Regulation of endothelium-derived nitric oxide production by the protein kinase Akt View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1999-06

AUTHORS

David Fulton, Jean-Philippe Gratton, Timothy J. McCabe, Jason Fontana, Yasushi Fujio, Kenneth Walsh, Thomas F. Franke, Andreas Papapetropoulos, William C. Sessa

ABSTRACT

Endothelial nitric oxide synthase (eNOS) is the nitric oxide synthase isoform responsible for maintaining systemic blood pressure, vascular remodelling and angiogenesis1,2,3,4. eNOS is phosphorylated in response to various forms of cellular stimulation5,6,7 but the role of phosphorylation in the regulation of nitric oxide (NO) production and the kinase(s) responsible are not known. Here we show that the serine/threonine protein kinase Akt (protein kinase B) can directly phosphorylate eNOS on serine 1179 and activate the enzyme, leading to NO production, whereas mutant eNOS (S1179A) is resistant to phosphorylation and activation by Akt. Moreover, using adenovirus-mediated gene transfer, activated Akt increases basal NO release from endothelial cells, and activation-deficient Akt attenuates NO production stimulated by vascular endothelial growth factor. Thus, eNOS is a newly described Akt substrate linking signal transduction by Akt to the release of the gaseous second messenger NO. More... »

PAGES

597-601

Journal

TITLE

Nature

ISSUE

6736

VOLUME

399

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/21218

DOI

http://dx.doi.org/10.1038/21218

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031898878

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10376602


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