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

Jessilyn Dunn, Sarah Gutbrod, Alanah Webb, Alina Pak, Simran K Jandu, Anil Bhunia, Dan E Berkowitz, Lakshmi Santhanam

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

Molecular and cellular biochemistry 2011 Sep

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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.

Citation

Jessilyn Dunn, Sarah Gutbrod, Alanah Webb, Alina Pak, Simran K Jandu, Anil Bhunia, Dan E Berkowitz, Lakshmi Santhanam. S-nitrosation of arginase 1 requires direct interaction with inducible nitric oxide synthase. Molecular and cellular biochemistry. 2011 Sep;355(1-2):83-9