Magnesium and Cell Survival (Glutathione)

[1] Linus Pauling Institute http://lpi.oregonstate.edu/infocenter/minerals/magnesium/index.html#function

[2] Virginia Minnich, M. B. Smith, M. J. Brauner, and Philip W. Majerus. Glutathione biosynthesis in human erythrocytes. Department of Internal Medicine, Washington University School of Medicine, J Clin Invest. 1971 March; 50(3): 507–513. Abstract: The two enzymes required for de novo glutathione synthesis, glutamyl cysteine synthetase and glutathione synthetase, have been demonstrated in hemolysates of human erythrocytes. Glutamyl cysteine synthetase requires glutamic acid, cysteine, adenosine triphosphate (ATP), and magnesium ions to form ?-glutamyl cysteine. The activity of this enzyme in hemolysates from 25 normal subjects was 0.43±0.04 ?mole glutamyl cysteine formed per g hemoglobin per min. Glutathione synthetase requires ?-glutamyl cysteine, glycine, ATP, and magnesium ions to form glutathione. The activity of this enzyme in hemolysates from 25 normal subjects was 0.19±0.03 ?mole glutathione formed per g hemoglobin per min. Glutathione synthetase also catalyzes an exchange reaction between glycine and glutathione, but this reaction is not significant under the conditions used for assay of hemolysates. The capacity for erythrocytes to synthesize glutathione exceeds the rate of glutathione turnover by 150-fold, indicating that there is considerable reserve capacity for glutathione synthesis. A patient with erythrocyte glutathione synthetase deficiency has been described. The inability of patients’ extracts to synthesize glutathione is corrected by the addition of pure glutathione synthetase, indicating that there is no inhibitor in the patients’ erythrocytes.

[3] Braverman, E.R. (with Pfeiffer, C.C.)(1987). The healing nutrients within: Facts, findings and new research on amino acids. New Canaan: Keats Publishing

[4] http://www.dorway.org/blayautism.txt

[5] http://www.dorway.org/blayautism.txt

[6] Linus Pauling Institute http://lpi.oregonstate.edu/infocenter/minerals/magnesium/index.html#function

[7] Virginia Minnich, M. B. Smith, M. J. Brauner, and Philip W. Majerus. Glutathione biosynthesis in human erythrocytes. Department of Internal Medicine, Washington University School of Medicine, J Clin Invest. 1971 March; 50(3): 507–513. Abstract: The two enzymes required for de novo glutathione synthesis, glutamyl cysteine synthetase and glutathione synthetase, have been demonstrated in hemolysates of human erythrocytes. Glutamyl cysteine synthetase requires glutamic acid, cysteine, adenosine triphosphate (ATP), and magnesium ions to form ?-glutamyl cysteine. The activity of this enzyme in hemolysates from 25 normal subjects was 0.43±0.04 ?mole glutamyl cysteine formed per g hemoglobin per min. Glutathione synthetase requires ?-glutamyl cysteine, glycine, ATP, and magnesium ions to form glutathione. The activity of this enzyme in hemolysates from 25 normal subjects was 0.19±0.03 ?mole glutathione formed per g hemoglobin per min. Glutathione synthetase also catalyzes an exchange reaction between glycine and glutathione, but this reaction is not significant under the conditions used for assay of hemolysates. The capacity for erythrocytes to synthesize glutathione exceeds the rate of glutathione turnover by 150-fold, indicating that there is considerable reserve capacity for glutathione synthesis. A patient with erythrocyte glutathione synthetase deficiency has been described. The inability of patients’ extracts to synthesize glutathione is corrected by the addition of pure glutathione synthetase, indicating that there is no inhibitor in the patients’ erythrocytes.

[8] Braverman, E.R. (with Pfeiffer, C.C.)(1987). The healing nutrients within: Facts, findings and new research on amino acids. New Canaan: Keats Publishing

[9] Barbagallo, M. et al. Effects of glutathione on red blood cell intracellular magnesium: relation to glucose metabolism. Hypertension. 1999 Jul;34(1):76-82. Institute of Internal Medicine and Geriatrics, University of Palermo, Italy. mabar@unipa.it

[10] Magnesium deficiency (MgD) has been associated with production of reactive oxygen species, cytokines, and eicosanoids, as well as vascular compromise in vivo. Although MgD-induced inflammatory change occurs during “chronic” MgD in vivo, acute MgD may also affect the vasculature and consequently, predispose endothelial cells (EC) to perturbations associated with chronic MgD. As oxyradical production is a significant component of chronic MgD, we examined the effect of acute MgD on EC oxidant production in vitro. In addition we determined EC; pH, mitochondrial function, lysosomal integrity and general cellular antioxidant capacity. Decreasing Mg2+ (< or = 250microM) significantly increased EC oxidant production relative to control Mg2+ (1000microM). MgD-induced oxidant production, occurring within 30min, was attenuated by EC treatment with oxyradical scavengers and inhibitors of eicosanoid biosynthesis. Coincident with increased oxidant production were reductions in intracellular glutathione (GSH) and corresponding EC alkalinization. These data suggest that acute MgD is sufficient for induction of EC oxidant production, the extent of which may determine, at least in part, the extent of EC dysfunction/injury associated with chronic MgD. Effect of acute magnesium deficiency (MgD) on aortic endothelial cell (EC) oxidant production.Wiles ME, Wagner TL, Weglicki WB. The George Washington University Medical Center, Division of Experimental Medicine, Washington, D.C., USA. mwiles@nexstar.com Life Sci. 1997;60(3):221-36.

[11] Martin, Hélène. Richert, Lysiane. Berthelot, Alain Magnesium Deficiency Induces Apoptosis in Primary Cultures of Rat Hepatocytes.* Laboratoire de Physiologie, et Laboratoire de Biologie Cellulaire, UFR des Sciences Médicales et Pharmaceutiques, Besançon, France. 2003 The American Society for Nutritional Sciences J. Nutr. 133:2505-2511, August 2003