathione:oxygen oxidoreductase. This enzyme participates in glutathione ... displaystyle \rightleftharpoons } glutathione disulfide + H2O2 Thus, the two substrates of this enzyme are glutathione and O2, ... Kusakabe H, Kuninaka A, Yoshino H (1982). "Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp ...

https://en.wikipedia.org/wiki/Glutathione_oxidase

"Erythrocyte glutathione synthetase deficiency leads not only to glutathione but also to glutathione-S-transferase deficiency". ... Glutathione synthetase deficiency can be classified into three types: mild, moderate and severe. Mild glutathione synthetase ... Glutathione helps prevent damage to cells by neutralizing harmful molecules generated during energy production. Glutathione ... This cycle is necessary for producing a molecule called glutathione. Glutathione protects cells from damage caused by unstable ...

https://en.wikipedia.org/wiki/Glutathione_synthetase_deficiency

Since glutathione, ascorbate and NADPH are present in high concentrations in plant cells it is assumed that the glutathione- ... yielding oxidized glutathione (GSSG). Finally GSSG is reduced by glutathione reductase (GR) using NADPH as the electron donor. ... such as glutathione S-transferase omega 1 or glutaredoxins. In plants, the glutathione-ascorbate cycle operates in the cytosol ... Thus ascorbate and glutathione are not consumed; the net electron flow is from NADPH to H2O2. The reduction of dehydroascorbate ...

https://en.wikipedia.org/wiki/Glutathione-ascorbate_cycle

In enzymology, a glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase. Other ... the two substrates of this enzyme are glutathione and [Glu(-Cys)]n-Gly, whereas its two products are Gly and [Glu(-Cys)]n+1-Gly ... are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)". Proc ...

https://en.wikipedia.org/wiki/Glutathione_gamma-glutamylcysteinyltransferase

NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione ... In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction CoA + glutathione + ... glutathione, and NADP+, whereas its 3 products are CoA-glutathione, NADPH, and H+. This enzyme belongs to the family of ... The systematic name of this enzyme class is glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include ...

https://en.wikipedia.org/wiki/CoA-glutathione_reductase

... (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase. This ... glutathione amide disulfide + NADH + H+ Glutathione amide reductase is a dimeric flavoprotein (FAD). Vergauwen B, Pauwels F, ... Glutathione+amide+reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.8.1). ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ...

https://en.wikipedia.org/wiki/Glutathione_amide_reductase

This enzyme participates in methionine metabolism and glutathione metabolism. Racker E (December 1955). "Glutathione- ... glutathione disulfide + 2 homocysteine Thus, the two substrates of this enzyme are glutathione and homocystine, whereas its two ... In enzymology, a glutathione-homocystine transhydrogenase (EC 1.8.4.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:homocystine oxidoreductase. ...

https://en.wikipedia.org/wiki/Glutathione—homocystine_transhydrogenase

... glutathione disulfide + ascorbate Thus, the two substrates of this enzyme are glutathione and dehydroascorbate, whereas its two ... In enzymology, a glutathione dehydrogenase (ascorbate) (EC 1.8.5.1) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:dehydroascorbate oxidoreductase. Other names in common use include ... Crook EM (March 1941). "The system dehydroascorbic acid-glutathione". The Biochemical Journal. 35 (3): 226-36. doi:10.1042/ ...

https://en.wikipedia.org/wiki/Glutathione_dehydrogenase_(ascorbate)

Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions ... Glutathione transferases play a key role in catalyzing such reactions. Bacterial glutathione transferases of all classes are ... A GST monomer binds a glutathione molecule to its N-terminal glutathione-binding site. On the adjacent hydrophobic alpha- ... After completion of this reaction, glutathione reductase recycles oxidized glutathione back to the reduced form so that it ...

https://en.wikipedia.org/wiki/Bacterial_glutathione_transferase

Affinity chromatography Bacterial glutathione transferase Glutathione S-transferase Mu 1 Glutathione S-transferase, C-terminal ... Overview of Glutathione S-Transferases Glutathione+S-Transferase at the US National Library of Medicine Medical Subject ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles ... "Glutathione S-transferase pull-down assays using dehydrated immobilized glutathione resin". Analytical Biochemistry. 322 (2): ...

https://en.wikipedia.org/wiki/Glutathione_S-transferase

... glutathione disulfide + 2 cysteine Thus, the two substrates of this enzyme are glutathione and cystine, whereas its two ... In enzymology, a glutathione-cystine transhydrogenase (EC 1.8.4.4) is an enzyme that catalyzes the chemical reaction 2 ... The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine ... This enzyme participates in cysteine metabolism and glutathione metabolism. Nagai S, Black S (1968). "A thiol-disulfide ...

https://en.wikipedia.org/wiki/Glutathione—cystine_transhydrogenase

... (EC 1.11.1.17) is an enzyme with systematic name glutathione amide:hydrogen-peroxide ... Glutathione+amide-dependent+peroxidase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ... This enzyme catalyses the following chemical reaction 2 glutathione amide + H2O2 ⇌ {\displaystyle \rightleftharpoons } ...

https://en.wikipedia.org/wiki/Glutathione_amide-dependent_peroxidase

... glutathione-coenzyme A glutathione disulfide transhydrogenase, glutathione coenzyme A-glutathione transhydrogenase, glutathione ... CoA-glutathione + glutathione Thus, the two substrates of this enzyme are CoA and glutathione disulfide, whereas its two ... a glutathione-CoA-glutathione transhydrogenase (EC 1.8.4.3) is an enzyme that catalyzes the chemical reaction CoA + glutathione ... coenzyme A-glutathione transhydrogenase, coenzyme A:oxidized-glutathione oxidoreductase, and coenzyme A:glutathione-disulfide ...

https://en.wikipedia.org/wiki/Glutathione—CoA-glutathione_transhydrogenase

... hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). This enzyme participates in glutathione metabolism. ... glutathione disulfide + lipid + 2 H2O Thus, the two substrates of this enzyme are glutathione and lipid hydroperoxide, whereas ... glutathione, (phospholipid hydroperoxide-reducing), phospholipid hydroperoxide glutathione peroxidase, ... In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical ...

https://en.wikipedia.org/wiki/Phospholipid-hydroperoxide_glutathione_peroxidase

... is an enzyme that in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTA1 glutathione S-transferase A1". Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA ... This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped ... 1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate ...

https://en.wikipedia.org/wiki/Glutathione_S-transferase_A1

... glutathione disulfide + protein-dithiol Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas ... glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione), GSH-insulin transhydrogenase, protein- ... This enzyme participates in glutathione metabolism. As of late 2007, only one structure has been solved for this class of ... In enzymology, a protein-disulfide reductase (glutathione) (EC 1.8.4.2) is an enzyme that catalyzes the chemical reaction 2 ...

https://en.wikipedia.org/wiki/Protein-disulfide_reductase_(glutathione)

The systematic name of this enzyme class is S-(hydroxymethyl)glutathione formaldehyde-lyase (glutathione-forming). Other names ... The enzyme S-(hydroxymethyl)glutathione synthase (EC 4.4.1.22) catalyzes the reaction S-(hydroxymethyl)glutathione ⇌ {\ ... Goenrich M, Bartoschek S, Hagemeier CH, Griesinger C, Vorholt JA (February 2002). "A glutathione-dependent formaldehyde- ... in common use include glutathione-dependent formaldehyde-activating enzyme, Gfa, and S-(hydroxymethyl)glutathione formaldehyde- ...

https://en.wikipedia.org/wiki/S-(hydroxymethyl)glutathione_synthase

... and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione. This enzyme belongs to the family of ... glutathione disulfide ⇌ {\displaystyle \rightleftharpoons } adenylyl sulfate + 2 glutathione The 3 substrates of this enzyme ... Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction AMP + sulfite + ... The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate- ...

https://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase_(glutathione)

... glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent ... In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction S ... The systematic name of this enzyme class is S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include ... Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF (2000). "Kinetic mechanism of human glutathione-dependent ...

https://en.wikipedia.org/wiki/S-(hydroxymethyl)glutathione_dehydrogenase

2 glutathione Thus, the two substrates of this enzyme are xanthine dehydrogenase and glutathione disulfide, whereas its two ... oxidized-glutathione), glutathione-dependent thiol:disulfide oxidoreductase, and thiol:disulfide oxidoreductase. This enzyme ... In enzymology, an enzyme-thiol transhydrogenase (glutathione-disulfide) (EC 1.8.4.7) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase. Other names in ...

https://en.wikipedia.org/wiki/Enzyme-thiol_transhydrogenase_(glutathione-disulfide)

... (gene name GSTM1) is a human glutathione S-transferase. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTM1 glutathione S-transferase M1". Engel LS, Taioli E, Pfeiffer R, Garcia-Closas M, Marcus PM, Lan Q, et al. ( ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 v t ... This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in ...

https://en.wikipedia.org/wiki/Glutathione_S-transferase_Mu_1

... is an enzyme that in humans is encoded by the MGST1 gene. The MAPEG family (Membrane- ... Cholon A, Giaccia AJ, Lewis AD (1992). "What role do glutathione S-transferases play in the cellular response to ionizing ... DeJong JL, Mohandas T, Tu CP (1990). "The gene for the microsomal glutathione S-transferase is on human chromosome 12". ... This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid ...

https://en.wikipedia.org/wiki/Microsomal_glutathione_S-transferase_1

... is a structural domain of glutathione S-transferase (GST). GST conjugates reduced ... GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol. Glutathione S- ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles ... The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed ...

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The oxidized disulfide form of glutathione was decreased and the glutathione redox ratio increased after treatment (P , 0.008 ... Efficacy of methylcobalamin and folinic acid treatment on glutathione redox status in children with autism.. James SJ, Melnyk S ... The 3-mo intervention resulted in significant increases in cysteine, cysteinylglycine, and glutathione concentrations (P , ... CONCLUSIONS: The significant improvements observed in transmethylation metabolites and glutathione redox status after treatment ...

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Life span profiles of glutathione and acetaminophen detoxification. Drug Metab Dispos. 1990 Nov-Dec18(6):882-7.PubMed ID1981532 ... At intervals for 24 hr, samples of blood and other tissues were obtained, processed, and analyzed for reduced GSH, glutathione ...

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Carbamazepine-Induced Liver Injury Requires CYP3A-Mediated Metabolism and Glutathione Depletion in Rats. Azumi Iida, Eita ... Carbamazepine-Induced Liver Injury Requires CYP3A-Mediated Metabolism and Glutathione Depletion in Rats ...

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Anti-apoptotic activity of the glutathione peroxidase homologue encoded by HIV-1. UNCG Author/Contributor (non-UNCG co-authors ... Anti-apoptotic activity of the glutathione peroxidase homologue encoded by HIV-1. PDF (Portable Document Format). 1117 KB. ... The third reading frame of the envelope gene from HIV-1 codes for a protein homologous to the human selenoprotein glutathione ... of cell death induced by the ROS donor tert-butylhydroperoxide was also observed in cells depleted from endogenous glutathione ...

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Harris M. J., Coggan M., Langton L., Wilson S. R., Board P. G. Polymorphism of the Pi class glutathione S-transferase in normal ... Hudson C. E., Kelly M. M., Schwartz D. A., Schofield D. A., DeHaven J. E., Schulte B. A., Norris J. S. Glutathione S- ... Harries L. W., Stubbins M. J., Forman D., Howard G. C., Wolf C. R. Identification of genetic polymorphisms at the glutathione S ... No Association between the I105V Polymorphism of the Glutathione S-Transferase P1 Gene (GSTP1) and Prostate Cancer Risk: A ...

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glutathione peroxidase 4b [Source:ZFIN;Acc:ZDB-GEN... [more]. gpx4a. 3.662e-60. 58.86. glutathione peroxidase 4a [Source:ZFIN; ... glutathione peroxidase 4a [Source:ZFIN;Acc:ZDB-GEN... [more]. gpx4b. 5.793e-40. 66.67. glutathione peroxidase 4b [Source:ZFIN; ... glutathione peroxidase 4b [Source:ZFIN;Acc:ZDB-GEN... [more]. gpx4a. 6.628e-49. 53.16. glutathione peroxidase 4a [Source:ZFIN; ... glutathione peroxidase 4b [Source:ZFIN;Acc:ZDB-GEN... [more]. gpx7. 3.103e-30. 43.75. glutathione peroxidase 7 [Source:ZFIN;Acc ...

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acts as the substrate for the enzyme glutathione peroxidase. (hindawi.com)
Dietary selenium is a potential major modulator of Hhe-induced myocardial fibrosis, since a major cellular defense against oxidant stress is the selenium requiring enzyme glutathione peroxidase- 1 (GPx-1). (nih.gov)
Intake of the dark roast CB most effectively improved the antioxidant status of erythrocytes: superoxide dismutase and glutathione peroxidase activity decreased by 5.8 and 15%, respectively, whereas tocopherol and total glutathione concentrations increased by 41 and 14%, respectively. (bottomlinefitness.com)
Other family members, demonstrating glutathione S-transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. (nih.gov)
The third reading frame of the envelope gene from HIV-1 codes for a protein homologous to the human selenoprotein glutathione peroxidase (GPX). (uncg.edu)
The present study focused on mapping polymorphism in an important antioxidant enzyme glutathione peroxidase 1 (GPx1) among osteoporosis and healthy Asian Indians. (who.int)

L-Glutathione is an antioxidant that our body produces from three basic amino acids that are found in our food. (streetdirectory.com)
Although glutathione plays an important role in the body as an antioxidant, supplementing with glutathione has not been shown to slow aging or benefit most people with conditions associated with reduced levels of glutathione, such as cancer, cataracts, HIV infection, and diabetes (although there may be a modest benefit among older people with type 2 diabetes). (consumerlab.com)
Glutathione is called an antioxidant because of its role in protecting cells from the damaging effects of these unstable molecules. (medlineplus.gov)
With a nickname like " the master antioxidant 1 ," glutathione is a one-of-a-kind bioactive that deserves your attention. (mindbodygreen.com)
Thing is, glutathione can only have its full impact if you've got ample amounts of it-and while your body can produce its own stash of the antioxidant (with some help from you in the form of a healthy diet and lifestyle), you might not be churning out enough to keep up with the stresses of modern living. (mindbodygreen.com)
Glutathione is an antioxidant that's made up of the three amino acids- glutamine, glycine, and cysteine 2 -all of which are rich in the mineral sulfur. (mindbodygreen.com)
The antioxidant functions of Glutathione Reduced include recycling vitamins E and C and serving as an antioxidant in all types of tissues. (needs.com)
The discovery of glutathione first was in 1888 by De-Rey-Pailhade, but its role as an antioxidant and detoxifier was not discovered until 30 years later. (naturalremedies.org)
Taking supplements such as acetylcysteine, which is an antioxidant that can regenerate glutathione within cells. (naturalremedies.org)
Another antioxidant to consider is the mineral selenium, which helps to boost glutathione production within the body. (naturalremedies.org)
Glutathione is the most prevalent antioxidant in the body and a key regulator of detoxification. (essentialformulas.com)
Glutathione (Reduced) - Reduced glutathione is involved in the synthesis and repair of DNA, and enhances the antioxidant activity of vitamin C, the transport of amino acids, and the detoxification of harmful compounds. (pureprescriptions.com)
Reduced glutathione is an antioxidant important for cellular health and liver function. (pureprescriptions.com)
Antioxidant Support: Glutathione is a key component of the antioxidant system, which protects the body from free radicals at the cellular level. (pureprescriptions.com)
Glutathione is an antioxidant and detoxifier. (nih.gov)

One Frontiers in Immunology study suggests that glutathione helps "fine-tune" our immune response 6 , helping the body to respond effectively when needed without kicking into unhelpful overdrive. (mindbodygreen.com)
Research suggests that glutathione taken orally is not well absorbed within the gastrointestinal tract. (naturalremedies.org)
It has resulted in the proposal of the ' Glutathione Deficiency Hypothesis ,' which suggests that glutathione deficiency is a primary cause of biological aging. (essentialformulas.com)

Glutathione and its precursors, Cysteine, Glycine and L-Glutamic Acid, are all readily available as food supplements in your local health food store. (streetdirectory.com)
Existing in almost every cell of the body, Glutathione is a small molecule made up of three amino acids: cysteine, glycine, and glutamic acid. (naturalremedies.org)
At intervals for 24 hr, samples of blood and other tissues were obtained, processed, and analyzed for reduced GSH, glutathione disulfide (GSSG), cysteine, and cystine using HPLC with dual electrochemical detection. (harvard.edu)

We have examined whether pentoxifylline ameliorates interstitial edema, inflammatory infiltrate, and glutathione depletion associated with cerulein-induced pancreatitis. (aspetjournals.org)
Cotreatment of animals with pentoxifylline significantly reduced cerulein-induced pancreatic inflammation and edema and attenuated the depletion of pancreatic glutathione and the increase in serum lipase activity, nitrate, and tumor necrosis factor-α levels. (aspetjournals.org)
Because glutathione is so critical to the health of every cell in the body, taking drugs that contain acetaminophen and the resulting depletion of glutathione can cause serious health problems for people of all ages. (essentialformulas.com)

Glutathione synthetase deficiency is a genetic metabolic disorder that affects the body's ability to produce an important substance called glutathione. (nih.gov)
People with Glutathione synthetase deficiency do not have enough of the molecule called glutathione synthetase, which helps the body produce glutathione. (nih.gov)
People with Glutathione synthetase deficiency can have mild, moderate, or severe disease. (nih.gov)
Glutathione synthetase deficiency is caused by genetic changes (pathogenic variantss) in the GSS gene. (nih.gov)
Diagnosis of a metabolic disorder such as Glutathione synthetase deficiency may be suspected when a doctor observes signs of the deficiency including metabolic acidosis. (nih.gov)
When Do Symptoms of Glutathione synthetase deficiency Begin? (nih.gov)
Glutathione synthetase deficiency is a disorder that prevents the production of an important molecule called glutathione. (medlineplus.gov)
Glutathione synthetase deficiency can be classified into three types: mild, moderate, and severe. (medlineplus.gov)
Mild glutathione synthetase deficiency usually results in the destruction of red blood cells (hemolytic anemia). (medlineplus.gov)
Individuals with moderate glutathione synthetase deficiency may experience symptoms beginning shortly after birth including hemolytic anemia, 5-oxoprolinuria, and elevated acidity in the blood and tissues (metabolic acidosis). (medlineplus.gov)
In addition to the features present in moderate glutathione synthetase deficiency, individuals affected by the severe form of this disorder may experience neurological symptoms. (medlineplus.gov)
Some people with severe glutathione synthetase deficiency also develop recurrent bacterial infections. (medlineplus.gov)
Glutathione synthetase deficiency is very rare. (medlineplus.gov)
Mutations in the GSS gene cause glutathione synthetase deficiency. (medlineplus.gov)
Mutations in the GSS gene prevent cells from making adequate levels of glutathione, leading to the signs and symptoms of glutathione synthetase deficiency. (medlineplus.gov)
Ben Ameur S, Aloulou H, Nasrallah F, Kamoun T, Kaabachi N, Hachicha M. Hemolytic anemia and metabolic acidosis: think about glutathione synthetase deficiency. (medlineplus.gov)
We report a patient with glutathione synthetase (GS) deficiency who developed acetaminophen-induced hepatotoxicity after a two-day treatment with regular doses of acetaminophen. (nih.gov)
In fact, researchers are concluding glutathione deficiency may play a role in patients with schizophrenia. (bottomlinefitness.com)

Ristoff E, Larsson A. Inborn errors in the metabolism of glutathione. (medlineplus.gov)
Glutathione metabolism and its implications for health. (medlineplus.gov)
Glutathione is important to intermediary metabolism, immune response, and overall health. (naturalremedies.org)
The MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family consists of six human proteins, two of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. (nih.gov)

Glutathione is also used in repairing cellular damage from harmful free radicals and reducing oxidative stress. (naturalremedies.org)
Polymorphisms in glutathione S-transferase (GST) genes can increase oxidative stress, which may affect cancer prognosis. (nih.gov)
Glutathione was implicated in several neuropsychiatric diseases related to oxidative stress. (nih.gov)

The GSS gene provides instructions for making an enzyme called glutathione synthetase. (medlineplus.gov)
Global Kinetic Mechanism of Microsomal Glutathione Transferase 1 and Insights into Dynamic Enzyme Activation. (nih.gov)
In this work was used an experimental system based on an S. cerevisiae yeast mutant with a lack of the glutathione reductase enzyme and allyl alcohol as a precursor of acrolein inside the cell to determine the cellular processes influencing glutathione homeostasis . (bvsalud.org)

The higher level of NADPH can be used by the thioredoxin system and other enzymes requiring NADPH to reduce cytosolic GSSG and maintain glutathione redox potential. (bvsalud.org)

This cycle is necessary for producing a molecule called glutathione. (medlineplus.gov)

The benefits of glutathione. (mindbodygreen.com)
We'll also discuss some of the other benefits of Glutathione Skin Brightener so that you can make an informed decision about whether or not this product is right for you. (vitanetonline.com)

She wants to know what she can do about it, so I explain why it might be elevated, why it might not be an issue, why it might be one, and what she can do to boost glutathione, which her doctor recommended she increase. (marksdailyapple.com)
Foods that naturally boost glutathione levels are fruits, herbs, vegetables and meats. (naturalremedies.org)

Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme. (eurekamag.com)

It's worth restating, though: According to Hyman, glutathione 5 is a critical and integral part of the body's intrinsic detoxification system. (mindbodygreen.com)
Also unsurprising given its role in detoxification: The highest concentrations of glutathione in the body are found in the liver and kidneys . (mindbodygreen.com)
Chen TS, Richie JP Jr, Lang CA. Life span profiles of glutathione and acetaminophen detoxification. (harvard.edu)
The liver is the primary organ for detoxification, and consequently, the highest levels of glutathione in the body are found in the liver. (essentialformulas.com)

Glutathione is the most abundant intracellular thiol (i.e., a compound containing a sulfhydryl [SH] group) and low molecular weight tripeptide found in living cells. (needs.com)
This approach appeared to be highly interesting for temporary immobilization and subsequent glutathione triggered intracellular delivery of proteins from hydrogels. (eurekamag.com)
In addition, an intracellular abundance of reduced glutathione, as compared to oxidized glutathione, helps ensure healthy cell function. (pureprescriptions.com)

L-Glutathione and other antioxidants attack the free radicals and destroy them before they have a chance to attack the cells. (streetdirectory.com)
According to functional medicine doctor and mbg Collective member Mark Hyman, M.D., the sticky, flypaper-like nature of the sulfur in glutathione is what allows it to essentially grab on to free radicals and toxins (like mercury and other heavy metals) in order to usher them out of the body. (mindbodygreen.com)
No surprise here considering all that talk earlier about glutathione being like flypaper for free radicals and toxins, right? (mindbodygreen.com)

OBJECTIVE: The objective of this study was to determine whether or not treatment with the metabolic precursors, methylcobalamin and folinic acid, would improve plasma concentrations of transmethylation/transsulfuration metabolites and glutathione redox status in autistic children. (blogspot.com)
In other words, dark roast coffee is more effective than light roast coffee in reducing body weight, and in restoring red blood cell vitamin E and glutathione concentrations in healthy volunteers. (bottomlinefitness.com)

CONCLUSIONS: The significant improvements observed in transmethylation metabolites and glutathione redox status after treatment suggest that targeted nutritional intervention with methylcobalamin and folinic acid may be of clinical benefit in some children who have autism. (blogspot.com)
Redox perturbations in yeast cells lacking glutathione reductase. (bvsalud.org)
Cellular redox homeostasis has a major effect on cell functions and its maintenance is supported by glutathione and protein thiols which serve as redox buffers in cells . (bvsalud.org)

Glutathione, also referred to as L-Glutathione, L-gammaglutamyl, L-cysteinylglycine or GSH, is a tripeptide naturally occurring in the body. (naturalremedies.org)
Isolating glutathione lead to understanding of this powerful tripeptide and exploration of its many uses. (naturalremedies.org)

Essentially, it is time to supplement your diet with L-Glutathione or the proteins that help your body make more of this essential nutrient. (streetdirectory.com)
Glutathione also plays a role in processing medications and cancer-causing compounds (carcinogens), and building DNA, proteins, and other important cellular components. (medlineplus.gov)

These methods are administering glutathione using nasal sprays, sublingual (under the tongue), patches, and through injections. (naturalremedies.org)

A naturally occurring compound, L-Glutathione (Tathion,) has demonstrated that it is effective in fighting cancer, environmental poisons, and even cataracts. (streetdirectory.com)
Glutathione is naturally produced by the liver and works in that organ to combat toxins and turn them into bile ,"* explains Toronto-based dietitian Abby Langer, R.D. This pungent stuff then plays a role of its own: It's actually a must-have for the optimal digestion of fat, she explains. (mindbodygreen.com)
Reduced glutathione is derived naturally from corn glucose fermentation. (pureprescriptions.com)

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If you're looking for a serum that can provide all these benefits, then Glutathione Skin Brightener may be right for you! (vitanetonline.com)

The purpose of this article is to explain how ingestion of the popular pain-relieving medication acetaminophen depletes glutathione levels in the liver, which can cause liver damage and result in death. (essentialformulas.com)

However, still little is known about how complex cellular networks influence glutathione homeostasis . (bvsalud.org)

Although L-Glutathione is readily made by your body, supplementation with it and its precursors may increase your overall level of protection. (streetdirectory.com)
In addition to eating a healthy and balanced diet, supplementation with Glutathione and its constituents can only help to increase your overall level of health, and may even slow down the process of growing old. (streetdirectory.com)
Other methods of glutathione supplementation have been found to be somewhat effective. (naturalremedies.org)

Most people don't realize that this process rapidly depletes glutathione in the liver, resulting in liver damage and can cause death. (essentialformulas.com)

This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. (nih.gov)

vii , viii Conversely, studies in numerous species of animals have shown that boosting glutathione levels results in better health and increased longevity, and analyses in humans indicate that higher glutathione levels are associated with better health and increased longevity. (essentialformulas.com)

Hopkins made is the discovery and characterization of glutathione that is described in the Journal of Biological Chemistry. (naturalremedies.org)

Because it protects our cells by attacking the external poisons, the levels of L-Glutathione in our blood have the potential to significantly impact our overall health. (streetdirectory.com)
Levels of glutathione in the brain appear to be lower in people with Alzheimer's disease, but it is unknown if glutathione supplements are beneficial. (consumerlab.com)
In addition, Hopkins observed the way the body utilized oxygen in relation to glutathione levels. (naturalremedies.org)
Watermelon, avocado, fruits rich in vitamin C like oranges, foods containing vitamin E like almonds all contain positive levels of glutathione. (naturalremedies.org)
the higher your glutathione levels are the healthier you will be. (bottomlinefitness.com)
I predict that concern about glutathione levels will eventually be on par with other preventative health issues. (bottomlinefitness.com)
Low glutathione levels are associated with virtually all chronic lifestyle-related diseases. (essentialformulas.com)
For example, glutathione levels in centenarians are similar to the levels of young adults. (essentialformulas.com)
x Consequently, glutathione levels are now recognized as a reliable biomarker of aging. (essentialformulas.com)

Glutathione helps prevent damage to cells by neutralizing harmful molecules generated during energy production. (medlineplus.gov)
Glutathione protects cells from damage caused by unstable oxygen-containing molecules, which are byproducts of energy production. (medlineplus.gov)

Often referred to as the "mother of all antioxidants," glutathione is vital in aiding the multiplication of lymphocytes, the cells that mediate specific immunity, that occur in the development of an effective immune response. (naturalremedies.org)

It turns out that L-Glutathione is one of the most effective antioxidants that our body produces. (streetdirectory.com)

In addition to its brightening and wrinkle-reducing properties, Glutathione Skin Brightener Cream is also formulated with other clinically-tested ingredients that provide numerous benefits for your skin. (vitanetonline.com)
Glutathione Skin Brightener™ Cream is formulated with several clinically-tested ingredients including Ceramosides® and Aquaxyl® to create a skin cream that not only helps brighten the skin's appearance and improve elasticity, but also provides intense moisture and hydration while reducing the appearance of skin pigmentation. (vitanetonline.com)

Featuring Acyl-Glutathione and vitamin F blend to help provide optimal nourishment for visibly supple, even-toned and radiant-looking skin. (perriconemd.com)

He recognized that glutathione was important as a hydrogen acceptor in a number of biochemical reactions. (naturalremedies.org)
If taking an oral glutathione supplement, it is important to only take the dose recommended on the instructions and only take supplements from a very reputable manufacturer, as these supplements are not closely regulated. (naturalremedies.org)
Many researchers say glutathione is probably the most important substance we require to stay healthy. (bottomlinefitness.com)

In addition to this role in daily immune function, Hyman also suggests that ample glutathione is crucial for long-term immunity, as well. (mindbodygreen.com)

Do glutathione supplements work to prevent aging or for other conditions? (consumerlab.com)
Tests have shown that some 'glutathione' supplements contain little glutathione, less glutathione than listed, and/or are contaminated with lead. (consumerlab.com)
Oral supplements of glutathione are easily available at many places on the Internet such as amazon.com and vitacost.com and can also be found in retail stores such as GNC or walmart. (naturalremedies.org)

In addition, the level of tissue damage from Carbon Monoxide, Hydrogen Sulfide, heavy metals, pesticides, and environmental poisoning has been demonstrated to be significantly lower with adequate L-Glutathione in the blood stream. (streetdirectory.com)

What is glutathione - and what does it do in the body? (mindbodygreen.com)
Glutathione also works to maintain the epithelial tissues (the lining found in organs like the intestines), which act as barriers between compounds ingested by the body and the bloodstream and are crucial for maintaining immune balance. (mindbodygreen.com)
Glutathione, however, must be generated within the cells before it can work effectively within the body. (naturalremedies.org)
It is rumored that actress Suzanne Summers spends over nine hundred dollars a month on glutathione injections to keep her healthy and give her body a youthful appearance. (naturalremedies.org)
There have been some studies that have shown that the glutathione found in whey protein can be absorbed by the body. (naturalremedies.org)
Consequently, glutathione regulates the health of every cell in the body. (essentialformulas.com)

Essential FX Acyl-Glutathione Smoothing & Brightening Under-Eye Cream (15 mL / 0.5 US fl. (perriconemd.com)

This compound builds up when glutathione is not processed correctly in cells. (medlineplus.gov)

A quick search of the term "glutathione" on PubMed.gov reveals 94,117 scholarly articles, reviews and abstracts. (bottomlinefitness.com)

In cerebrospinal fluid of drug-free schizophrenic patients, a significant decrease in the level of total glutathione was observed as compared to controls. (bottomlinefitness.com)

Knockdown of microsomal glutathione S-transferase 1 inhibits lung adenocarcinoma cell proliferation and induces apoptosis. (nih.gov)
The inhibition of cell death induced by the ROS donor tert-butylhydroperoxide was also observed in cells depleted from endogenous glutathione (GSH), suggesting that GSH is not the sole electron acceptor for HIV-1 GPX. (uncg.edu)

Essential GSH is a breakthrough liquid formulation uniquely designed to increase the systemic bioavailability of glutathione, via an oral liposomal-based delivery. (breakspearmedical.com)

Microsomal glutathione S-transferase 1 targets the autophagy signaling pathway to suppress ferroptosis in gastric carcinoma cells. (nih.gov)

Anatomy12

Organisms6

Diseases3

Chemicals and Drugs119

Analytical, Diagnostic and Therapeutic Techniques and Equipment8

Phenomena and Processes28

Information Science3

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

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

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

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

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

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

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

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

Glutathione

Glutathione Transferase

Glutathione Peroxidase

Glutathione Reductase

Glutathione Disulfide

Glutathione Synthase

Buthionine Sulfoximine

Glutathione S-Transferase pi

Glutamate-Cysteine Ligase

Dinitrochlorobenzene

Oxidative Stress

Methionine Sulfoximine

Antioxidants

Oxidation-Reduction

Sulfhydryl Compounds

Selenium

Catalase

Maleates

Liver

Cysteine

Lipid Peroxidation

Acetylcysteine

gamma-Glutamyltransferase

Superoxide Dismutase

Hydrogen Peroxide

Isoenzymes

Reactive Oxygen Species

Cystine

Malondialdehyde

Kinetics

Molecular Sequence Data

Glutaredoxins

Pyrrolidonecarboxylic Acid

Amino Acid Sequence

Erythrocytes

Thiobarbituric Acid Reactive Substances

Oxidants

Diamide

Metabolic Detoxication, Drug

Ascorbic Acid

Peroxides

Ethacrynic Acid

Lipid Peroxides

tert-Butylhydroperoxide

S-Nitrosoglutathione

Thioredoxins

Chromatography, High Pressure Liquid

Peroxidases

Substrate Specificity

Lactoylglutathione Lyase

Thioredoxin-Disulfide Reductase

Aldehydes

Cytosol

Protein Disulfide Reductase (Glutathione)

NADP

Disulfides

Dithiothreitol

Acetaminophen

Oxidoreductases

Base Sequence

Rats, Wistar

Dose-Response Relationship, Drug

Selenoproteins

Selenious Acid

Rats, Sprague-Dawley

Free Radical Scavengers

Antimetabolites

Recombinant Fusion Proteins

Cells, Cultured

Organoselenium Compounds

Free Radicals

Cell Survival

Rats, Inbred Strains

Binding Sites

Biotransformation

Catalysis

Cell Line

Gene Expression Regulation, Enzymologic

Cloning, Molecular

NF-E2-Related Factor 2