Oxidation and Damage to DNA, Protein, and Lipids

Oxidative damage to DNA, proteins and other macromolecules accumulates with age and has been postulated to be a major, but not the only, type of endogenous damage leading to aging. Superoxide(O2.-), hydrogen peroxide (H2O2), and hydroxyl radical (.OH), which are mutagens produced by radiation, are also by-products of normal metabolism. Lipid peroxidation gives rise to mutagenic lipid epoxides, lipid hydroperoxides, lipid alkoxyl and peroxyl radicals, and enals ([[alpha]], ß-unsaturated aldehydes). Singlet oxygen, a high energy and mutagenic form of oxygen, can be produced by transfer of energy from light, the respiratory burst from neutrophils, or lipid peroxidation.

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Animals have numerous antioxidants defenses, but since these defenses are not perfect, some DNA is oxidized. Oxidatively damaged DNA is repaired by enzymes that excise the lesions, which are then excreted in the urine. We have developed methods to assay several of these excised damaged bases in the urine of rodents and humans almost all of which appear as the free base from repair by glycosylases. We estimate that the number of oxidative hits to DNA per cell per day is about l00,000 in the rat and about l0,000 in the human. DNA repair enzymes efficiently remove most, but not all, of the lesions formed. Oxidative lesions in DNA accumulate with age, so that by the time a rat is old (2 years) it has about two million DNA lesions per cell, which is about twice that in a young rat. Mutations also accumulate with age . For example, the somatic mutation frequency in human lymphocytes, of which the contribution of oxidative DNA lesions is unknown, is about nine times greater in elderly people than in neonates. The importance of oxidative DNA lesions in cancer and aging is underscored by the existence of specific repair glycosylases that excise these lesions from DNA. In the case of 8-hydroxy-2'-deoxyguanosine, a lesion formed from oxidative damage to guanine residues in DNA, loss of a specific glycosylase activity leads to an appreciable increase in the spontaneous mutation rate, indicating the intrinsic mutagenic potential of this DNA lesion. Many other oxidative DNA lesions are likely to be important as well.

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Mitochondrial DNA (mtDNA) from rat liver has more than ten times the level of oxidative DNA damage than does nuclear DNA from the same tissue. This increase may be due to a lack of mtDNA repair enzymes, lack of histones protecting mtDNA, and the proximity of mtDNA to oxidants generated during oxidative phosphorylation. The cell defends itself against this high rate of damage by a constant turnover of mitochondria, thus presumably removing those damaged mitochondria that produce increased oxidants. Despite this turnover, oxidative lesions appear to accumulate with age in mtDNA at a higher rate than in nuclear DNA.

Oxidative damage could also account for the mutations in mtDNA that accumulate with age

Endogenous oxidants also damage proteins. Stadtman and his colleagues have shown that the proteolytic enzymes that hydrolyze oxidized proteins are not sufficient to prevent an age-associated accumulation of oxidized proteins. In two human diseases associated with premature aging, Werner's syndrome and progeria, oxidized proteins accumulate at a much higher rate than is normal. Fluorescent age pigments, which are thought to be due in part to cross-links between protein and lipid peroxidation products, also accumulate with aging.

How much glutathione is enough?

Unfortunately, there is no Recommended Dietary Allowance (RDA) for glutathione to indicate how much is enough.

One hundred milligrams each day is the usual recommended dosage for glutathione.

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Glutathione Levels Predictably Declined With Age

Scientists at the University of Pavia found that Glutathione peroxidase (GSH-Px) levels also follow this age-related pattern up to about age 75 (Fig. 3), after which they noted a slight increase with age in a cross-sectional study (Fig. 4). They interpreted this as a self-selection process, which enabled those with the highest Glutathione peroxidase levels to survive the longest.

In another study of enzyme activity in the very old, Dr. Helle Anderson and colleagues at Odense University in Denmark compared the levels of Glutathione reductase (GR) in 41 centenarians between 100-105 years old, to that in 52 community controls between the ages of 60-79. They found that the mean Glutathione reductase (GR) activity was significantly higher in centenarians than in the group of younger elderly subjects, and that centenarians with the best functional capacity tended to have the highest GR activity.

They concluded that high GR activity appears likely to be associated with increased survival.8 In a later study, Lang’s group evaluatedGlutathione levels in 87 women in excellent physical and mental health, ranging in age from 60 to 103. The scientists found that all subjects had very high blood Glutathione levels. They followed these women for five years, and concluded that “high blood Glutathione concentrations … are characteristic of long-lived women.”

Glutathione ability to slow the aging process

Studies at the Louisville School of Medicine have clearly shown that Glutathione possesses the unique ability to slow the aging process.

While Glutathione aids in the protection of all cells and membranes, a study at Harvard Medical School found that Glutathione is especially able to enhance immune system cells, protecting against damage from radiation and helping to reduce the side effects of chemotherapy and x-rays and alcohol.

As a detoxifier of metals and drugs, Glutathione also aids in the treatment of blood and liver disorders.

As individuals grow older, Glutathione levels drop, and the ability to detoxify free radicals decreases.

It can protect against cadmium, copper, and acetaminophen (the active agent in Tylenol) toxicity. Glutathione aids the liver in detoxification, slows the aging process, helps the cardiovascular and immune systems, and is helpful in preventing or treating many other health conditions.

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Brief overview of Glutathione

The sheer amount of information on Glutathione is literally overwhelming. Due to the clinical terminology many of these documents are written in.

A brief overview of Glutathione:

Glutathione is a tri-peptide composed of three amino acids: Cysteine, Glutamic Acid and Glycine.

Glutathione and the enzymes it forms, such as GSH peroxidase, are essential to all life and are found in tissues of virtually all plants and animals. GSH is present in all human cells, with the highest levels found in the liver, the lenses of the eyes, pancreas, spleen and kidneys.

Glutathione acts as a powerful antioxidant, a key protector against all types of pollution and is effective in preventing aging. It protects DNA and RNA from free-radical damage.

Glutathione also protects against cellular peroxidation caused by exposure to pesticides, plastics, benzene and carbon tetrachloride, as well as heavy metals, cigarette smoke, smog, drugs, solvents, dyes, phenols and nitrates.

Glutathione works to inhibit the formation of free radicals, dangerous agents that suppress the immune system and promote the formation of mutagens and carcinogens. Free radicals also speed up the aging process, and it is due to this antioxidant activity that Glutathione is considered useful in the prevention and treatment of a wide range of degenerative diseases.

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