S‐Thiolation of human endothelial cell glyceraldehyde‐3‐phosphate dehydrogenase after hydrogen peroxide treatment

Abstract

Exposure of human umbilical vein endothelial cells to oxidants such as hydrogen peroxide, tert-butyl hydroperoxide and diamide has been shown to induce oxidant-specific S-thiolation of cellular proteins. In this study one of the main S-thiolated proteins in hydrogen-peroxide-treated cells was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. Additionally, we have shown that the post-translational modification of the cysteinyl thiols of glyceraldehyde-3-phosphate dehydrogenase accompanies an inhibition of the enzyme and that both events are simultaneously and rapidly reversed upon the removal of the oxidative stimulus.