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)

Although humans may accept fairly large amounts of orally ingested copper (0.25 to 1.0 gm) without visible harmful effects, patients with Wilson's disease, and persons with G6PD deficiency may represent persons at unusual risk to hemolytic anemia from ingestion of Cu(II). This study reports that in vitro exposure of G6PD deficient red blood cells to copper produced marked elevations of methemoglobin and decreases in GSH when compared with normal red cells. Chlorite, a by-product of chlorine dioxide disinfection of water, produced decreases in GSH and G6PD activity, while increasing methemoglobin levels markedly over red cells with normal G6PD activity. The combined action of chlorite and copper was additive in producing increased levels of hemoglobin and decreases in levels of GSH and G6PD deficient cells. The combined ingestion of copper and chlorite may represent an increased risk to persons with G6PD deficiency.
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PMID:G6PD-deficiency: a potential high-risk group to copper and chlorite ingestion. 746 5

Chlorite, a by-product of chlorine dioxide disinfection of water, is a strong oxidant compound that produces markedly exaggerated effects in vitro on red cells of G6PD deficient humans when compared to normal human cells. Levels of methemoglobin are significantly greater and GSH levels significantly lower in the G6PD deficient cells than in normal cells after chlorite exposure. Persons with G6PD deficiency may be 3 to 4 times more likely to develop hemolytic anemia from chlorite exposure as persons with normal activity levels when GSH levels are used as a measure of susceptibility. The proposed use of chlorine dioxide as an alternate disinfectant for drinking water supplies should consider this potential high risk group.
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PMID:Groups at potentially high risk from chlorine dioxide treated water. 746 14

Copper(II) complexes were encapsulated in human red blood cells in order to test their possible use as antioxidant drugs by virtue of their labile character. ESR spectroscopy was used to verify whether encapsulation in red blood cells leads to the modification of such complexes. With copper(II) complexes bound to dipeptides or tripeptides, an interaction with hemoglobin was found to be present, the hemoglobin having a strong coordinative site formed by four nitrogen donor atoms. Instead, with copper(II) complexes with TAD or PheANN3, which have the greatest stability. ESR spectra always showed the original species. Only the copper(II) complex with GHL gave rise to a complicated behavior, which contained signals from iron(III) species probably coming from oxidative processes. Encapsulation of all copper(II) complexes in erythrocytes caused a slight oxidative stress, compared to the unloaded and to the native cells. However, no significant differences were observed in the major metabolic properties (GSH, glycolytic rate, hexose monophosphate shunt, Ca(2+)-ATPase) of erythrocytes loaded with different copper(II) complexes, with the exception of methemoglobin levels, which were markedly increased in the case of [Cu(GHL)H-1] compared to [Cu(TAD)]. This latter finding suggests that methemoglobin formation can be affected by the type of complex used for encapsulation, depending on the direct interaction of the copper(II) complex with hemoglobin.
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PMID:Copper(II) complexes encapsulated in human red blood cells. 759 66

The reaction of oxidation of oxyhemoglobin (oxyHb) to methemoglobin (metHb) by sodium nitrite in the presence of reduced glutathione is characterized by the changed ratios between the slow and rapid reaction phases. The duration of the lag phase increases as the glutathione concentration in the solution rises. The autocatalytic phase was inhibited and glutathione was oxidized to the disulfide form. The decreased rate of the reaction of oxyHb oxidation by sodium nitrite may be due to the effects of both the intermediate and the end products of oxidized glutathione. It is suggested that the thyil radical interacts to form the intermediate compound, anione glutathione disulfide (GSSG), which reduces metHb, thus increasing the lag phase duration. The autocatalytic phase inhibition can also be induced by electron transfer from the superoxide anion to the GSSG form. In addition to the GSSG, S-nitrosoglutathione was also formed during oxyHb oxidation by nitrite. In the absence of oxyHb in the neutral neutral medium, reduced glutathione (GSH) was not essentially oxidized by sodium nitrite. At pH lower than 6.0 S-nitrosoglutathione was observed to be formed due to the interaction of sodium nitrite with GSH. The addition of salts or increased pH of the solution induced hydrolysis of the product.
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PMID:Glutathione oxidation under the action of sodium nitrite on hemoglobin. 762 May 20

The methemoglobin formation and methemoglobin reduction in canine erythrocytes characterized by inherited high potassium (K+) and normal reduced glutathione concentrations (HK-low GSH cells) were compared with those in canine erythrocytes with inherited high K+ and high GSH concentrations (HK-high GSH cells) and normal canine erythrocytes with low K+ and low (= normal) GSH concentrations (LK-low GSH cells). The rate of methemoglobin formation induced by sodium nitrite (NaNO2) was in the order; LK-low GSH > HK-low GSH > HK-high GSH cells, and the difference among groups was significant at 7 and 15 min. Methemoglobin reduction in a medium containing glucose occurred rapidly in both HK-high GSH and HK-low GSH cells, and the rate of reduction was 1.7-fold higher than in LK-low GSH cells. Accumulation of pyruvate equivalent to the amount of methemoglobin reduced indicated that methemoglobin was predominantly reduced by NADH-methemoglobin reductase coupled to glycolysis. HK-low GSH cells showed an increased glycolytic rate and high pyruvate kinase activity similar to the levels in HK-high GSH cells. It is therefore evident that HK-low GSH cells offer greater protection against oxidation of hemoglobin to methemoglobin than LK-low GSH cells because of the increased glycolytic rate in HK-low GSH cells attributable to high pyruvate kinase activity in these cells.
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PMID:Methemoglobin formation and reduction in canine erythrocytes characterized by inherited high Na+, K(+)-ATPase activity with normal and high glutathione concentrations. 786 86

The in vivo effects of human placental extract (1-4 ml/kg) on hepatic lipid peroxidation, blood and liver glutathione (GSH) levels and several enzymes associated with the antioxidant defence mechanism; i.e., catalase, glutathione peroxidase, glutathione reductase and glutathione S-transferase, together with some blood biochemical responses were investigated in rats. At an optimal dose level (4 ml/kg), a single acute intraperitoneal administration of the extract caused a significant enhancement (49.9%; p < 0.001) of lipid peroxidation with a decline in GSH level both in blood (45.1%; p < 0.001) and liver (61.0%; p < 0.001) in comparison to control animals. Activities of catalase, glutathione peroxidase and glutathione reductase were inhibited in a dose-responsive way by the treatment with the extract which also increased the activity of glutathione S-transferase in a dose-dependent manner. The extract was found to be hepatotoxic in terms of elevation of serum glutamate oxaloacetate transaminase, serum glutamate pyruvate transaminase, serum lactate dehydrogenase and blood methemoglobin concentration. Results of this study suggest the adverse consequences of the administration of the extract due to its substantial ability to alter normal cellular processes.
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PMID:Elevated lipid peroxidation, decreased glutathione levels and changes in glutathione-related enzymes in rats treated with human placental extract. 821 15

Incubation of human red blood cells (RBCs) with t-butyl hydroperoxide (tBHP) resulted in inhibition of the Ca-pump ATPase. This was demonstrated using an assay of the Ca-pump ATPase activity in intact RBCs. In this assay, activity of the Ca-pump ATPase is expressed as the rate constant of the initial loss of ATP in RBCs exposed to Ca and A23187. Pseudo-first-order rate constants (Ca-pump ATPase rate constants) were lower in the presence of tBHP versus controls. Incubation of RBCs with tBHP resulted in both a time- and concentration-dependent inhibition of the Ca-pump ATPase (IC50 approximately 1 mM). Incubation of RBCs with tBHP also resulted in decreased oxyhemoglobin, increased methemoglobin and increased thiobarbituric acid reactive substances (TBARS). GSH levels were significantly lower in the presence of tBHP. GSH fell from a control value of 2.2 mmol/l RBC to 0.46 mmol/l RBC after incubation with 0.25 mM tBHP for 15 min. Both butylated hydroxytoluene and stobadine prevented the formation of TBARS and were partially effective in protecting the Ca-pump ATPase from tBHP-induced inhibition. Dithiothreitol was completely effective in preventing the tBHP-induced formation of TBARS as well as inhibition of the Ca-pump ATPase. However, when added after exposure to tBHP, dithiothreitol was unable to restore Ca-pump ATPase activity completely. An activity of dithiothreitol independent of enzymic thiol group reduction was apparent. In the presence of mercaptosuccinate, a potent inhibitor of glutathione peroxidase, the ability of dithiothreitol to protect the Ca-pump ATPase from tBHP-induced inhibition was abolished. Therefore, protection by dithiothreitol may be afforded by its ability to replenish GSH from oxidized glutathione, thus allowing glutathione peroxidase to metabolize tBHP. These results may be interpreted to suggest that inhibition of the Ca-pump ATPase in intact RBCs occurs as a result of tBHP-induced oxidant stress and subsequent lipid peroxidation which can be prevented by certain antioxidants including butylated hydroxytoluene, stobadine, and thiol-containing compounds such as dithiothreitol. These findings provide further insight into the mode of action of hydroperoxides and certain reactive oxygen species that have been implicated in oxidative stress associated with various pathological conditions. The importance of the GSH/glutathione peroxidase system in metabolizing organic hydroperoxides is also demonstrated.
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PMID:Inhibition of the Ca pump of intact red blood cells by t-butyl hydroperoxide: importance of glutathione peroxidase. 824 Dec 52

Red blood cells in iron deficiency anemia (IDA) have a decreased activity of essential antioxidant enzymes. The present study examined the effect of in vitro exposure to oxidative agents in IDA cells and their recovery capacity. Red cells of 26 IDA patients and 10 healthy subjects were examined. Cells of IDA patients had higher levels of reduced glutathione (GSH), and normal methemoglobin and malonyldialdehyde (MDA) levels. Exposure to butyl hydroperoxide revealed a dose-dependent sensitivity in IDA cells, with extensive GSH depletion and increased MDA levels. These changes were partially reversible by incubation with dithiothreitol. Exposure to phenazine methosulfate, to produce intracellular superoxide ions, resulted in moderate GSH depletion and methemoglobin production. IDA cells were more sensitive than control cells to high concentrations of this substance. This effect was further augmented by preincubation with a superoxide dismutase inhibitor. Our data demonstrate that IDA cells are more susceptible to oxidation but have good capacity for recovery.
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PMID:Iron deficiency anemia: recovery from in vitro oxidative stress. 809 40

Avian erythrocytes differ from mammalian erythrocytes in being nucleated and oval. In the circulation, chicken cells survive for only 35 days, compared to 120 days for human cells. In humans, red cell oxidation processes, involving methemoglobin formation, have been correlated with cellular aging. This study compared oxidative resistance of two avian red cells (chicken and ostrich) to that of discoid enucleated human cells. Reduced glutathione levels (GSH) and methemoglobin were higher in chicken and ostrich cells than in human cells. SOD levels were higher in human cells. Diamide exposure diminished intracellular GSH levels in all species, with the greatest effect on human cells. Regeneration potential was high for all cells. Ostrich cells were more sensitive to hydrogen peroxide when hemoglobin oxidation was involved; BHP exposure affected GSH depletion and methemoglobin production in ostrich cells more than in the others. Lipid peroxidation was found to be highest in the human cells. Chicken cells were only slightly more resistant than human cells. Our data suggest that the extensive, complex oxidation by BHP cannot represent in vivo aging processes. In addition, the milder, selective oxidation by diamide affects human cells (endowed with long life span) more than avian cells. It is concluded that in vitro oxidation by diamide and BHP cannot be correlated with red cell survival.
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PMID:Effect of oxidative stress on avian erythrocytes. 867 16

Ionizing radiation is currently used for prevention of transfusion associated graft versus host disease (TAGVHD). As radiation damage is associated with the production of activated oxygen species, the aim of this study was to observe the immediate effect of ionizing radiation on red cell membrane and intracellular oxidative defense systems. Neonatal and iron deficiency (IDA) cells, known for their increased sensitivity to oxidative stress, were chosen and compared with normal cells. Irradiation was performed in doses of 1500 cGy, 3000 cGy and 5000 cGy. GSH and methemoglobin levels and the activity of different antioxidant enzymes, measured under optimal in vitro conditions, were preserved in all cells after irradiation. Only radiation at the highest does of 5000 cGy, caused significant potassium leakage in neonatal cells and insignificant increase in IDA cells. Thus, cells with increased sensitivity to oxidative stress are more susceptible to damage by ionizing radiation than normal cells.
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PMID:Effect of radiation on red cell membrane and intracellular oxidative defense systems. 872 21


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