Glutathione—nutritional and pharmacologic viewpoints: part V

Nutrition, 2001

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes more and more evident that depletion of GSH is associated with severe disease states. (1) From this perspective, the possibility of manipulating the availability of GSH becomes a very attractive form of treatment. In view of the strong correlation between the plasma

Nutrition, 2001

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes

Nutrition, 2002

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes

Nutrition, 2001

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes

Nutrition, 2001

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes

Nutrition, 2001

GSH is quantitatively the most import biological antioxidant and scavenger. In addition it has a number of important functions in amino acid transport across membranes, in protein synthesis and degradation, in gene regulation and in cellular redox regulation. It becomes

Indian journal of experimental biology, 2000

abundant intracellular thiol compound present in virtually all mammalian tissues -• Functions of GSH in reductive processes are essential for the synthesis and also degradation of proteins, formation of the deoxyribonucleotid precursors of deoxyribonucleic acid (DNA), regulation of enzymes, and protection of the cells against reactive oxygen species and free radicals produced even in normal metabolism•. By its multifunctional properties GSH attracts the interest of researchers in various subjects such as enzyme mechanisms, biosynthesis of macromolecules, intermediary metabolism, drug metabolism, radiation, cancer, oxygen toxicity, transport, immunology, endocrinology, environmental toxins, aging and exercise·-. Most of the new information about GSH biochemistry is produced with selective inhibitors of the enzymes involved in GSH turnover. Selective modulation of GSH metabolism also makes new therapeutic approaches possible• Glutathione metabolism still looks promising to scientists ...

Glutathione (␥-glutamyl-cysteinyl-glycine; GSH) is the most abundant low-molecular-weight thiol, and GSH/ glutathione disulfide is the major redox couple in animal cells. The synthesis of GSH from glutamate, cysteine, and glycine is catalyzed sequentially by two cytosolic enzymes, ␥-glutamylcysteine synthetase and GSH synthetase. Compelling evidence shows that GSH synthesis is regulated primarily by ␥-glutamylcysteine synthetase activity, cysteine availability, and GSH feedback inhibition. Animal and human studies demonstrate that adequate protein nutrition is crucial for the maintenance of GSH homeostasis. In addition, enteral or parenteral cystine, methionine, N-acetylcysteine, and L-2-oxothiazolidine-4-carboxylate are effective precursors of cysteine for tissue GSH synthesis. Glutathione plays important roles in antioxidant defense, nutrient metabolism, and regulation of cellular events (including gene expression, DNA and protein synthesis, cell proliferation and apoptosis, signal transduction, cytokine production and immune response, and protein glutathionylation). Glutathione deficiency contributes to oxidative stress, which plays a key role in aging and the pathogenesis of many diseases (including kwashiorkor, seizure, Alzheimer's disease, Parkinson's disease, liver disease, cystic fibrosis, sickle cell anemia, HIV, AIDS, cancer, heart attack, stroke, and diabetes). New knowledge of the nutritional regulation of GSH metabolism is critical for the development of effective strategies to improve health and to treat these diseases. J. Nutr. 134: 489 -492, 2004.

Biological Chemistry, 2000

Glutathione (GSH) plays an important role in a multitude of cellular processes, including cell differentiation, proliferation, and apoptosis, and as a result, disturbances in GSH homeostasis are implicated in the etiology and/or progression of a number of human diseases, including cancer, diseases of aging, cystic fibrosis, and cardiovascular, inflammatory, immune, metabolic, and neurodegenerative diseases. Owing to the pleiotropic effects of GSH on cell functions, it has been quite difficult to define the role of GSH in the onset and/or the expression of human diseases, although significant progress is being made. GSH levels, turnover rates, and/or oxidation state can be compromised by inherited or acquired defects in the enzymes, transporters, signaling molecules, or transcription factors that are involved in its homeostasis, or from exposure to reactive chemicals or metabolic intermediates. GSH deficiency or a decrease in the GSH/glutathione disulfide ratio manifests itself large...