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dc.contributor.authorThors, Brynhildur*
dc.contributor.authorHalldorsson, Haraldur*
dc.contributor.authorThorgeirsson, Gudmundur*
dc.date.accessioned2007-09-12T15:13:38Z
dc.date.available2007-09-12T15:13:38Z
dc.date.issued2004-08-27
dc.date.submitted2007-09-12
dc.identifier.citationFEBS Lett. 2004, 573(1-3):175-80en
dc.identifier.issn0014-5793
dc.identifier.pmid15327994
dc.identifier.doi10.1016/j.febslet.2004.07.078
dc.identifier.urihttp://hdl.handle.net/2336/13600
dc.descriptionTo access publisher full text version of this article. Please click on the hyperlink in Additional Links fielden
dc.description.abstractHistamine 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 II 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 P13K-Akt.
dc.language.isoenen
dc.publisherElsevier Science B.V.en
dc.relation.urlhttp://www.sciencedirect.com/science/article/B6T36-4D2C7CS-D/2/0602dcd9f2daacfc90a7c0dbf93de7b2en
dc.subject.mesh1-Phosphatidylinositol 3-Kinaseen
dc.subject.meshCa(2+)-Calmodulin Dependent Protein Kinaseen
dc.subject.meshThrombinen
dc.subject.meshSignal Transductionen
dc.subject.meshProto-Oncogene Proteinen
dc.subject.meshPhosphoserineen
dc.subject.meshNitric Oxide Synthase Type IIIen
dc.subject.meshMultienzyme Complexesen
dc.titleThrombin and histamine stimulate endothelial nitric-oxide synthase phosphorylation at Ser1177 via an AMPK mediated pathway independent of PI3K-Akten
dc.typeArticleen
dc.identifier.journalFEBS lettersen
dc.format.digYES
html.description.abstractHistamine 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 II 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 P13K-Akt.


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