AMP-activated protein kinase functionally phosphorylates endothelial nitric oxide synthase Ser633.

@article{Chen2009AMPactivatedPK,
  title={AMP-activated protein kinase functionally phosphorylates endothelial nitric oxide synthase Ser633.},
  author={Zhen Chen and I-Chen Peng and Wei Sun and Mei-I. Su and Pang-Hung Hsu and Yi Fu and Yi Zhu and Kathryn Defea and Songqin Pan and Ming-Daw Tsai and John Y-J Shyy},
  journal={Circulation research},
  year={2009},
  volume={104 4},
  pages={496-505}
}
Endothelial nitric oxide synthase (eNOS) plays a central role in maintaining cardiovascular homeostasis by controlling NO bioavailability. The activity of eNOS in vascular endothelial cells (ECs) largely depends on posttranslational modifications, including phosphorylation. Because the activity of AMP-activated protein kinase (AMPK) in ECs can be increased by multiple cardiovascular events, we studied the phosphorylation of eNOS Ser633 by AMPK and examined its functional relevance in the mouse… CONTINUE READING

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