S-THIOLATION OF HUMAN ENDOTHELIAL-CELL GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AFTER HYDROGEN-PEROXIDE TREATMENT

被引:150
作者
SCHUPPEKOISTINEN, I
MOLDEUS, P
BERGMAN, T
COTGREAVE, IA
机构
[1] KAROLINSKA INST,DEPT ENVIRONM MED,DIV TOXICOL,S-17177 STOCKHOLM,SWEDEN
[2] KAROLINSKA INST,DEPT MED BIOCHEM & BIOPHYS,STOCKHOLM,SWEDEN
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 221卷 / 03期
关键词
D O I
10.1111/j.1432-1033.1994.tb18821.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1033 / 1037
页数:5
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