1989
DOI: 10.1182/blood.v73.1.334.bloodjournal731334
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Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes

Abstract: Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH predispose affected erythrocytes to destruction from peroxides. Conversely, genetic deficiencies of catalase do not predispose affected erythrocytes to peroxide-induced destruction. These observations have served to strengthen the assumption that the NADPH/glutathione/glutathione peroxidase pathway is the principal means for disposal of H2O2 in human erythrocytes. Recently, however, mammalian catalase was found to have tightly bound NAD… Show more

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Cited by 55 publications
(25 citation statements)
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“…How a host cell with a [GSH]/[CSSG] ratio of 27 supports parasite growth and maintain its own integrity is an intriguing puzzle. A possible explanation can be found in recent reports, which suggest that catalase may be at least as important as GSH in cellular defense against H,O, (Gaetani et al, 1989;., 1991 a). Moreover, it seems that the status of NADPH rather than that of GSH is the major determinant of RBC sensitivity to H,O, challenge (Scott et al, 1991 b).…”
Section: Discussionmentioning
confidence: 94%
See 1 more Smart Citation
“…How a host cell with a [GSH]/[CSSG] ratio of 27 supports parasite growth and maintain its own integrity is an intriguing puzzle. A possible explanation can be found in recent reports, which suggest that catalase may be at least as important as GSH in cellular defense against H,O, (Gaetani et al, 1989;., 1991 a). Moreover, it seems that the status of NADPH rather than that of GSH is the major determinant of RBC sensitivity to H,O, challenge (Scott et al, 1991 b).…”
Section: Discussionmentioning
confidence: 94%
“…Detoxification of H,O, in the glutathione peroxidase route is an efficient process, even at low concentrations of H,O, (Costarides et al, 1991), and is considered to be the main event at low H,O, levels (Cohen and Hochstein, 1963). More recent observations, however, suggest that glutathione peroxidase and catalase are equally effective in erythrocytes at high H,O, flows (Gaetani et al, 1989;Scott et al, 1991b). Oxidants and radicals can react directly with GSH to give superoxide radicals, which are eliminated by superoxide dismutase activity and GSSG (Munday and Winterbourn, 1989).…”
mentioning
confidence: 99%
“…For example, accumulation of soluble sugar was shown to be related to the acquisition of heat tolerance in sugarcane Ghazanfar 2006, Wahid andClose 2007). More importantly, increased concentration of sugar could be a natural response to protect against oxidative damage by strengthening the antioxidant system, because soluble sugar can feed NADPH-producing metabolic pathways such as the oxidative pentose-phosphate (OPP) pathway, which contribute to ROS-scavenging (Gaetani et al 1989, May et al 1998. Also, glucose has been shown to enhance cellular defences against the cytotoxicity of hydrogen peroxide in certain mammalian cell types (Averill-Bates and Przybytkowski 1994).…”
Section: Discussionmentioning
confidence: 99%
“…Supplementation with vitamin E was found to induce the activity of glucose-6-phosphate dehydrogenase (G-6-PDH) and glutathione reductase in this study. Glutathione reductase is the enzyme that converts GSSG to GSH, with the help of NADPH, which is supplied by G-6-PDH (Gaetani et al 1989). This may also be a reason for the increased level of GSH observed in vitamin Esupplemented rats.…”
Section: Discussionmentioning
confidence: 99%