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.
Original language | English (US) |
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Pages (from-to) | 83-89 |
Number of pages | 7 |
Journal | Molecular and Cellular Biochemistry |
Volume | 355 |
Issue number | 1-2 |
DOIs | |
State | Published - Sep 2011 |
Keywords
- Aging
- Arginase
- Endothelial dysfunction
- Nitric oxide synthase
- Nitrosation
- Nitrosylation
ASJC Scopus subject areas
- Molecular Biology
- Clinical Biochemistry
- Cell Biology