Re: Glutathione as a Chelator of heavy metals

[Guest guest]

In a message dated 22/12/2006 16:38:30 GMT Standard Time, richvank@...

writes:

Over the very long term, I suspect that if the glutathione level could

be raised to near normal, glutathione would eventually take out quite

a bit of mercury. The reason is that there is a dynamic equilibrium

in chemistry. That is, the atoms of mercury are continually in

motion, coming loose from their binding sites, and rebinding at other

sites. If the glutathione concentration is high enough, it should be

able to grab some of this mercury in between binding sites, and over

the long term, it will take mercury out.

Rich

***It took me a year to raise my glutathione unti i stopped noticing an

improvement. I bvelive it does replenish glutathione and chelate heavy metals

which are " easier to grab " .

Regards

CS

[Guest guest]

Andy cutler on glutathione :-

" Neither NAC nor glutathione remove any mercury from the brain "

go to :- frequent-dose-chelation/

to learn whats best .

>

> WHY GLUTATHIONE IS A CHELATOR OF HEAVY METALS

> (taken from The Detoxx Book by MD, Kane MD, and

> Neal Speight MD)

>

> In Chapter 7 of the Doctor's Book they say that Glutathione (GSH)

> performs many vital physiological and metabolic functions within all

> cells. It is a potent reducing agent with many actions at the

> molecular, cellular and tissue levels because of its impact as a

> systemic anti-toxin. They think that the glutathione status of a

> cell, the excess of reduced glutathione (GSH) over oxidized

> glutathione (GSSG) may be one of the most accurate indicators of

> cellular health.

>

> GSH is the most abundant nonprotein thiol in the body and it provides

> the reactive thiol (SH) group which is responsible for the varied

> functions of GSH which include –

>

> • Maintenance of protein structure and function

> • Regulation of protein synthesis and degradation

> • Stabilisation of immune function

> • Protection against oxidative damage

> • DETOXIFICATION OF REACTIVE CHEMICALS

>

> GSH also serves as a storage and transport functions in –

>

> • Leukotriene and prostaglandin metabolism

> • Reduction of ribonucleotides to deoxyribonucleotides

> • Modulation of microtubule-related processes

> • Formation of bile

>

> GSH is a tripeptide formed by linking 2 amino-acids, L-glutamate, L-

> cysteine and glycine. The liver is the major site of biosynthesis of

> GSH and has the greatest concentration of it followed by the spleen,

> kidney, lens, erythrocytes and leukocytes.

>

> It is a complicated system that keeps GSH in the form that enables it

> to perform the vital functions mentioned above; oxidant stress will

> overwhelm the system and stop it from working leading to the

> depletion of the intracellular pool of GSH. It can also be depleted

> when GSH is conjugated to foreign compounds.

>

> Proteins may be activated or inhibited by the exchange between

> protein and GSH.

>

> GSH plays a major role in detoxifying many reactive metabolites by

> binding to endogenous compounds which serves to –

>

> • Limit and regulate the reactivity of chemicals

> • Facilitate membrane transport and elimination from the cell

> • May lead to the formation of essential biological mediators

>

>

>

>

> GSH forms metal complexes via non-enzymatic reactions. It plays a

> crucial role in metal transport, storage and metabolism being one of

> the most versatile metal binding ligands in the body. GSH contains 6

> potential co-ordination sites for metal binding; the cysteinyl

> sulfhydryl, the glutamyl amino, the glycl and glutamyl carboxyl

> groups and 2 peptide linkages.

>

> Mercury may bind to a variety of enzyme systems with a particular

> affinity for ligands containing sulfhydryl groups. GSH is the major

> dialyzable methyl mercury binding substance in the brain and may bind

> up to 30% of cellular methylmercury.

>

> A considerable amount of methymercury is excreted into bile when

> adequate concentration biliary GSH is available thus the primary

> mechanism for removal of mercury is through its bond with GSH via

> bile, however a sluggish biliary flow due to biliary congestion

> renders an impaired elimination of Hg.

>

> Oral loading of L-cystine and N-acetyl cysteine (NAC) would be

> contraindicated in the mercury compromised patient in that these

> compounds may facilitate redistribution of mercury from tissues

> throughout the body and exacerbate the adverse neurological impact of

> mercury.

>

> However the supplementation of branched chain amino acids and L-

> Phenylaline would be supportive to the metal toxic patient and

> inhibit the transport of the methylmercury complex across the blood

> brain barrier. Although the oral use of methionine might be

> considered in patients with disturbed methylation pathways, as is

> often the case in states of neurotoxicity, methionine may stimulate

> homocystine synthesis. In addition the use of methionine can

> suppress the release of GSH from the liver.

>

> Neurotoxins may present in tandem as pathogenic and heavy metal

> burdens as mercury, lead, cadmium and arsenic. Both pathogenic and

> heavy metals are lipid soluble and may reside in the liver and

> biliary tree. Removal of mercury is challenging due to its

> lipophilic nature.

>

> The administration of DMPS and DMSA can mobilize heavy metals such as

> mercury yet may cause serious side effects in patients with

> neurological involvement.

>

> Conversely the use of an IV Glutathione fast push can safely and

> efficiently relieve the body burden of heavy metals, biotoxins,

> endogenous and exogenous toxins.

>

> (My question is will other forms of GSH such as lipoceutical GSH do

> the same thing?)

>

> Pam

>

[Guest guest]

Hi, all.

The paper by Aposhian et al. reported that adding glutathione to rats

did not result in more removal of mercury from either the kidneys or

the brain, at least over a short time period.

I think the reason for this is that the bond strength of mercury to

glutathione is similar to the bond strength of mercury to sulfur atoms

in enzymes and other proteins. Thus, glutathione is not able to

compete strongly for the mercury once it is already bound in the body.

In a healthy person, in which the glutathione level in the cells is

normal, and the glutathione transferase enzymes are normal, I think

that the reason glutathione is able to detox the mercury about as fast

as it comes in, is that the concentration of mercury is so high in the

cells (millimolar levels) that it is able to compete effectively just

on an a priori probability basis, i.e., it offers so many binding

sites that it gets most of the mercury before it binds to enzymes or

other proteins.

Over the very long term, I suspect that if the glutathione level could

be raised to near normal, glutathione would eventually take out quite

a bit of mercury. The reason is that there is a dynamic equilibrium

in chemistry. That is, the atoms of mercury are continually in

motion, coming loose from their binding sites, and rebinding at other

sites. If the glutathione concentration is high enough, it should be

able to grab some of this mercury in between binding sites, and over

the long term, it will take mercury out.

Rich

>

> Andy cutler on glutathione :-

> " Neither NAC nor glutathione remove any mercury from the brain "

> go to :- frequent-dose-

chelation/

> to learn whats best .

>