Involvement of Ca2+/calmodulin-dependent protein kinase II in endothelial NO production and endothelium-dependent relaxation.

Détails

ID Serval
serval:BIB_29805
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Involvement of Ca2+/calmodulin-dependent protein kinase II in endothelial NO production and endothelium-dependent relaxation.
Périodique
American Journal of Physiology. Heart and Circulatory Physiology
Auteur(s)
Schneider J.C., El Kebir D., Chéreau C., Lanone S., Huang X.L., De Buys Roessingh A.S., Mercier J.C., Dall'Ava-Santucci J., Dinh-Xuan A.T.
ISSN
0363-6135 (Print)
ISSN-L
0363-6135
Statut éditorial
Publié
Date de publication
2003
Volume
284
Numéro
6
Pages
H2311-H2319
Langue
anglais
Notes
Publication types: In Vitro ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Nitric oxide (NO) is synthesized from l-arginine by the Ca(2+)/calmodulin-sensitive endothelial NO synthase (NOS) isoform (eNOS). The present study assesses the role of Ca(2+)/calmodulin-dependent protein kinase II (CaMK II) in endothelium-dependent relaxation and NO synthesis. The effects of three CaMK II inhibitors were investigated in endothelium-intact aortic rings of normotensive rats. NO synthesis was assessed by a NO sensor and chemiluminescence in culture medium of cultured porcine aortic endothelial cells stimulated with the Ca(2+) ionophore A23187 and thapsigargin. Rat aortic endothelial NOS activity was measured by the conversion of l-[(3)H]arginine to l-[(3)H]citrulline. Three CaMK II inhibitors, polypeptide 281-302, KN-93, and lavendustin C, attenuated the endothelium-dependent relaxation of endothelium-intact rat aortic rings in response to acetylcholine, A23187, and thapsigargin. None of the CaMK II inhibitors affected the relaxation induced by NO donors. In a porcine aortic endothelial cell line, KN-93 decreased NO synthesis and caused a rightward shift of the concentration-response curves to A23187 and thapsigargin. In rat aortic endothelial cells, KN-93 significantly decreased bradykinin-induced eNOS activity. These results suggest that CaMK II was involved in NO synthesis as a result of Ca(2+)-dependent activation of eNOS.
Mots-clé
Acetylcholine/pharmacology, Animals, Aorta, Thoracic/drug effects, Benzylamines/pharmacology, Calcimycin/pharmacology, Calcium/pharmacology, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors, Calcium-Calmodulin-Dependent Protein Kinases/metabolism, Cell Line, Cells, Cultured, Electric Stimulation, Endothelium, Vascular/enzymology, Endothelium, Vascular/metabolism, Enzyme Inhibitors/pharmacology, Immunoblotting, Muscle Contraction/physiology, Muscle Relaxation/physiology, Muscle, Smooth, Vascular/enzymology, Muscle, Smooth, Vascular/physiology, Nitric Oxide/biosynthesis, Nitric Oxide Donors/pharmacology, Nitric Oxide Synthase/metabolism, Nitric Oxide Synthase Type III, Phosphorylation, Rats, S-Nitroso-N-Acetylpenicillamine/pharmacology, Sulfonamides/pharmacology, Swine, Thapsigargin/pharmacology, Vasodilator Agents/pharmacology
Pubmed
Web of science
Création de la notice
19/11/2007 13:27
Dernière modification de la notice
20/08/2019 14:09
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