In vitro inhibition of topoisomerase IIα by reduced glutathione.

  • Zahid M Delwar Department of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.;
  • Marina Fernanda Vita
  • Åke Siden
  • Mabel Cruz
  • Juan Sebastian Yakisich

Abstract

In most cells, the major intracellular redox buffer is glutathione (GSH) and its disulfide-oxidized (GSSG) form. The GSH/GSSG system maintains the intracellular redox balance and the essential thiol status of proteins by thiol disulfide exchange. Topoisomerases are thiol proteins and are a target of thiol-reactive substances. In this study, the inhibitory effect of physiological concentration of GSH and GSSG on topoisomerase IIα activity in vitro was investigated. GSH (0-10 mM) inhibited topoisomerase IIα in a concentration-dependent manner while GSSG (1-100 µM) had no significant effect. These findings suggest that the GSH/GSSG system could have a potential in vivo role in regulating topoisomerase IIα activity.
Published
2011-06-06
Section
Articles