Identification of flow-dependent endothelial nitric-oxide synthase phosphorylation sites by mass spectrometry and regulation of phosphorylation and nitric oxide production by the phosphatidylinositol 3-kinase inhibitor LY294002.

@article{Gallis1999IdentificationOF,
  title={Identification of flow-dependent endothelial nitric-oxide synthase phosphorylation sites by mass spectrometry and regulation of phosphorylation and nitric oxide production by the phosphatidylinositol 3-kinase inhibitor LY294002.},
  author={Byron M. Gallis and Garry L. Corthals and David R. Goodlett and Hiroto Ueba and Francis Y Kim and Steven R. Presnell and Daniel Figeys and David G Harrison and Bradford C. Berk and Ruedi Aebersold and Marshall A. Corson},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 42},
  pages={30101-8}
}
Endothelial cells release nitric oxide (NO) acutely in response to increased laminar fluid shear stress, and the increase is correlated with enhanced phosphorylation of endothelial nitric-oxide synthase (eNOS). Phosphoamino acid analysis of eNOS from bovine aortic endothelial cells labeled with [(32)P]orthophosphate demonstrated that only phosphoserine was present in eNOS under both static and flow conditions. Fluid shear stress induced phosphate incorporation into two specific eNOS tryptic… CONTINUE READING
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