Title : Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity.

Pub. Date : 2001 Jun 8

PMID : 11397791






4 Functional Relationships(s)
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1 Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity. Threonine nitric oxide synthase 3 Homo sapiens
2 In the present study, we assessed whether the agonist-induced (Ca(2+)-dependent, high-output) activation of eNOS is associated with changes in the phosphorylation of Thr(495) in the calmodulin (CaM)-binding domain. Threonine nitric oxide synthase 3 Homo sapiens
3 eNOS Thr(495) was constitutively phosphorylated in porcine aortic endothelial cells and was rapidly dephosphorylated after bradykinin stimulation. Threonine nitric oxide synthase 3 Homo sapiens
4 These results suggest that the dual phosphorylation of Ser(1177) and Thr(495) determines the activity of eNOS in agonist-stimulated endothelial cells. Threonine nitric oxide synthase 3 Homo sapiens