دورية أكاديمية

Thrombin and histamine stimulate endothelial nitric‐oxide synthase phosphorylation at Ser1177 via an AMPK mediated pathway independent of PI3K‐Akt

التفاصيل البيبلوغرافية
العنوان: Thrombin and histamine stimulate endothelial nitric‐oxide synthase phosphorylation at Ser1177 via an AMPK mediated pathway independent of PI3K‐Akt
المؤلفون: Thors, Brynhildur, Halldórsson, Haraldur, Thorgeirsson, Gudmundur
المصدر: FEBS Letters ; volume 573, issue 1-3, page 175-180 ; ISSN 0014-5793 1873-3468
بيانات النشر: Wiley
سنة النشر: 2004
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: 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 Ca 2+ /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.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1016/j.febslet.2004.07.078
الإتاحة: https://doi.org/10.1016/j.febslet.2004.07.078Test
حقوق: http://onlinelibrary.wiley.com/termsAndConditions#vorTest
رقم الانضمام: edsbas.C36535E2
قاعدة البيانات: BASE