[HTML][HTML] Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells
Recent studies have indicated that endothelial nitric-oxide synthase (eNOS) is regulated by
reversible phosphorylation in intact endothelial cells. AMP-activated protein kinase (AMPK)
has previously been demonstrated to phosphorylate and activate eNOS at Ser-1177 in vitro,
yet the function of AMPK in endothelium is poorly characterized. We therefore determined
whether activation of AMPK with 5′-aminoimidazole-4-carboxamide ribonucleoside
(AICAR) stimulated NO production in human aortic endothelial cells. AICAR caused the time …
reversible phosphorylation in intact endothelial cells. AMP-activated protein kinase (AMPK)
has previously been demonstrated to phosphorylate and activate eNOS at Ser-1177 in vitro,
yet the function of AMPK in endothelium is poorly characterized. We therefore determined
whether activation of AMPK with 5′-aminoimidazole-4-carboxamide ribonucleoside
(AICAR) stimulated NO production in human aortic endothelial cells. AICAR caused the time …