S-thiolation of human endothelial cell glyceraldehyde-3-phosphate
dehydrogenase after hydrogen peroxide treatment.
Author: Schuppe-Koistinen I; Moldéus P; Bergman T; Cotgreave IA
Source: Eur J Biochem 1994 May 1; 221(3):1033-7
Exposure of human umbilical vein endothelial cells to oxidants
such as hydrogen peroxide, tertbutyl 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.