OxyFile #325

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.