Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1260386 (GSH)
 38,102 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rats, sheep, and normal humans displayed a comparable sensitivity to copper acetate (3 mM)-induced changes in reduced glutathione (GSH) levels in vitro. However, the human erythrocytes were more sensitive than either animal to methemoglobin (METHB) formation with the rat being least sensitive. Ascorbic acid incubation markedly enhanced the occurrence of copper acetate-induced increases in METHB and decreases in GSH in the sheep and humans. However, ascorbic acid incubation reduced the occurrence of copper acetate-induced increases in METHB, while not effecting changes in GSH in rats.
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PMID:The effect of ascorbic acid on copper-induced oxidative changes in the erythrocytes of rats, sheep, and normal humans. 663 65

The effects of acrylonitrile (VCN) on hemoglobin and red cell metabolism were studied in vitro and in vivo using male Sprague-Dawley rats. Reduced glutathione (GSH) was rapidly depleted by VCN. The reaction between VCN and GSH to form S-cyanoethyl glutathione is both enzymic and nonenzymic. GSH depletion induced oxidation of considerable amount of hemoglobin to methemoglobin. Incubation of nitrite-treated erythrocytes with VCN (2-10 mM) resulted in a significant decrease in methemoglobin reduction. VCN initiated hemolysis in vitro at a concentration of 0.05 M, and at concentrations lower than 0.05 M rendered erythrocytes susceptible to osmotic fragility even at higher concentration of NaCl. Following oral administration of VCN (80 mg/kg), significant perturbations of levels of red-cell GSH, 2,3-diphosphoglycerate, adenosine triphosphate, pyruvate, lactate, and oxidized glutathione occurred within 1 h. These changes returned to normal levels between 6 and 24 h. A strong correlation between the depletion of GSH in vivo and covalent binding [2,3-14C]VCN to hemoglobin was observed. These in vivo and in vitro results suggest that chronic exposure to VCN may lead to methemoglobinemia and consequently may cause impaired delivery of oxygen to various tissues.
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PMID:The effects of acrylonitrile on hemoglobin and red cell metabolism. 666 18

A number of hydroxy analogues of the antimalarial drug primaquine [8-[(4-amino-1-methylbutyl)amino]-6-methoxyquinoline] were synthesized and characterized by 1H NMR and mass spectra. Several of the compounds were found to be active in forming methemoglobin in human erythrocytes, particularly in those from glucose-6-phosphate dehydrogenase (G6PD) deficient subjects. Decreased levels of glutathione (GSH) in G6PD-deficient erythrocytes were also found with compounds that were active methemoglobin formers.
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PMID:Synthesis of certain hydroxy analogues of the antimalarial drug primaquine and their in vitro methemoglobin-producing and glutathione-depleting activity in human erythrocytes. 669 88

Acetaminophen (APAP) was given orally to 6 mature cats (3 male and 3 female) in single progressive doses of 20 (low), 60 (medium), or 120 (high) mg APAP/kg body weight, each 3 weeks apart. Methemoglobin (MHB), reduced blood glutathione (GSH) and APAP blood concentrations, and blood NADH methemoglobin reductase and NADPH glutathione reductase activities were measured periodically for 8 days after dosing. A statistically significant increase in MHB formation (21.7% and 45.5%, respectively) occurred following the medium and high doses. NADH methemoglobin reductase activity at the high dose decreased significantly. Red blood cell GSH concentrations decreased significantly during the first 24 h after the high APAP dose and returned to normal by 192 h. NADPH glutathione reductase activity decreased significantly following the high dose, but not after the lower APAP doses.
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PMID:The effect of acetaminophen on methemoglobin and blood glutathione parameters in the cat. 674 Jul 6

Erythrocytes of both normal and glucose-6-phosphate dehydrogenase (G-6-PD)-deficient humans responded in a dose-dependent manner to the oxidant stress of methyl oleate hydroperoxide (MOHP) as measured by decreases in G-6-PD activity, increases in methemoglobin (METHB) levels, and decreases in reduced glutathione (GSH). The G-6-PD-deficient erythrocytes displayed a markedly enhanced sensitivity to MOHP-induced decreases in G-6-PD activity and METHB increases while being less sensitive than normal erythrocytes to changes in GSH levels.
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PMID:The effect of methyl oleate hydroperoxide, a possible toxic ozone intermediate, on human normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. 685 34

Stimulation of the hexose monophosphate shunt by primaquine results from the oxidation of NADPH by primaquine. This conclusion was based on the observations that primaquine lowered cellular NADPH but not GSH and that, in red cells in which the GSH was unavailable for reaction, primaquine still stimulated the rate of the hexose monophosphate shunt. In a non-cellular system, primaquine interacted with NADPH, but not GSH, to produce H2O2. Stimulation of the hexose monophosphate shunt by primaquine does not primarily involve H2O2 accumulation since stimulation of the pathway by primaquine was also observed in red cells containing methemoglobin, a red cell preparation in which no H2O2 accumulates. Methemoglobin prevented the formation and/or accumulation of H2O2 in intact red cells incubated with primaquine as well as in a non-cellular system containing primaquine plus Fe2+-EDTA as an H2O2 source. Methemoglobin probably acts by scavenging reactive intermediates since oxyhemoglobin was formed from methemoglobin in the non-cellular experiments. In the red cell, primaquine stimulated glucose-dependent conversion of methemoglobin to oxyhemoglobin.
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PMID:Primaquine-mediated oxidative metabolism in the human red cell. Lack of dependence on oxyhemoglobin, H2O2 formation, or glutathione turnover. 712 53

The influences of methylene blue (MB), thionine, ascorbic acid (ASA), sodium thiosulfate (STS), N-(2-mercaptopropionyl)-glycine (MPG) and reduced glutathione (GSH) on methemoglobin-(MHb)-emia and sulf-hemoglobin (SHb)-emia induced by 4-chloroaniline (4-Cl-A) i.p. were studied. Preventive or therapeutic effect on MHb-emia and preventive effect on SHb-emia in mice: MHb formation was inhibited by MB i.p. whether it was administered simultaneously with or after 4-Cl-A, but SHb formation was increased. Similar effects were seen with thionine. Both compounds proved to have MHb and SHb forming activities. STS or MPG, if administered i.p. simultaneously with 4-Cl-A, inhibited formation of MHb, but exerted no effect on delayed SHb formation. However, if administered i.p. or i.v. 120 minutes after 4-Cl-A when the peak of MHb formation had passed, there was a preventive effect on delayed SHb formation. GSH inhibited MHb formation and prevented SHb formation only when it was administered i.v. 120 minutes after 4-Cl-A. ASA did not inhibit MHb formation when it was administered either i.p. or i.v., but showed a preventive effect on SHb formation, if administered 120 minutes after 4-Cl-A. Combined i.v. administration of the corresponding doses to the clinical ones of MB and ASA 120 minutes after 4-Cl-A showed a therapeutic effect on MHb-emia and a preventive effect on SHb-emia. However, at higher dose levels, MB masked the preventive effect of ASA on SHb-emia. Therapeutic effect on SHb-emia in mice and rats: None of MB, STS, GSH and ASA proved to have any therapeutic effects for established SHb-emia. On the basis of these results, significance of clinical usage of drugs in the treatment of chemically induced MHb-emia and SHb-emia is discussed.
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PMID:[Studies of sulfhemoglobin formation by various drugs (4). Influences of various antidotes on chemically induced methemoglobinemia and sulfhemoglobinemia (author's transl)]. 720 79

Erythrocyte glutathione (GSH) can be rapidly depleted by incubating the cells with 1-chloro-2,4-dinitrobenzene (CDNB), which forms 2,4-dinitrophenyl-S-glutathione with GSH through the reaction catalyzed by glutathione S-transferase. GSH-CDNB conjugate thus formed stays undegraded within the erythrocytes. This indicates that in the erythrocytes, mercapturic acid pathway is inoperative. Depletion of GSH in the intact erythrocytes by CDNB results in rapid oxidation of large amounts of hemoglobin to methemoglobin. When glutathione S-transferase-free hemolysate of erythrocytes is incubated with CDNB, the depletion of GSH as well as methemoglobin formation are minimal. Glutathione peroxidase and glutathione reductase activities of the erythrocytes are not affected by CDNB. These studies provide a specific enzymatic method for rapid removal of erythrocyte GSH and also indicate that GSH is vital in maintaining a reduced environment within the erythrocytes.
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PMID:Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dinitrobenzene: the fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin. 727 4

The effects of several oxidant agents on metabolic and membrane parameters of glucose-6-phosphate dehydrogenase deficient erythrocytes (Mediterranean type) were examined in order to explore a possible common mechanism for their action on the deficient cells. The increase in methemoglobin and the decrease in GSH levels elicited by e oxidants were more pronounced in the deficient cells, provided glucose was present during the incubation of the cells with the drugs. However, glucose did not differentially modify other parameters: ATP level, filterability and osmotic fragility. There was no correlation between the effects produced by the oxidants on various parameters in either normal or deficient cells. It is concluded that in terms of the parameters studied more than one mechanism for the effects of the oxidants on cells should be assumed.
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PMID:Effect of oxidant agents on normal and G6PD-deficient erythrocytes. 739 64

The effects of age and dietary selenium on cellular susceptibility to oxidative stress were studied in rat erythrocytes. Young (26 or 40 days) and mature adult (11 or 15 months) male rats were fed a Torula yeast-based low selenium and low vitamin E diet supplemented with either 0, 1.0 to 2.0 ppm selenium (as sodium selenite) for 5 weeks. The rates of spontaneous hemolysis amd methemoglobin formation and levels of glutathione (GSH), glucose-6-phosphate (G6P) dehydrogenase, but not of GSH peroxidase, GSH reductase, superoxide dismutase and catalase were significantly higher in the erythrocytes of young rats than in those of the adults. Adult rats, however, had higher levels of plasma vitamin E and GSH peroxidase than those of the young group. Dietary selenium markedly increased activity of plasma GSH peroxidase and partially retarded the rates of hemolysis and methomoglobin formation, but it had no significant effect on the erythrocyte levels of GSH, GSH reductase, catalse, G6P dehydrogenase and superoxide dismutase or plasma vitamin E levels of young rats. Except of GSH peroxidase activity, dietary selenium had no significant effect on any other measurements made in the erythrocytes or plasma of adult rats. The results suggest that the ability of adult rats. The results suggest that the ability of adult rats to retain higher levels of vitamin E and selenium than the young rats may be partly responsible for the increased resistance of their erythrocytes against oxidative stress.
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PMID:Dietary selenium and age-related susceptibility of rat erythrocytes to oxidative damage. 744 74


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