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- A tripeptide composed of glutamate, cysteine and glycine
- Functions
- How the body makes it
- Oxidation
- Recycling (Reduction)
- Destruction
- Testing
- Supplementation
- My glutathione experience
- For more information
- How the body makes it
- Intracelluar antioxidant
- reduces hydrogen peroxide
- regenerates oxidized vitamins C and E
- removes the cellular debris from free radical attacks: lipid peroxides, damaged DNA, proteins, etc.
- Essential donor of sulfhydryl groups necessary for the detoxification of the liver. Enables conversion of Phase I Detox products to water-soluble forms. Detoxifies many environmental toxins, including
- solvents
- herbicides
- fungicides
- polycyclic aromatiac hyrdrocarbons
- heavy metals
- Facilitates cell carbohydrate metabolism, calcium metabolism, blood platelet and membrane functions.
- Involved in amino acid transport across cell membranes (the gamma-glutamyl cycle, primarily in the kidney).
- Part of the peptidoleukotrienes.
- Cofactor for enzymatic reactions [which?].
- Aids rearrangement of protein disulfide bonds.
- Essential for thyroid hormone synthesis of T4 to T3.
- Essential for hair growth.
GSH works through the operation of a group of enzymes called glutathione S-transferases (GST). These show wide variation from individual to individual, with genes for them sometimes even missing. (See GST.)
- production requires
- Cysteine
- Glycine
- Glutamine
- enzymes
- gamma-glutamylcysteine synthetase (key step in glutathione synthesis, dependent on ATP)
- glutathione synthetase
- functioning requires enzymes (in which genetic deficiencies are common): [need more info]
- Glutathione S-transferases (GST).Various mutations and deficiencies in these enzymes are relatively common. See My Genovations' DetoxiGenomics Profile.
- [?more? quinone reductase?]
- recycling requires
- Selenium
- Vitamin C
- After accepting free radicals, it becomes oxidized Glutathione Disulfide (GSSG).
- Mechanisms
- Immune-Metal Pathology: a proposed model of glutathione depletion due to mercuy. Results of studies using MELISA testing.
- Thiol binding
- (It's also depleted by acetaminophen, which I used a lot of for years when I was losing teeth, until I could no longer tolerate it.)
- Common sources of substrates (compounds using GSH to detox):
- Cigarette smoke
- herbicides, fungicides, insect sprays, industrial solvents.
- Symptoms
- Glutathione peroxidase (GPx)
- oxidizes glutathione (GSH) to glutathione disulfide (GSSH).
- reduces H2O2 to H2O.
- requires selenium (essential) for both its protein synthesis and enzymatic activity.
- Then re-reduction of the oxidized form of glutathione (GSSG) is catalysed by glutathione reductase, with co-factor NADPH, resulting in two units of GSH.
- also requires vitamin C, and phosphate [for what?]
- also copper, zinc, or manganese for SOD; and iron for catalase
- —That's from Glutathione peroxidase enzyme, by Tamer Fouad, M.D., an article on The Doctor's Lounge site. (He cites Halliwell, 1995)
- [Hmm, does that mean they'll work somewhat without?]
- "When increasing amounts of glutathione are oxidized, some of the oxidized glutathiones undergo renal degradation by gammaglutamyl transpeptidase, resulting in an irreversible loss of glutathione." From Oxidized and Free Whole Blood Thiols in Preeclampsia, by Maarten T. M. Raijmakers et al. (They cite Uhlig S, Wendel A. The physiological consequences of glutathione variations. Life Sci 1992;51:1083–94.)
- Great Smokies' Liver Detox Profile includes [what kind?]
- [others?]
- Glutathione, on the PDRHealth site. Extensive references.
- Glutathione, on the Vitacost site. Extensive references.
- Glutatione Synthetase
- On curcumin:
- Glutathione - Your Brain's Master Antioxidant Defense, by Priya Shah, with references, including "Can Curry Protect Against Alzheimer's?; American Physiological Society (APS) Press Release; 16-Apr-2004.
- Induction of apoptosis by curcumin: mediation by glutathione S-transferase P1-1 inhibition. Duvoix A, Morceau F, Delhalle S, Schmitz M, Schnekenburger M, Galteau MM, Dicato M, Diederich M. Laboratoire de Recherche sur le Cancer et les Maladies du Sang, Centre Universitaire de Luxembourg, 162A Avenue de la Faiencerie, L-1511 Luxembourg, Luxembourg.
- Acetylcysteine and Glutathione: New Understandings, by Richard A. Passwater PhD. "NAC is produced in living organisms from the amino acid cysteine {two compounds that are involved in intracellular glutathione production are N-acetyl-L-cysteine (NAC) and L-2-oxo-thiazolidine 4-carboxylate (Procysteine)}. " References.
- Dental Mercury Exposure at CFS Nutrition's site.
- Amino Acid Derivatives — search for "Glutathione Functions"
- Impaired Sulfur Oxidation at CFS Nutrition's site. Discusses both cysteine dioxygenase and sulfite oxidase. "When a person is a poor sulfur oxidizer they often find ordinary foods bearing sulfur compounds to be a source of discomfort. Broccoli and garlic being but two examples of foods which can contribute to uncomfortable excess cystiene levels in such people." Hmm, "discomfort" -- like my liver attacks?
- Abstract on PubMed of "The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance", by JD Hayes JD and DJ Pulford, of the
Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Scotland, U.K. - My pages:
- Glutathione Supplementation
- Molybdenum
- Sulfur Metabolism
- Glutathione conjugation in liver Phase II detox.
- Acetaminophen Poisoning
- SAMe
- L-Cysteine
- Homocysteine
Last updated 1 December 2005