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Mol Cell Biochem. 2011 Sep;355(1-2):83-9. doi: 10.1007/s11010-011-0841-2. Epub 2011 May 1.

S-nitrosation of arginase 1 requires direct interaction with inducible nitric oxide synthase.

Author information

1
Johns Hopkins University School of Medicine, 720 Rutland Ave Ross 1150, Baltimore, MD 21205, USA.

Abstract

Arginase constrains endothelial nitric oxide synthase activity by competing for the common substrate, L -Arginine. We have recently shown that inducible nitric oxide synthase (NOS2) S-nitrosates and activates arginase 1 (Arg1) leading to age-associated vascular dysfunction. Here, we demonstrate that a direct interaction of Arg1 with NOS2 is necessary for its S-nitrosation. The specific domain of NOS2 that mediates this interaction is identified. Disruption of this interaction in human aortic endothelial cells prevents Arg1 S-nitrosation and activation. Thus, disruption of NOS2-Arg1 interaction may represent a therapeutic strategy to attenuate age related vascular endothelial dysfunction.

PMID:
21533769
PMCID:
PMC3744166
DOI:
10.1007/s11010-011-0841-2
[Indexed for MEDLINE]
Free PMC Article

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