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

Academic Article


  • 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. © 2011 Springer Science+Business Media, LLC.
  • Authors

    Digital Object Identifier (doi)

    Author List

  • Dunn J; Gutbrod S; Webb A; Pak A; Jandu SK; Bhunia A; Berkowitz DE; Santhanam L
  • Start Page

  • 83
  • End Page

  • 89
  • Volume

  • 355
  • Issue

  • 1-2