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 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 27 Issue: 4
  • Publication Date: 2003
  • Page Numbers: pp.433-443


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%.