Mold and Glutathione

Posted On October 20, 2020 at 6:55 am by / No Comments

Mold and Glutathione

Glutathione :

  • A tripeptide of cysteine, glutamine and glycine
  • Protects from reactive oxygen species
  • Protects from reactive nitrogen species
  • Cofactor for many antioxidant enzymes such as peroxidases and transferases
  • Storage form of cysteine
  • Storage form and transporter of nitric oxide
  • Metabolizes estrogens, leukotrienes, and prostaglandins
  • Involved in regulation of some transcription factors
  • Detoxifies many endogenous substances and  xenobiotics, mycotoxins and other toxins


Two Forms Of Glutathione

Glutathione exists in two forms. It is found in an oxidized form and a free or reduced form. Only the free or reduced form has antioxidant activity. Once it is used and therefore oxidized, it needs to be recycled back to the reduced form again before it can continue with its antioxidant behavior.    It is recycled back, and fourth, over, and, over again. The oxidized form is called glutathione disulfide (GSSG) and the reduced form is called glutathione (GSH). GSH is used by the body to neutralize reactive oxygen species which leads to its alteration into GSSG from GSH. (loses it’s super hero antioxidant powers when it is oxidized) The GSH needs the enzyme glutathione peroxidase to help it reduce free radicals. Glutathione is oxidized to GSSG in this process. Only GSH has the antioxidant activity. Think of the glutathione (GSH) as a super hero. It saves the body from damage by being oxidized into (GSSG), rather than allowing free radicals to oxidize important cellular components in our body (damaging mitochondria). Basically, it takes the hit to save our body from damage. However, to be able to continue functioning as an antioxidant, it has to change back into the reduced form and regaining it’s super hero powers.

Low levels of glutathione peroxidase are seen in vitiligo (H. Zedan, 2015), relapsing-remitting multiple sclerosis (k. Socha, 2014), and type 2 diabetes (O. Sedighi, 2014) and thought to be a contributing factor in these diseases.

  • Glutathione peroxidase genetic polymorphisms may also be associated with development of celiac disease. (M. Katar, 2014)
  • The liver toxic effects of acetaminophen, a drug responsible for considerable drug-induced liver injury are brought on with excessive doses of this common pain and fever drug. This is associated with rapidly depleted intracellular GSH reserves and can be treated with n-acetylcysteine (NAC) the first 48 hours after overdose.

The most common symptom is nausea

How to increase Glutathione!


  • Turmeric – Curcuma longa
  • Milk thistle – Silybum marianum
  • Cinnamonum – Cinnamon (human study did not specify species)
  • Cordyceps – Coryceps sinensis/militaris  (okay, a mushroom and not technically an herb)
  • Gotu kola – Centella asiatica

Milk thistle – Silybum marianum: 1 Tablespoon BID Milk thistle contains a mixture of several related polyphenolic compounds called silymarin. Silymarin is an antioxidant which lowers the liver’s oxidative stress associated with toxin metabolism, particularly lipid peroxidation, which has the effect of conserving cellular glutathione levels. Like NAC, silymarin can protect against acetaminophen toxicity (possibly by the similar mechanism of preserving glutathione levels). Silymarin, however, may be a more effective antidote than NAC for acetaminophen toxicity if the treatment is delayed (in an animal model, it was effective when administered up to 24 hours after overdose).

Turmeric – Curcuma longa: Curcumin induces gstA gene expression and overall glutathione activity.

Cordyseps – Cordyseps sinensis research shows it increases glutathione peroxidase. Glutathione peroxidase is a necessary enzyme to help glutathione act as an antioxidant.

Mold and Mycotoxins

Mycotoxins can decrease the formation of glutathione by decreasing gene expression of the enzymes needed to form glutathione. In humans this chronic depletion of glutathione has been shown to lead to chronic health conditions, including chronic asthma and nuerological issues. A decrease in glutathione due to mycotoxin-related depletion may contribute to the range of conditions associated with mycotoxin accumulation. Since the mycotoxins destroy the action of the enzymes necessary for glutathione production, glutathione may need to be supplemented rather than supplementing the rate limiting amino acid as n-acetyl-cysteine. Glutathione has been beneficially used in animal research of aflatoxin-related hepatocellular carcinoma. Clinicians and individuals with mold related illness, or also called CIRS due to water-damaged buildings, suggest that studies using liposomal glutathione in the management of mycotoxin-related conditions is warranted. Acetyl-glutathione is used with good results also. I use an acetylated form of glutathione as it has better absorption when acetylated. By acetylating it, the glutathione is not oxidized and broken down into it’s componant amino acids as other gluathiones usually are. The acetylation of the glutathione Nebulized glutathione is also used but should only be used under the care of a trained practitioner. Bronchoconstriction has occured among patients some patients.

Glutathione depletion in antigen presenting cells inhibits Th1-associated cytokine production and/or favors Th-2-associated responses. Multiple chemical sensitivities in individuals are thought to be associated with decreased Th-1, increased Th-2 response. Mycotoxins (as well as other toxins) can deplete the body of glutathione and could add to the problems with an improper antigen presenting cells activity that has already be theorized to be an issue for people with mold sensitivity.

Emothion & N-Acetyl-Cysteine
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Research is proving that oxidative stress is a significant factor in the pathophysiology of mycotoxin-related illness. Oxidative stress appears to be directly related to suppression of glutamate-cysteine ligase catalytic subunit (GCLC), gene function, post-translational modification of Nrf2 or the presence of excess transforming growth factor-beta (TGF-β). This suggests that the lack of glutathione may be due to the inability of mycotoxin-affected cells to adequately form glutathione.

The demonstration that the oxidative stress associated with mycotoxins can be related to direct suppression of enzymes for glutathione synthesis, post-translational modification of Nrf2 or the presence of excess TGF-β suggests that the lack of glutathione may be due to the inability of mycotoxin-affected cells to adequately form glutathione. Decreased function of the enzymes of glutathione production results in a microenvironment depleted of glutathione on a chronic basis. In humans, deficiency of glutathione can lead to chronic conditions. Mycotoxin-related depletion of glutathione may contribute to the range of conditions associated with mycotoxin accumulation. The lack of function of the enzymes of glutathione production in these conditions suggests that more efficient resolution of the effects of glutathione depletion may require the administration of the complete glutathione molecule. These observations echo an early report regarding the benefit of glutathione in the management of aflatoxin-related hepatocellular carcinoma in an animal model, which proposed that administration of the intact glutathione molecule was needed for benefit of the use of glutathione.


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