H2S Signals Through Protein S-Sulfhydration

被引：604

作者：

Mustafa, Asif K. ^{[1
]}

Gadalla, Moataz M. ^{[2
]}

Sen, Nilkantha ^{[1
]}

Kim, Seyun ^{[1
]}

Mu, Weitong ^{[1
]}

Gazi, Sadia K. ^{[1
]}

Barrow, Roxanne K. ^{[1
]}

Yang, Guangdong ^{[3
]}

Wang, Rui ^{[3
]}

Snyder, Solomon H. ^{[1
,2
,4
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Solomon H Snyder Dept Neurosci, Baltimore, MD 21205 USA

[2] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA

[3] Lakehead Univ, Dept Biol, Thunder Bay, ON P7B 5E1, Canada

[4] Johns Hopkins Univ, Sch Med, Dept Psychiat & Behav Sci, Baltimore, MD 21205 USA

来源：

SCIENCE SIGNALING | 2009年 / 2卷 / 96期

关键词：

HYDROGEN-SULFIDE; NITRIC-OXIDE; NITROSYLATION; VASORELAXANT; CYSTEINE; LIVER; MICE;

D O I：

10.1126/scisignal.2000464

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：

Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins.

引用

页数：8

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