The effect of tert-butylhydroperoxide on the thiol redox status in human erythrocytes and the protective role of glucose and antioxidants

Aksoy Y., Ogus I., KARTAL ÖZER N.

TURKISH JOURNAL OF CHEMISTRY, vol.27, no.4, pp.433-443, 2003 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 27 Issue: 4
  • Publication Date: 2003
  • 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


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%.