The effect of tert-butylhydroperoxide on the thiol redox status in human erythrocytes and the protective role of glucose and antioxidants
TURKISH JOURNAL OF CHEMISTRY, vol.27, no.4, pp.433-443, 2003 (SCI-Expanded, Scopus, TRDizin)
- Publication Type: Article / Article
- Volume: 27 Issue: 4
- Publication Date: 2003
- Journal Name: TURKISH JOURNAL OF CHEMISTRY
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, TR DİZİN (ULAKBİM)
- Page Numbers: pp.433-443
- Keywords: human erythrocytes, GSH, GSSG, thiol redox status, tert-butylhydroperoxide, ascorbate, alpha-tocopherol, PROTEIN MIXED DISULFIDES, OXIDATIVE STRESS, OXIDIZED GLUTATHIONE, BLOOD, TRANSPORT, CYSTEINE, SYSTEM
- Hacettepe University Affiliated: Yes
Abstract
For survival, living cells maintain their thiol redox status within acceptable limits by three different mechanisms: i. glutathione disulfide export, ii. reduction of glutathione disulfide by pentose phosphate pathway and, iii. reduction of glutathione disulfide by Protein-SH. To assess the relative contribution of each one of the systems, intracellular [glutathione], [glutathione disulfide] and their export, in fresh and aged erythrocytes subjected to oxidative stress, in +/-glucose and +/-antioxidants, were measured. Glutathione was rapidly oxidized by tert-butylhydroperoxide in +/-glucose in both groups. The regeneration of glutathione, in both groups, in +/-glucose was about 100 and 50%, respectively. In parallel, intracellular glutathione disulfide concentrations were increased by about 200-350%.