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

Author

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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
    Present addresses: Northeastern Ohio Universities College of Medicine Department of Integrative Medical Sciences, Rootstown, Ohio 44272, USA (Y.-R.C); Department of Anesthesiology, College of Medicine, Ohio State University, Columbus, Ohio 43210, USA (L.J.D.).)

  • Lawrence J. Druhan

    (College of Medicine, Ohio State University
    Present addresses: Northeastern Ohio Universities College of Medicine Department of Integrative Medical Sciences, Rootstown, Ohio 44272, USA (Y.-R.C); Department of Anesthesiology, College of Medicine, Ohio State University, Columbus, Ohio 43210, USA (L.J.D.).)

  • Jay L. Zweier

    (College of Medicine, Ohio State University)

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.

Suggested Citation

  • Chun-An Chen & Tse-Yao Wang & Saradhadevi Varadharaj & Levy A. Reyes & Craig Hemann & M. A. Hassan Talukder & Yeong-Renn Chen & Lawrence J. Druhan & Jay L. Zweier, 2010. "S-glutathionylation uncouples eNOS and regulates its cellular and vascular function," Nature, Nature, vol. 468(7327), pages 1115-1118, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7327:d:10.1038_nature09599
    DOI: 10.1038/nature09599
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    Cited by:

    1. Yuxian Guo & Yaru Liu & Shihao Zhao & Wangting Xu & Yiqing Li & Pengwei Zhao & Di Wang & Hongqiang Cheng & Yuehai Ke & Xue Zhang, 2021. "Oxidative stress-induced FABP5 S-glutathionylation protects against acute lung injury by suppressing inflammation in macrophages," Nature Communications, Nature, vol. 12(1), pages 1-18, December.

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