Journal
FEBS LETTERS
Volume 573, Issue 1-3, Pages 175-180Publisher
WILEY
DOI: 10.1016/j.febslet.2004.07.078
Keywords
eNOS; AMPK; histamine; thrombin; endothelial cell
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Histamine and thrombin cause phosphorylation and activation of endothelial NO-synthase (eNOS) on Ser1177. We tested the role of various protein kinases in mediating this effect in human umbilical vein endothelial cells. Inhibition of the Ca2+/ calmodulin-dependent protein kinase 11 or phosphoinositide 3-kinase (PI3K) had no effect. H89, an inhibitor of both protein kinase A (PKA) and 5'-AMP-activated protein kinase (AMPK), strongly inhibited phosphorylation and activity of eNOS. Conversely, the PKA inhibitor Rp-adenosine 3'5'-cyclic monophosphate (cAMPS) had no effect and eNOS was not phosphorylated by treatments that affect cAMP levels. Thrombin and histamine caused phosphorylation of AMPK on Thr172 as well as on its' downstream target acetyl-CoA carboxylase. Activation of AMPK using AICAR or CCCP also resulted in eNOS phosphorylation. We conclude that histamine and thrombin cause eNOS phosphorylation in an AMPK mediated manner, independent of PI3K-Akt. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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