S-glutathionylation uncouples eNOS and regulates its cellular and vascular function

Chun-An Chen, Tse-Yao Wang, Saradhadevi Varadharaj, Levy A. Reyes, Craig Hemann, M. A. Hassan Talukder, Yeong-Renn Chen, Lawrence J. Druhan and Jay L. Zweier ()
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Chun-An Chen: College of Medicine, Ohio State University
Tse-Yao Wang: College of Medicine, Ohio State University
Saradhadevi Varadharaj: College of Medicine, Ohio State University
Levy A. Reyes: College of Medicine, Ohio State University
Craig Hemann: College of Medicine, Ohio State University
M. A. Hassan Talukder: College of Medicine, Ohio State University
Yeong-Renn Chen: College of Medicine, Ohio State University
Lawrence J. Druhan: College of Medicine, Ohio State University
Jay L. Zweier: College of Medicine, Ohio State University

Nature, 2010, vol. 468, issue 7327, 1115-1118

Abstract: A molecular switch for eNOS The enzyme eNOS (endothelial nitric oxide synthase) is vital for regulating vascular function as it can produce both the vasodilator nitric oxide and the vasoconstrictor superoxide. Jay Zweier and colleagues show that a modification associated with oxidant stress, S-glutathionylation, switches the enzyme from forming nitric oxide to forming superoxide. In hypertensive vessels, S-glutathionylation of eNOS is increased, and this is associated with impaired endothelium-dependent vasodilation. Oxidant stress occurs in many diseases including heart attack, stroke, diabetes and cancer. This work suggests that agents that reset this redox switch, thereby restoring normal nitric oxide synthase function, may have therapeutic potential.

Date: 2010
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DOI: 10.1038/nature09599

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