The N-terminal portion of autoinhibitory element modulates human endothelial nitric-oxide synthase activity through coordinated controls of phosphorylation at Thr495 and Ser1177

The N-terminal portion of autoinhibitory element modulates human endothelial nitric-oxide synthase activity through coordinated controls of phosphorylation at Thr495 and Ser1177

NO production catalysed by eNOS (endothelial nitric-oxide synthase) plays an important role in the cardiovascular system. A variety of agonists activate eNOS through the Ser1177 phosphorylation concomitant with Thr495 dephosphorylation, resulting in increased ·NO production with a basal level of ca...

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Bibliographic Details
Main Authors: Pei‑Rung Wu, Bo‑Rui Chen, Chi‑Chun Hsieh, Wei‑Chung Lin, Kenneth K. Wu, Yeukuang Hwu, Pei‑Feng Chen
Format: Article
Language:English
Published: Portland Press, Biochemical Society 2014-08-01
Series:Bioscience Reports
Subjects:
autoinhibitory element
calcium/calmodulin
CaM-binding domain
endothelial nitric-oxide synthase
mobility shift gel
phosphorylation/dephosphorylation
Online Access:http://www.bioscirep.org/bsr/034/e129/bsr034e129.htm

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