Calcineurin-mediated dephosphorylation of eNOS at serine 116 affects eNOS enzymatic activity indirectly by facilitating c-Src binding and tyrosine 83 phosphorylation
L Ruan, CM Torres, RJ Buffett, S Kennard, D Fulton… - Vascular …, 2013 - Elsevier
It has been shown previously that phosphorylation of the endothelial nitric oxide synthase
(eNOS) at serine 116 (S116) under basal conditions suppresses eNOS enzymatic activity in
endothelial cells. It has also been shown that vascular endothelial growth factor (VEGF)
treatment of endothelial cells produces a rapid S116 dephosphorylation, which is blocked by
the calcineurin inhibitor, cyclosporin A (CsA). In this study, we show that activation of eNOS
in response to a variety of other eNOS-activating agonists and the cytosolic calcium …
(eNOS) at serine 116 (S116) under basal conditions suppresses eNOS enzymatic activity in
endothelial cells. It has also been shown that vascular endothelial growth factor (VEGF)
treatment of endothelial cells produces a rapid S116 dephosphorylation, which is blocked by
the calcineurin inhibitor, cyclosporin A (CsA). In this study, we show that activation of eNOS
in response to a variety of other eNOS-activating agonists and the cytosolic calcium …