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THE
IMPORTANCE OF GLUTATHIONE (GSH) IN HUMAN HEALTH
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• Glutathione Metabolic Functions
• Glutathione Deficiency States
• Glutathione And The Role Of Cysteine And Cystine
In GSH Synthesis
• Cystine to Cysteine
• Non-toxic Cystine Source
• Glutathione Conclusion |
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Glutathione Metabolic
Functions
Glutathione is
often referred to as GSH. GSH’s metabolic functions include
(Gutman, 1998):
• Enhancement of Immune Function
• Elimination of Toxins
• Elimination of Carcinogens
• Antioxidant Cell Protection
• Protection against Ionizing Radiation
• DNA Synthesis and Repair
• Protein Synthesis
• Prostaglandin Synthesis
• Leukotriene Synthesis
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Glutathione Deficiency
States
Cellular depletion of glutathione has been implicated as a causative, or contributory
factor in many pathologies including Parkinson's, Alzheimer's, cataracts, arteriosclerosis,
cystic fibrosis, malnutrition, aging, AIDS and cancer (Bounous et al., 1991).
In addition, glutathione is essential in supporting the immune system, including
natural killer cells (Droege et al., 1997) and in the maintenance of T-lymphocytes
(Gutman, 1998). Recent research indicates that propensities toward many degenerative
diseases and aging itself are related to the capacity of the cell to robustly
recover from oxidative insult. The capacity of a cell to recover from such
insult can be determined by measuring the intracellular stores of glutathione
(Noelle et al., 1981).
The liver is the main detoxification organ of the body. In the liver we find
very high concentrations of GSH, as it is a major factor in numerous biochemical
detoxification pathways. Numerous studies have demonstrated that patients with
compromised liver function due to alcohol abuse have significant reduction
of GSH in the liver (Lamestro, 1995).
Now that we’ve laid a foundation for the importance of glutathione, let’s
discuss glutathione and the role of cysteine and cystine in glutathione synthesis.
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Glutathione And
The Role Of Cysteine And Cystine In GSH Synthesis
Glutathione (GSH) is a pre-eminent
cellular antioxidant which is abundant in cytoplasm, nuclei and
the mitochondria. Glutathione
(GSH) is a very small molecule made intracellularly from three
amino acids and is referred to as a tripeptide. When naturally
occurring within the body GSH is synthesized in a series of biochemical
reactions which require ATP, magnesium and its three precursor components – glutamine, cysteine, and glycine. Of these three
amino acids cysteine is the hardest to find thus, glutamate and
glycine deficiencies are minor compared to the body’s deficiency
of cysteine. Cysteine is a sulfur containing amino acid. Cysteine
(the sulfhydryl group [SH]) provides glutathione with its biological
potency. In general, the rate of synthesis of gamma-glutamylcysteine
determines the rate of synthesis of glutathione (DeLeve, 1991).
In other words, when cells have cysteine, they can
efficiently manufacture GSH.
However, this amino-acid is not only absent or deficient in many diets; it
must also be available in an accessible form the cells can utilize.
The challenge is in providing
cysteine for the production of intracellular glutathione. Consumption
of cysteine itself is
problematic in a number of regards. Free cysteine is toxic (Meister,
1984; Baruchel et at., 1996) and is poorly absorbed and transported.
Another form N-acetyl-L-cysteine (NAC) is an amine protected version
of cysteine. It is rapidly hydrolyzed in the body to the amino
acid cysteine. However, NAC must be taken every couple of hours
because it’s only effective 1-2 hours. Oral dosage toxic
side effects can include headaches, dizziness and blurred vision.
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Cystine to Cysteine
However, there is a form of cysteine that is non-toxic,
easily transported into the gut, and transferred into cells. This
nontoxic, easily transported cysteine is in the form of a non-denatured
cystine that is comprised of two cysteine molecules joined together
by a disulfide bond. Upon cell entry this cystine is reduced to
cysteine (Droege et al., 1994).Having established that non-denatured cystine is the crucial element in supporting
intracellular glutathione production, let's discuss where we best find it.
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Non-toxic Cystine Source
The greatest source of cystine
is found in labile bioactive
whey proteins i.e. alpha-lactalbumin,
serum albumin, and lactoferrin. However,
in the manufacturing process, during the separation of whey components,
there is significant denaturation that
is caused by mechanical stress, heat, acid, alkali, and other
agents. Denatured proteins lose biological activity, though not
nutritional value. However, the glutathione precursors found
in this source must have biological activity in order to be effectively
utilized in the glutathione pathway. IMUPlus is
such a product. |
Technically speaking, the non-denatured labile alpha-lactalbumin has
4 cystine residues. Non-denatured serum albumin has 17 cystine residues and
6 glutamylcystine (Glu-Cys) dipeptides
and non-denatured lactoferrin has
17 cystine residues and 4 Glu-Cys dipeptides.
So, it is obvious that a product high in the non-denatured conformation of
these proteins is essential for increasing intracellular glutathione levels.
IMUPlus utilizes proprietary processes to
configure a specialized formula of pure bioactive polypeptides
and glycopeptides that are abundantly rich in non-denatured bioactive alpha-lactalbumin, lactoferrin,
lysozyme, lactoperoxidase, glycomacropeptides,
and bovine serum albumin. The formula is protective packaged in
an individual serving packet preserving the fragile labile bioactive
components to assure biological activity is delivered to consumer.
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Glutathione Conclusion
Because every system in the body can be affected
by the state of the glutathione system, especially the immune system,
the nervous system, the gastrointestinal, and the pulmonary system,
it’s easy to understand why experts say, “We literally
can’t survive without this miraculous antioxidant” and “Your
life depends on glutathione” .
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“What You Should Know About the
Super Antioxidant Miracle”, Earl Mindell, R.Ph.,Ph.D.
“Glutathione - Your Body’s Most Powerful Protector”, Jimmy
Gutman, MD, FACEP |
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