Glutathione, why you need it

Glutathione is an essential factor in energy utilization, detoxification, and preventing the diseases we associate with aging. Glutathione deficiency has been linked to:

• Age-related diseases such as Alzheimer’s and Parkinson’s
• Coronary and autoimmune diseases
• Arthritis, asthma and other inflammatory conditions
• Cancer
• Mitochondrial dysfunction
• Muscle weakness and fatigue

Glutathione levels can be enhanced somewhat by taking supplements such as alpha lipoic acid, which is known to regenerate glutathione. Alpha lipoic acid also helps to regenerate vitamins C and E so that they remain active longer in your body. Red meat and organ meats are the best dietary source of alpha lipoic acid.

Glutamine can be used as a supplement since it’s a direct precursor to glutathione. However, there is quite a bit of evidence it is poorly absorbed.

There is also evidence that vitamin D increases intracellular glutathione.  I am an enthusiastic fan of vitamin D, and this is yet one more reason it’s so important for your health.

Some nutritional authorities recommend taking a form of cysteine known as N-acetyl-cysteine NAC, but I would advise against using this supplement if you still have mercury amalgam fillings because it could interfere with detoxification of the mercury.

Fortunately, there are natural ways to boost your body’s glutathione reserves.

Vitamins and supplements have their uses but are always less desirable than nutrients in their natural form, obtained from the foods you eat. What has been proven beyond a doubt is that whole food based diets--rich in vegetables, fruits, nuts, seeds, and quality protein--promote health and longevity.

What Foods Promote the Highest Glutathione Levels?

Many whole foods contain significant amounts of glutathione or its precursors. Foods richest in sulfur-containing amino acids are usually the best sources of glutathione:

• The overall top food for maximizing your glutathione is high quality whey protein. It must be cold pressed whey protein derived from grass fed cows, and free of hormones, chemicals and sugar. 
  Quality whey provides all the key amino acids for glutathione production (cysteine, glycine and glutamate) and contains a unique cysteine residue (glutamylcysteine) that is highly bioactive in its affinity for converting to glutathione. 
  
  Glutamylcysteine is a bonded cysteine molecule (cysteine plus glutamate) that naturally occurs in Bovine Serum Albumin – a fragile immune component of the whey. This unique cysteine is exclusive to whey and rarely appears in other protein foods – which makes whey protein the best glutathione-promoting food source. 
  
  Furthermore, whey provides critical co-factors, immunoglobulins, lactoferrin and alpha Lactalbumin (also a great source of cysteine), which together help create the right metabolic environment for high glutathione activity.
• Raw milk products, raw eggs and meat: Glutathione occurs in the highest levels in fresh, uncooked meats and raw milk, but is almost entirely absent in pasteurized dairy products.
• Fresh fruits and vegetables provide excellent glutathione, but once cooked, values become negligible. Spinach, potatoes, asparagus, avocado, squash, okra, cauliflower, broccoli, walnuts, garlic and tomatoes have the highest glutathione per serving.
• The herb milk thistle is an excellent source of the antioxidant compound silymarin, which may help to prevent glutathione depletion in the liver. Glutathione is crucial in the liver for detoxification and can become depleted from acetaminophen (Tylenol), alcohol consumption, and general toxic overload.
• Curcumin may also be useful for increasing glutathione levels.

Keeping your glutathione levels up is a matter of increasing factors that boost your glutathione and decreasing factors that lower it. The things that deplete your glutathione the fastest are chemicals, toxins and sugar.

PURE-NATURAL-WHEY

If you want to supplement your diet with whey protein products, you have to be careful because not all whey protein products are created equal. Supermarket and nutrition store shelves are lined with protein powder choices, 99 percent of which are loaded with sugar and chemicals that don’t support your health goal.

If you’re going to supplement, you should only use a high quality whey protein that provides all the necessary nutritional elements for NATURALLY boosting glutathione and also preventing its decline.

Be sure your whey protein supplement has the following features:

1. The whey comes from grass-fed cows that are not treated with pesticides or hormones
2. Cold processed, since heat destroys whey’s fragile molecular structure
3. Whey protein concentrate, not protein isolates
4. Sweetened naturally, not artificially, and low in carbohydrates
5. Highly digestible—look for medium chain fatty acids (MCTs), not long chain fatty acids

more healthy eating with http://www.rawfoodsonabudget.com 

References

• Bounous G. Whey protein concentrate (WPC) and glutathione modulation in cancer treatment. Anticancer Res. 2000 Nov-Dec;20(6C):4785-92.
• Bounous G., Gold P. 1991. The biological activity of undenatured dietary whey proteins: role of glutathione. Clin Invest Med.Aug;14(4):296-309.
• Dickinson D., Iles K., Zhang K., Blank V., and Forman H. (2003) Curcumin alters EpRE and AP-1 binding complexes and elevates glutamate-cysteine ligase gene expression. J FASEB 17, 472.
• Donnini D., Zambito A.M., Perrella G; Ambesi-Impiombato F.S., Curcio F. Glucose may induce cell death through a free radical-mediated mechanism. Biochem Biophys Res Commun. 219(2):412-7 1996 Feb 15.
• El-Hawary Z., El-Hawary M.F.S., Morcus S.R. 1977. Blood glucose, glutathione, and total keto-acids levels in alloxan-diabetic rats. Zeitschrift für Ernährungswissenschaft 16(4): 227-230.
• Fidelus R.K., Tsan M.F. Glutathione and lymphocyte activation: a function of aging and auto-immune disease. Immunology. 1987 61:503-508.
• Glutathione. 
• Glutathione White Paper. Richard Van Konynenburg, PhD. 
• Herbert F.K., Cotonio Bourne M., Groen J. 1930. The effect of glutathione on the determination of blood-sugar. Department of Chemical Pathology, St. Bartholomew’s Hospital, London.
• Higashi T., Tateshi N., Naruse A., Sakamoto Y. (1977) A novel physiological role of liver glutathione as a reservoir of L-cystein. J Biochem. 82, 117.
• Huh K., Kwon T.H., Kim J.S., Park J.M. Role of the hepatic xanthine oxidase in thyroid dysfunction: effect of thyroid hormones in oxidative stress in rat liver. Arch Pharm Res; 21(3):236-40 Jun 1998.
• Loven D., Schedl H., Wilson H., Daabees T.T., Stegink L.D., Diekus M., Oberley L. Effect of insulin and oral glutathione on glutathione levels and superoxide dismutase activities in organs of rats with streptozocin-induced diabetes. 
• Meister A. (1983) Selective modification of glutathione metabolism. Science. 220, 472.
• Meredith M.J., Reed D.J. (1983) Depletion in vitro of mitochondrial glutathione in rat hepatocytes and enhancement of lipid peroxidation by adriamycin and 1,3Bis(2-chloroethyl)-1-nitrosaurea (BCNU). Biochem Pharmacol. 32, 1383.
• Powell L.A., Warpeha K.M., Xu W., Walker B., Trimble E.R. High glucose decreases intracellular glutathione concentrations and upregulates inducible nitric oxide synthase gene expression in intestinal epithelial cells. Journal of Molecular Endocrinology.December 1, 2004 33:797-803.
• Seymen, O., Seven A., Candan G., Yigit G., Hatemi S., Hatemi H. The effect of iron supplementation on GSH levels, GSH-Px, and SOD activities of erythrocytes in L-thyroxine administration. Acta Med Okayama. 51(3):129-33 1997 Jun.
• Stohs S.J., Lawson T., Al-Turk W.A. (1984) Changes in glutathione and glutathione metabolizing enzymes erythrocytes and lymphocytes of mice as a function of age. Gen Pharmacol. 15, 267.
• Tsan M.F., Danis E.H., Del Vecchio P.J., Rosano C.B. (1985) Enhancement of intracellular glutathione protects endothelial cells against oxidative damage. Biochem Biophys. Res. Commun. 127, 270.
• Wellner V.P., Anderson M.E., Puri R.N., Jensen G.L., Meister A. (1982) Radioprotection by glutathione ester: transport of glutathione ester in human lymphoid cells and fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 81, 4732.