Title : Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1.

Pub. Date : 1996 Nov 1

PMID : 8910295






7 Functional Relationships(s)
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1 Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1. Tyrosine nitric oxide synthase 3 Bos taurus
2 Here, we demonstrate that eNOS is tyrosine-phosphorylated in bovine aortic endothelial cells (BAEC) using 32P metabolic labeling followed by phosphoamino acid analysis and by phosphotyrosine specific Western blotting. Tyrosine nitric oxide synthase 3 Bos taurus
3 Treatment of BAEC with hydrogen peroxide and the protein tyrosine phosphatase inhibitor, sodium orthovanadate, increases eNOS tyrosine phosphorylation. Tyrosine nitric oxide synthase 3 Bos taurus
4 Because eNOS is localized in plasmalemma caveolae, we examined if tyrosine phosphorylated eNOS interacts with caveolin-1, the coat protein of caveolae. Tyrosine nitric oxide synthase 3 Bos taurus
5 Conversely, immunoprecipitation of caveolin-1 resulted in the co-precipitation of tyrosine-phosphorylated eNOS. Tyrosine nitric oxide synthase 3 Bos taurus
6 Thus, tyrosine phosphorylation is a novel regulatory mechanism for eNOS and caveolin-1 is the first eNOS-associated protein. Tyrosine nitric oxide synthase 3 Bos taurus
7 Collectively, these observations provide a novel regulatory mechanism for eNOS and suggest that tyrosine phosphorylation may influence its activity, subcellular trafficking, and interaction with other caveolin-interacting proteins in caveolae. Tyrosine nitric oxide synthase 3 Bos taurus