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- Title
N-Acetyl cysteine,L-cysteine, and ß-mercaptoethanol augment seleniumglutathione peroxidase activity in glucose-6-phosphate dehydrogenasedeficient human erythrocytes.
- Authors
Alicigüzel, Y.; Aslan, M.
- Abstract
In glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes, failure to maintain normal levels of reduced glutathione (GSH) due to decreased NADPH regeneration in the hexose monophosphate pathway results in acute hemolytic anemia following exposure to oxidative insults, such as ingestion ofVicia favabeans or use of certain drugs. GSH is a source of protection against oxidative attack, used by the selenium-dependent glutathione peroxidase (Se-GSH-Px)/reductase (GR) system to detoxify hydrogen peroxide and organic peroxides, provided that sufficient GSH is made available. In this study, Se-GSH-Px activity was analyzed in G6PD-deficient patients in the presence of reducing agents such asN-Acetyl cysteine,L-cysteine, and ß-mercaptoethanol. Se-GSH-Px activity was decreased in G6PD-deficient red blood cells (RBCs).N-Acetyl cysteine,L-cysteine, and ß-mercaptoethanol increased Se-GSH-Px activity in G6PD-deficient human erythrocytes, indicating that other reducing agents can be utilized to complement Se-GSH-Px activity in G6PD deficiency. Based on the increased susceptibility of G6PD-deficient patients to oxidative stress, the reported increase in Se- GSH-Px activity can facilitate the detoxification of reactive oxygen species.
- Subjects
DEHYDROGENASES; ERYTHROCYTES; GLUTATHIONE; PENTOSE phosphate pathway; SELENIUM; HYDROGEN peroxide; OXIDATIVE stress
- Publication
Clinical & Experimental Medicine, 2004, Vol 4, Issue 1, p50
- ISSN
1591-8890
- Publication type
Article
- DOI
10.1007/s10238-004-0038-z