Sodium orthovanadate induced tyrosine phosphorylation of platelet nitric oxide synthase negatively regulates enzyme activity.

The post-translational regulation of platelet nitric oxide synthase (NOS) activity is poorly understood. In the present study we examined how tyrosine phosphorylation of NOS, induced by the tyrosine phosphatase inhibitor sodium orthovanadate (VO4), influenced enzyme activity. Platelet NOS was basally tyrosine phosphorylated, but incubation with VO4 (100-1000 microM) led to a concentration-dependent increase in tyrosine phosphorylation of the enzyme with maximal effects observed at 500 microM.