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  1. #1
    Join Date
    Apr 2004


    I remember when i first started noticing my hair loss i went to some quack 'trichologist' and he recommened this supplement.

    It basically assists with immune deficiency issues and is in a lot of supplements these days, but you can get it in it's pure form, basically as the most powerful anti-oxident available on the planet.

    Reading that hair loss can be attributed to immunity problems made me remember Glutathione.

    Does anyone have any thoughts on this?

  2. #2
    Senior Member Jacob's Avatar
    Join Date
    Apr 2005
    From what I've read..taking it in it's pure form doesn't do much. There is a(very expensive) liposomal version that is supposed to be good though. One other one I came across may work as well..will have to dig it up.

    GliSODin may increase it:
    According to PL Thomas President Paul Flowerman, “This is the third and most important study conducted on the mechanism of action of GliSODin. This study validates the concept of GliSODin as an ‘antioxidant catalyst,’ showing significant promotion of internal antioxidant production, including superoxide dismutase (SOD), catalase and glutathione peroxidase.”
    Supplements such as Sam-e..whey etc..may also work.
    Immunocal®/HMS-90 is a natural, un-denatured, patented, whey protein (milk derivative) food supplement, which assists the body in maintaining optimal concentrations of glutathione (GSH). It is a delivery system for getting the amino acid, cysteine, into all of the cells in your body. Cysteine is a part of the glutathione molecule and determines the rate at which it is manufactured by the cell.
    BTW..I've been using glutathione in a couple of topicals lately. Oxi-Cell and Elsom Research's EquiClear with glut and sod.

  3. #3
    I use L-Glutimine in powder form to help with my immune sysytem but not for my MPB. I do a lot of running and weigt training and it helps me from getting run down. Works a treat for that IMHO.
    It's around £32 (I use the Reflex brand) for a tub - should last around 3-4 months or so. I take 5g 3 times a day.


  4. #4
    Junior Member
    Join Date
    Oct 2005
    glutathione is a major antioxidant within the body. If free radicals are the primary mechanism of your hair loss it will definatly do you some good. My opinion for what its worth, is that glutathione is great to take for to promote overall health. If free radicals are causing that much damage to your hair you should also be observing similiar overall health problems. If that is the case you should see a physician immediatly, if not try lowering your DHT, like the rest of us.

  5. #5
    Senior Member Pete's Avatar
    Join Date
    May 2002
    The best way to boost intra cellular Glutathione is via Whey Protein Isolate - you can do some further reading here :

  6. #6
    Senior Member Jacob's Avatar
    Join Date
    Apr 2005


    Bump to a very old thread..Acetyl-glutathione may be worth looking into imo..if anyone can find some decent prices

    Acetyl-glutathione is a compound normally found in a human body, as an analog to the potent antioxidant, reduced glutathione. Glutathione is, of course, a potent intracellular antioxidant, and it's depletion is a component of every chronic disease and inflammatory condition, or the most chronic circumstance of aging. It may also act - as other peptides have been found to behave - as a signal to other metabolic processes.

    Reduced glutathione is acted upon by peptidase almost immediately in the blood and tissues and, thus, loses its ability to enter cells and act intercellularly. This happens in a very short period of time, and, thus, IV glutathione - while having a remarkable impact on metabolism - is short-lived. Inhalation of glutathione has shown promise in COPD and emphysema, and we believe this continues to be a valuable tool; however, continual inhalation treatment along with oral acetyl-glutathione supplementation seems to work much better.

    Acetyl-glutathione (acetylated at anyone of the three possible positions of the tripeptide) is made by the liver and transported to all other tissues. It is easily assimilated intracellularly and then allowed to perform its powerful antioxidant and metabolic regulatory effects without prior decomposition by peptidases.

    It has been found that acetyl-glutathione is absorbed orally and is transported to all tissues of the body with remarkable anti-aging effects, anti-viral effects, and in some studies an effect on some cancers. More and more is being discovered about this remarkable compound. Studies are ongoing regarding the use of this product in HIV infections, most cancers, and all inflammatory diseases.*
    It is my hypothesis, actually, that a high homocysteine level - which is observed in virtually all degenerative disease states - is actually the body's own way of trying to produce more glutathione. In our ignorance, we have mimicked Big Pharma's approach here to illness; as natural health practitioners we have found ways to simply lower homocysteine levels rather than address the "root" reason they are elevated in the first place! I hope we are moving towards a better understanding of the critical importance of adequate intracellular glutathione to our overall health. Glutathione is the:

    * Master antioxidant
    * Master anti-inflammatory
    * Master detoxifier

    Specific conditions of ill-health that raise the glutathione flag for me include the neurodegenerative diseases such as Alzheimer's disease and Parkinson's'; cancers of all kinds; any condition of mercury/heavy metal toxicity; gastrointestinal inflammatory diseases such as Crohn's, IBS, ulcerative colitis, etc.,; cardiovascular disease, pulmonary disease (including COPD, pulmonary fibrosis, cystic fibrosis, asthma), liver disease, obesity (gluathione detoxifies the liver; a well-functioning liver is critical to ones ability to burn fat).
    Site on testimonials...not a whole lot yet:

    Since it doesn't have the odor of regular glutathione...a topical containing it would be interesting to try. There are a few out there.

  7. #7
    Senior Member Jacob's Avatar
    Join Date
    Apr 2005


    It's been mentioned before how glutathione levels seem to be lower in the balding areas...some info as posted by kingpin and choreboy elsewhere:

    The reduced glutathione to oxidized glutathione levels appear to influence G6PDH and maybe vice versa.But this shows indirectly(I believe) that glutathione levels ARE lower in mpb scalp.There is another study which says alopecic scalp is lower in glutathione also but doesnt state if they meant mpb specifically.

    The second abstract suggests glutathione is an important part of androgen signaling.Maybe we become more androgen sensitive because of lower glutathione levels? But just blocking the androgen receptor may not be enough because perhaps it doesnt reverse the redox status? Sometimes when pathways are shut down too long merely reversing the original offender doesnt restore them to back to baseline levels as a new homeostatic setpoint was determined.

    We can increase glutathione levels and G6PDH(an energy enzyme) by l-carnitine and alpha lipoic acid and NAC and aged garlic(because of s-allyl cysteine).

    If you think about what the cell is attempting to do,it makes sense.If a cell has a poor antioxidant defense system it better shut down energy pathways like G6PDH or it could lead to cancer.


    Biosci Biotechnol Biochem 1999 Dec;63(12):2219-21 Related Articles, Books

    Activity of glucose-6-phosphate 1-dehydrogenase in hair follicles with male-pattern alopecia.

    Adachi K, Watanabe Y, Inouye K

    Research and Development Headquarters, Lion Corporation, Kanagawa, Japan.

    [Medline record in process]

    Activity of glucose-6-phosphate 1-dehydrogenase (G6PDH) in human hair follicles was measured. A good relationship has been demonstrated between the activity and the ratio of the number of the anagen hairs to that of all the plucked hairs in the frontal-parietal region of the scalp with male-pattern alopecia. As the ratio becomes lower so that the advancing degree of alopecia is higher, the G6PDH activity becomes lower.

    PMID: 10664855, UI: 20128240

    Purification of androgen receptors in human sebocytes and hair. Sawaya ME.

    University of Miami School of Medicine, Department of Dermatology and Cutaneous Surgery, FL 33101.

    Human sebaceous glands (SG) and hair follicles (HF) are target structures in the skin for androgen action. They contain steroid enzymes, capable of transforming weak androgens into the target-tissue-active androgens testosterone (T) and dihydrotestosterone (DHT), which bind to the androgen receptor (AR) to regulate cellular transcription. The AR from HF and SG from human scalp tissue has been purified greater than 86,000 times by phenyl-sepharose, DEAE-sephacel, gel filtration chromatography, and ultrafiltration. Sucrose density gradient analysis and non-denaturing gradient polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS)-PAGE revealed two molecular species of AR, an active form called monomer, capable of binding DHT with great specificity (4S, m = 62,000 Da, Kd = 0.6 nM, Bmax 8260 fmol/micrograms protein), and the other, an inactive form of the monomer called tetramer (10.8S, m = 252,000 Da, Kd = 2.9 nM). The two species are interconvertible, and after purification each appeared as a single band on SDS-PAGE. The conversion of the monomer to the tetramer AR form is influenced by reduced and oxidized glutathione, and possibly by an endogenous disulfide converting factor (DCF). Furthermore, biochemical events in the androgenic signal transduction sequence were shown to be stimulated by androgens via the AR. These include the total nuclear AR content, chromatin binding of AR complexes, and stimulation of RNA polymerase II, thus influencing gene expression, which is important in understanding regulation of HF growth and SG proliferation.

    L-carnitine and DL-alpha-lipoic acid reverse the age-related deficit in glutathione redox state in skeletal muscle and heart tissues. Kumaran S, Savitha S, Anusuya Devi M, Panneerselvam C.

    Department of Medical Biochemistry, Dr. AL Mudaliar Post Graduate Institute of Basic Medical Sciences, Uni

    Use of stimulators of glutathione synthesis as hair growth promotors

    The composition is topically, or otherwise administered, to stimulate intracellular glutathione synthesis. Specifically, the composition may include glutathione esters; L-2-oxothiazolidine-4-carboxylic acid; and esters of 2-oxothiazolidine-4-carboxylic acid.

    Although male pattern baldness has an unknown etiology, continual oxidative damage is part of aging. Oxidative damage coupled with reduced blood flow and follicle nutrition may play a substantial role in the mechanism of baldness. Treatment with a composition including an intracellular glutathione stimulator, that will function at least in part as an antioxidant, the inventor believes is clearly beneficial.

    According to Nappl and Kermici (Electrophoretic Analysis of Alkylated Proteins of Human Hair from Various Ethnic Groups, J. Soc. Cosmet. Chem., 40, 91-99, 1989.), cysteine, the disulfide form of cysteine, makes up 12.6 to 13.7% of the total amino acid composition of human hair. In addition, cysteine is the rate limiting substrate in the synthesis of glutathione, a major component at cellular antioxidant defenses.

    Pruche, Kermici and Prunieras, (Changes in Glutathione Content in Human Hair Follicle Keratinocytes as a Function of Age of Donor: Relation with Glutathione Dependent Enzymes, Int. Journal of Cosmetic Science 13, 117-124, 1991) demonstrate that glutathione content in hair follicles during the growth phase (anlagen) declines with aging. The activity of enzymes associated with glutathione (glutathione-S-transferase, gamma -glutamyl-transpeptidase, glutathione reductase, and glucose-6-phosphate dehydrogenase) also decline with age. In contrast, glutathione peroxidase, the enzyme directly involved in eliminating toxic lipid peroxides, does not decline (Kermici et al., Evidence for an Age-Correlated Change in Glutathione Metabolism Enzyme Activities in Human Hair Follicle, Mech. of Aging and Devel., 53, 73-84, 1990.).

    As a result, the direct antioxidant and capacity of the glutathione system may remain functional, but the ability to provide substrate for that system is clearly compromised as activity at the two enzymes which recycle intracellular glutathione, glutathione reductase and glucose-6-phosphate dehydrogenase, and the enzyme which leaves plasma glutathione allowing uptake of its constituent amino acids, gamma -glutamyl-transpeptidase, are all significantly reduced.

    Since cysteine is a major component of, the demand for this thiol containing amino acid in the growth phase hair follicles is high. If the glutathione recycling capacity of these cells is diminished, the requirement for cysteine to support glutathione synthesis would further increase the demand for this key amino acid. As gamma -glutamyl-transpeptidase activity also declines with age, an exogenous source of cysteine becomes critical to support hair growth and prevent oxygen radical induced follicle damage

    A number of intracellular glutathione stimulators are known, for example: glutathione esters; L-2-oxothiazolidine-4-carboxylic acid; and esters of 2-oxothiazolidine-4-carboxylic acid. Preferably, pursuant to the present invention, L-2-oxothiazolidine-4-carboxylic acid and 2-oxothiazolidine-4-carboxylic acid esters are utilized. L-2-oxothiazolidine-4-carboxylic acid and esters of 2-oxothiazolidine-4-carboxylic acid not only act as stimulators of intracellular glutathione synthesis, but also provide intracellular cysteine. As stated above, cysteine is a major amino acid component of hair and should contribute to hair growth and loss prevention, in addition to supporting glutathione synthesis.

    L-2-oxothiazolidine-4-carboxylic acid is transported into most cells where it is converted by the action of 5-oxo-L-prolinase in the presence of adenosine triphosphate to produce S-carboxyl cysteine. S-carboxyl cysteine is then decarboxylated to produce cysteine. Cysteine is then available for glutathione synthesis

  8. #8
    Senior Member Jacob's Avatar
    Join Date
    Apr 2005



    Cysteine is a non-essential amino acid used for protein synthesis. Although we make some cysteine in our cells, it is also the rate-limiting amino acid for the synthesis of glutathione, a small molecule that plays many essential roles in cells. Cysteine is unstable, somewhat toxic, and weakly mutagenic when taken orally or by injection. But procysteine, a modified form of cysteine, is somewhat less toxic, and much more stable "on the shelf" than cysteine (White et al., 1993). It is rapidly converted into cysteine and carbon dioxide inside cells. This conversion makes it good for raising intracellular concentrations of cysteine, which, in turn, raises intracellular levels of glutathione.

    Glutathione is made up of three amino acids, linked together like the amino acids in normal proteins. But, glutathione is a small molecule. It is important in many cellular functions including the folding of proteins into their correct structures. It also is an antioxidant (Kehrer and Lund, 1994) that detoxifies free radicals directly by interacting with them. And, it also is an important contributor to the detoxification of many free radicals and foreign chemicals by enzymes (Hayes and Pulford, 1995; Talalay et al., 1995). For example, it aids in the enzymatic detoxification of lipid peroxides and hydrogen peroxide.

    The synthesis of glutathione is often limited by the supply of free cysteine. The concentration of free cysteine is very low in plasma. Low levels of glutathione lead to a decrease in intracellular antioxidant activities, and a decrease in the activities of the enzymes which depend on correct intracellular oxidation-reduction potential for their structure and activity.

    There are no large clinical trials that demonstrate health benefits from glutathione or NADH supplementation. But a decrease in glutathione levels has been found in aging animals and humans, and in various disease states (Meydani et al., 1995). Glutathione levels decrease in the lens of the eye as we age. Lower glutathione levels have been found in the lens, spleen, liver, kidney and heart of old mice compared to young mice. In one study, half of elderly subjects had lower blood glutathione concentrations than younger subjects. There is a positive correlation between tissue glutathione levels and lifespan in mice. Glutathione inhibits liver cancer growth in humans and oral cancer in hamsters. Thus, the decline in glutathione levels with age may be related to the increase in cancer.

    The decrease in glutathione levels with age also may partly explain the age-related decrease in immunity. And, decreased glutathione may partly be responsible for the liver's loss of detoxification ability. This loss is found in most mammals, including humans. Low glutathione levels are associated with arthritis, diabetes, heart disease and cataracts.

    In clinical studies in the elderly, higher glutathione levels are associated with fewer illnesses and the perception of improved health. Finally, dietary supplementation with glutathione, or with supplements that raise glutathione levels, appears to improve the immune response in humans and experimental animals.


    NADH (a form of nicotinamide adenine dinucleotide) is a coenzyme that assists enzymes involved in energy production within mitochondria. NADH plays an important role in the generation of ATP, the body's energy currency, and has been found to be deficient in several age-related degenerative diseases. Uncontrolled studies in Europe have found NADH beneficial for patients suffering from Parkinson's disease, Alzheimer's disease, and depression (Birkmayer, et al, 1990).

    NADH also is needed for the regeneration of glutathione after it becomes oxidized (Sies and Stahl, 1995; Kehrer and Lund, 1994). If NADH levels are depleted, glutathione levels also may fall. Thus, supplementation with NADH also may help restore glutathione to its active form.
    Glutathione enhances fibroblast collagen contraction and protects keratinocytes from apoptosis in hyperglycaemic culture

    Background Cutaneous wound healing is relatively slow in patients with diabetes. Objectives To test the hypothesis that this defect in healing of wounds in patients with diabetes results from dysfunction of skin fibroblasts and epidermal keratinocytes and that this dysfunction is related to disrupted intracellular glutathione (GSH) homeostasis. Methods We investigated the effects of esterified GSH on the contraction of fibroblasts in a fibroblast-populated collagen lattice and on keratinocyte apoptosis. Results High glucose medium (hyperglycaemia) reduced the contraction ability of fibroblasts (P < 0.05). The normalization of glucose medium concentrations for hyperglycaemic fibroblasts did not restore the contraction capacity. The percentage of apoptotic keratinocytes was statistically higher in hyperglycaemic cells (P < 0.05). GSH media concentrations ranging from 0.1 to 100 µmol L-1 restored the ability of hyperglycaemic fibroblasts to contract the gels in a concentration-dependent manner. Primary human keratinocytes grown in hyperglycaemic medium were more susceptible to apoptosis, and treatment with esterified GSH rescued the keratinocytes from apoptosis. Conclusions These data suggest that intracellular GSH can normalize skin cell functions disrupted by in vitro cell growth under hyperglycaemic conditions.

  9. #9
    Senior Member Jacob's Avatar
    Join Date
    Apr 2005


    Glutathione, glutathione S-transferase and reactive oxygen species of human scalp sebaceous glands in male pattern baldness.Giralt M, Cervello I, Nogues MR, Puerto AM, Ortin F, Argany N, Mallol J. Unit of Pharmacology, School of Medicine, University "Rovira i Virgili," Reus, Spain.

    We investigated the contribution of reactive oxygen species to the development of sebaceous gland hyperplasia and the characteristics of the glutathione S-transferase/glutathione system in male pattern baldness. Glutathione S-transferase, glutathione, and thiobarbituric acid-reactive substances were determined in sebaceous gland-enriched scalp skin of men affected by male pattern baldness and were subjected to hair autotransplantation. In comparison with the hairy occipital-donor areas, the following results were obtained in alopecic frontoparietal samples: glutathione S-transferase-specific activity increased 7-fold (p < 0.001); enzyme affinity towards 1-chloro-2,4-dinitrobenzene decreased 2-fold (p = 0.009); glutathione content decreased 2.5-fold (p = 0.017); and thiobarbituric acid reactive substances increased 2-fold (p = 0.006). Chromatofocusing analysis, bromosulfophthalein IC50 values, enzyme-linked immunosorbent assay, and immunohistochemistry with polyclonal antibodies raised against glutathione S-transferases alpha, mu, and pi demonstrated the presence of alpha, pi, and probably the 5.8 alpha isoenzymes in the sebaceous gland. These results support the hypothesis that reactive oxygen species are involved in the pathogenesis of sebaceous gland hyperplasia in male pattern baldness.

  10. #10
    Senior Member Hoppi's Avatar
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    Feb 2010
    Kent, UK
    (I'll fill this in later)


    I love glutathione! I increase it with NAC supplementation to help mercury chelation and strengthen and cleanse my liver! But I'm sure it's doing more stuff too! Apparently it's a v v strong antioxidant ^_^

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