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

Research output: Contribution to journalArticlepeer-review


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 languageEnglish (US)
Pages (from-to)83-89
Number of pages7
JournalMolecular and Cellular Biochemistry
Issue number1-2
StatePublished - Sep 2011


  • Aging
  • Arginase
  • Endothelial dysfunction
  • Nitric oxide synthase
  • Nitrosation
  • Nitrosylation

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology


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