S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment.
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.
Schuppe-Koistinen
I
I
Department of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden.
Moldéus
P
P
Bergman
T
T
Cotgreave
I A
IA
D015153:Blotting, Western; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D004730:Endothelium, Vascular / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D010084:Oxidation-Reduction; D011233:Precipitin Tests; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D014471:Umbilical Veins
D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D006861:Hydrogen Peroxide; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases