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juillet 2019   01 02 03 04 05 06 07 08 09 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31


Supplements useful to improved Glutathione functioning according to Wiki:

cysteine-rich foods - ??
NAC (N-acetylcysteine)
Alpha lipoic acid
SAMe (S-adenosylmethionine)
Calcitriol (for vitamin D)
silymarin (Milk Thistle herb)


Hypothesis: Glutathione, the ATP, sulphur-related anti-oxidant and reducer, (see also MSM), is a fundamental agent associated with, (non-anaerobic and non-ketone), metabolism of carbs (etc.), via the utilisation of and control of oxidative processes, ending in the production of lactic acid, (etc.). Therefore, it is highly suspect in the early development of diseases such as Alzheimers, TBI/dementia, Diabetes, CFS, etc., near the point of pathogen or toxin/antigen incursion and inflammatory immune or allergic-type responses. Therefore, it may have some close relation to endorphin tags, the establishment of aerobic/anaerobic thresholds, and potential migraine-type spasming via local vs electromagnetic field differentials, and related neurotransmitter and hormonal dysregulations.

Hypothesis: Glutathione is importantly related to protein kinase, cell regeneration and memory-establishment.

Hypothesis: Local spasming events as referenced above are responsible for many recurring, i.e., "stationary," sunspot-like points of neural "anxiety spirals," where there is disorders of neurochemical functions, as in endorphin or endocrine process completions, resulting in grounded local brain disorders producing OCD, Schizophrenia, Autism, Social Anxiety Disorder, and other brain disorders, their individual differences depending upon their individual locations within the brain. Even if Glutathione itself is not essential to such events or processes, this does not in itself negate that such processes may occur generally in the ways suggested.

Hypothesis: Dysregulation of the nitric oxide cycle, as with poor Glutathione function, triggers movement into anaerobic, non-carb ketone utilisation, and associated endorphin tag resetting, probable stress-learning. This movement would normally be associated w/ lactic acid production, (during low oxidative stress), but since Glutathione function is poor, then lactic acid production is greatly retarded, as in CFS, indicating high oxidative stress, dangerously incorrect anaerobic threshold.

Hypothesis: Sluggish liver caused by illnesses of poor (carb) metabolic or oxidative utilisation results in insufficient release of, e.g., supplementary ketone bodies, Glutathione, enzymes, etc., and so a feedback cycle of high stress and chronic illness results. (Poor liver function comparable to poor peristalsis, kidney, pancreatic, immune, etc, function, and resulting loops).



- Snippets from Wiki - https://en.wikipedia.org/wiki/Glutathione - - - - - - - - -

GLUTATHIONE:

ATP cycle -

Cells make Glutathione in two adenosine triphosphate (ATP)-dependent steps.


Deficiency -

Glutathione deficiency states include, but are not limited to, HIV/AIDS, chemical and infectious hepatitis, myalgic encephalomyelitis chronic fatigue syndrome ME / CFS,[45][46][47] prostate and other cancers, cataracts, Alzheimer's disease, Parkinson's disease, chronic obstructive pulmonary disease, asthma, radiation poisoning, malnutritive states, arduous physical stress, and aging, and has been associated with suboptimal immune response. ....

Low glutathione is also strongly implicated in wasting and negative nitrogen balance,[50] as seen in cancer, AIDS, sepsis, trauma, burns and even athletic overtraining...

Schizophrenia and bipolar disorder are associated with lowered glutathione. Accruing data suggest that oxidative stress may be a factor underlying the pathophysiology of bipolar disorder (BD), major depressive disorder (MDD), and schizophrenia (SCZ). Glutathione (GSH) is the major free radical scavenger in the brain.[52] Diminished GSH levels elevate cellular vulnerability towards oxidative stress; characterized by accumulating reactive oxygen species. GSH depletion has also been implicated in cellular predisposition to apoptosis.[53] Replenishment of glutathione using N-acetyl cysteine has been shown to reduce symptoms of both disorders.[54]

Excess glutamate at synapses, which may be released in conditions such as traumatic brain injury, can prevent the uptake of cysteine, a necessary building-block of glutathione. Without the protection from oxidative injury afforded by glutathione, cells may be damaged or killed.[60]


Supplements -

Research suggests that glutathione taken orally is not well absorbed across the gastrointestinal tract. ... However, it is possible to increase and maintain appropriate glutathione levels by increasing the daily consumption of cysteine-rich foods and/or supplements.[28]

Calcitriol, the active metabolite of vitamin D synthesized in the kidney, increases glutathione levels in the brain and appears to be a catalyst for glutathione production.[29]

In addition, plasma and liver GSH concentrations can be raised by administration of certain supplements that serve as GSH precursors. N-acetylcysteine, commonly referred to as NAC, is the most bioavailable precursor of glutathione.[30] Other supplements, including S-adenosylmethionine (SAMe)[31][32][33] and whey protein[34][35][36][37][38][39] have also been shown to increase glutathione content within the cell.

NAC is available both as a drug and as a generic supplement. Alpha lipoic acid has also been shown to restore intracellular glutathione.[40][41] Melatonin has been shown to stimulate a related enzyme, glutathione peroxidase,[42] and silymarin, an extract of the seeds of the milk thistle plant (Silybum marianum), has also demonstrated an ability to replenish glutathione levels in lab rats.[43][44]


Dopamine -

Glutathione has recently been used as an inhibitor of melanin in the cosmetics industry. In countries like Japan and the Philippines, this product is sold as a skin whitening soap. Glutathione competitively inhibits melanin synthesis in the reaction of tyrosinase and L-DOPA by interrupting L-DOPA's ability to bind to tyrosinase during melanin synthesis. The inhibition of melanin synthesis was reversed by increasing the concentration of L-DOPA, but not by increasing tyrosinase. Although the synthesized melanin was aggregated within one hour, the aggregation was inhibited by the addition of glutathione. These results indicate that glutathione inhibits the synthesis and agglutination of melanin by interrupting the function of L-DOPA."[21]


Regulation of nitric oxide cycle -

Regulation of the nitric oxide cycle, which is critical for life but can be problematic if unregulated[17]


Sulphur, (oxygen utilisation) ...

Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. In the process, glutathione is converted to its oxidized form glutathione disulfide (GSSG), also called L-(–)-glutathione.

In plants - APS reductase, an enzyme of the sulfur assimilation pathway uses glutathione as electron donor.


oxidative stress -

In healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (GSH) and less than 10% exists in the disulfide form (GSSG). An increased GSSG-to-GSH ratio is considered indicative of oxidative stress.

The ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity.[3]


Lactic acid product from detox

Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-lactoyl-glutathione to glutathione and D-lactic acid.

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