What is glutathione

Glutathione is produced naturally in the body via the synthesis of certain amino acids. It is produced in the liver and is used to neutralize certain toxins through its antioxidant effects. Glutathione is important in the immune system. Glu…

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“Glutathione is a very interesting, very small molecule that’s [produced by the body and] found in every cell,” says Gustavo Bounous, MD, director of research and development at Immunotec and a retired professor of surgery at McGi…

http://www.webmd.com/diet/features/glutathione-new-supplement-on-block?printing=true

One of the body’s most powerful intracellular antioxidant enzymes and detoxifying agents. Cysteine (along with glycine and glutamate) is an amino acid and precursor of glutathione. NAC enhances the production of glutathione. In addition, gl…

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Related Questions Answered on Y!Answers

what for is glutathione?

Q:

A: Glutathione (GSH), whose IUPAC name is 2-amino-5-{[2-[(carboxymethyl)amino]- 1-(mercaptomethyl)-2-oxoethyl]amino}-5-oxopentanoic acid, is γ-glutamylcysteinylglycine, a tripeptide. It contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain. Glutathione, an antioxidant, protects cells from toxins such as free radicals.Glutathione is present in tissues in concentrations as high as one millimolar. Cysteine, the business residue of glutathione, neither has the solubility nor activity of glutathione at physiological pH. It appears that nature has built the cysteine molecule into the glutathione tripeptide to make the amino acid more soluble and allow it to have redox buffering activity in a living tissue environment. Glutathione also plays roles in catalysis, metabolism, signal transduction, gene expression and apoptosis. It is a cofactor for glutathione S-transferases, enzymes which are involved in the detoxification of xenobiotics, including carcinogenic genotoxicants, and for the glutathione peroxidases, crucial selenium-containing antioxidant enzymes (see Selenium). It is also involved in the regeneration of ascorbate from its oxidized form, dehydroascorbate (see Vitamin C). There are undoubtedly roles of glutathione that are still to be discovered.Glutathione is present in the diet in amounts usually less than 100 milligrams daily, and it does not appear that much of the oral intake is absorbed from the intestine into the blood (see Pharmacokinetics). Glutathione is not an essential nutrient since it can be synthesized from the amino acids L-cysteine, L-glutamate and glycine. It is synthesized in two ATP-dependent steps: first, gamma-glutamylcysteine is synthesized from L-glutamate and cysteine via the enzyme gamma-glutamylcysteine synthetase—the rate limiting step— and second, glycine is added to the C-terminal of gamma-glutamylcysteine via the enzyme glutathione synthetase. The liver is the principal site of glutathione synthesis. In healthy tissue, more than 90% of the total glutathione pool is in the reduced form and less than 10% exists in the disulfide form. The enzyme glutathione disulfide reductase is the principal enzyme that maintains glutathione in its reduced form. This latter enzyme uses as its cofactor NADPH (reduced nicotinamide adenine dinucleotide phosphate). NADPH is generated by the oxidative reaction in the pentose phosphate pathway.The consequences of a functional glutathione deficiency, which results in tissue oxidative stress, can be seen in some pathological conditions. For example, those with glucose 6-phosphate dehydrogenase deficiency produce lower amounts of NADPH and hence, lower amounts of reduced glutathione. This condition is characterized by a hemolytic anemia. Conditions causing chronic glutathione deficiency all result in hemolytic anemia, among other pathological consequences. Oxidative stress caused by glutathione deficiency results in fragile erythrocyte membranes. Malaria-causing organisms (Plasmodia species) do not like to feed on these sick erythrocytes. That is about the only good news regarding this situation. Chronic functional glutathione deficiency is also associated with immune disorders, an increased incidence of malignancies, and in the case of HIV disease, probably accelerated pathogenesis of the disease. Acute manifestations of functional glutathione deficiency can be seen in those who have taken an overdosage of acetaminophen. This results in depletion of glutathione in the hepatocytes, leading to liver failure and death, if not promptly treated.Glutathione is an orphan drug for the treatment of AIDS-associated cachexia. It is thought that this disorder is due, in part, to oxidatively-stressed and damaged enterocytes. There is some evidence that although orally administered glutathione may not be absorbed into the blood from the small intestine to any significant extent, that it may be absorbed into the enterocytes where it may help repair damaged cells. Glutathione in one form or another is the subject of some medicinal chemistry research and some clinical trials. For example, an aerosolized form of glutathione is being studied in AIDS and cystic fibrosis patients. Glutathione, the principal antioxidant of the deep lung, appears to be diminished in those with AIDS. Prodrugs of gamma-L-glutamyl-L-cysteine are being evaluated as anticataract agents.ACTIONS AND PHARMACOLOGYACTIONSGlutathione has antioxidant activity. It may have detoxification, and immunomodulatory activities, and may have beneficial effects on sperm motility and in the protection against noise-induced hearing loss.MECHANISM OF ACTIONGlutathione is the principal intracellular non protein thiol and plays a major role in the maintenance of the intracellular redox state. It may be thought of as an intracellular redox buffer. Glutathione is a nucleophilic scavenger and an electron donor via the sulfhydryl group of its business residue, cysteine. Its reducing ability maintains molecules such as ascorbate and proteins in their reduced state. Glutathione is also the cofactor for the selenium-containing glutathione peroxidases (see Selenium), which are major antioxidant enzymes. These enzymes detoxify peroxides, such as hydrogen peroxide and other peroxides. Another antioxidant activity of glutathione is the maintenance of the antioxidant/reducing agent ascorbate in its reduced state. This is accomplished via glutathione-dependent dehydroascorbate reductase which is comprised of glutaredoxin and protein isomerase reductase. Glutathione may also react with the reactive nitrogen species peroxynitrite to form S-nitrosoglutathione.Glutathione S-transferases (GSTs) consist of a family of multifunctional enzymes that metabolize a wide variety of electrophilic compounds via glutathione conjunction. GSTs are involved in the detoxification of xenobiotic compounds and in the protection against such degenerative diseases as cancer. The mechanism of these enzymes involves a nucleophilic attack by glutathione on an electrophilic substrate. The resulting glutathione conjugates that form are more soluble than the original substrates and thus more easily exported from the cell. The release of glutathione-S-conjugates from cells is an ATP-dependent process mediated by membrane glycoproteins belonging to the multidrug-resistance protein (MRP) family. Proteins of the MRP family are essential for the transport of glutathione S-conjugates into the extracellular space. They are also known as glutathionine-S-conjugate pumps.Absorption of orally administered glutathione has been observed in some animals (mice, rats, guinea pigs). Oral glutathione has been demonstrated to reverse age-associated decline in immune responsiveness in mice. In one study, glutathione was found to enhance T-cell mediated responsiveness, including delayed-type hypersensitivity (DTH). The mechanism of this effect was ascribed to the antioxidant activity of glutathione.Parenterally administered glutathione was found to improve sperm motility in a small human trial. Again, the effect was thought to be due to the antioxidant activity of this substance.Noise-induced hearing loss is thought to be due to oxidative stress. Intraperitoneal administration of glutathione to guinea pigs was found to protect against noise-induced hearing loss and once more, the antioxidant activity of glutathione was thought to account for this effect.PHARMACOKINETICSThe pharmacokinetics of oral glutathionine in humans are not well understood. It appears that in some animals (mice, rats, guinea pigs), serum glutathione levels do increase following its oral administration. Most human studies of glutathione have not found this to be the case. It appears that oral glutathione is hydrolyzed in the intestine via the intestinal gamma-glutamyl transferase enzyme. A small amount of orally administered glutathione may reach the portal circulation, but apparently this is also rapidly metabolized by hepatic gamma-glutamyltransferase. Thus, most studies have not observed a significant increase in circulating glutathione following its oral administration. However, there is an occasional study that does show an increase in circulating glutathione after oral administration. Further, there is some evidence that glutathione may be absorbed into the enterocytes following ingestion, but may not be released by these cells into the circulation. Research is needed to resolve the issue of glutathione absorption.INDICATIONS AND USAGEThough glutathione is undoubtedly a potent antioxidant, indications for its use as a supplement are not yet well established. There is preliminary evidence that it might eventually prove to be useful in the management of some cancers, atherosclerosis, diabetes, lung disorders, noise-induced hearing loss, male infertility and to help prevent or ameliorate various toxicities. It may also have some anti-viral activity. Glutathione is an orphan drug for the treatment of AIDS-associated cachexia.Thiol groups are kept in a reduced state within ~5 mM in animal cells. In effect, glutathione reduces any disulfide bonds formed within cytoplasmic proteins to cysteines by acting as an electron donor. Glutathione is found almost exclusively in its reduced form, since the enzyme which reverts it from its oxidized form (GSSG), glutathione reductase, is constitutively active and inducible upon oxidative stress. In fact, the ratio of reduced to oxidized glutathione within cells is often used scientifically as a measure of cellular toxicity.FunctionGlutathione participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bile. Glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II catalyzes the hydrolysis of S-D-Lactoyl-glutathione to glutathione and D-lactate.GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in cytosol, microsomes, and mitochondria. However, it is also capable of participating in non-enzymatic conjugation with some chemicals, as in the case of n-acetyl-p-benzoquinone imine (NAPQI), the reactive cytochrome P450-reactive metabolite formed by acetaminophen (or paracetamol as it is known in the UK), that becomes toxic when GSH is depleted by an overdose of acetaminophen. Glutathione in this capacity binds to NAPQI as a suicide substrate and in the process detoxifies it, taking the place of cellular protein thiol groups which would otherwise be covalently modified; when all GSH has been spent, NAPQI begins to react with the cellular proteins, killing the cells in the process. The preferred treatment for an overdose of this painkiller is the administration (usually in atomized form) of N-acetylcysteine, which is used by cells to replace spent GSSG and renew the usable GSH pool.Phorone efficiently reacts to the GSH thiol groups which makes phorone a GSH depletor. It is used to study the effects of GSH as a hydrogen peroxide scavenger in asthma.The health food industry promotes oral glutathione as a very efficient antioxidant to be used against a whole range of diseases. Research suggests, however, that glutathione is not orally bioactive, and that very little of oral glutathione tablets or capsules is actually absorbed by the body. Glutathione precursors are preferred to oral glutathione itself to significantly increase glutathione content within the cell.Nutritional supplement companies also offer N-acetylcysteine, which has been shown to increase glutathione in vivo. In 1996 a Canadian company Immunotec Research Ltd. developed and now manufactures bioactive bonded cystine dietary supplement derived from lactose-free organic milk (whey protein) called Immunocal that is clinically proven to increase glutathione levels within the lymphocytes of the immune system by 35.5% while increasing peak power and muscular performance by 13%. N-acetylcysteine is a generically available supplement which has been demonstrated to increase intracellular reduced and total glutathione by 92% and 58% respectively.

glutathione?

Q: Can glutathione take away my freckles? If yes, please give me the most effective brandname of glutathione i can use. thanks.

A: I never heard glutathione taking away freckles, maybe..a big maybe it can prevent more from appearing. It is an antioxidant.I suggest you use a sunscreen with a spf of 30 to prevent more freckles it’s a lot cheaper and is effective.

What is the difference between l-glutathione and reduced glutathione?

Q: I need to know how l-glutathione is different from reduced glutathione or is it the same? Also I heard that the side effects of l-glutathione is akin whitening but it isn’t permanent or is it?

A: L-glutathione is “the reduced form of glutathione”. The reduced form of glutathione or L-glutathione is the kind of glutathione that has the side effect of skin whitening. The effects can be permanent, however you have to maintain your skin in good condition of-course. that would mean you have to stay clear from prolonged exposure to uv rays or sunlight, you have to drinks lots of water, and eat fruits and vegetables. If your considering whitening your skin however i suggest you first try Swiss l-glutathione bar. It’s a really good whitening soap that brings the effects of glutathione directly to your skin. visit their site here:http://www.swisscare4u.com