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Tytuł pozycji:

Identification and functional implication of a Rho kinase-dependent moesin-EBP50 interaction in noradrenaline-stimulated artery.

Tytuł :
Identification and functional implication of a Rho kinase-dependent moesin-EBP50 interaction in noradrenaline-stimulated artery.
Index Terms :
Amides - pharmacology
Animals
Muscle, Smooth, Vascular - drug effects, metabolism
Norepinephrine - metabolism
Phosphoproteins - metabolism
Potassium Chloride - pharmacology
Protein Binding
Protein Kinase C - analysis, antagonists & inhibitors, metabolism
Pyridines - pharmacology
RNA, Small Interfering - metabolism
Rats
Rats, Wistar
Antihypertensive Agents - metabolism
rho-Associated Kinases - antagonists & inhibitors, metabolism
Aorta - drug effects, metabolism
Carrier Proteins - metabolism
Ionomycin - pharmacology
Male
Mesenteric Arteries - drug effects, metabolism
Microfilament Proteins - metabolism
Muscle Contraction - drug effects
info:eu-repo/semantics/article
Wydawca :
2010
Dodane szczegóły :
UCL - SSS/IONS - Institute of NeuroScience
UCL - SSS/IREC/CARD - Pôle de recherche cardiovasculaire
Baeyens, Nicolas
Horman, Sandrine
Vertommen, Didier
Rider, Mark
Morel, Nicole
Typ dokumentu :
Zasób elektroniczny
URL :
http://hdl.handle.net/2078.1/89752">http://hdl.handle.net/2078.1/89752
Dostępność :
Open access content. Open access content
info:eu-repo/semantics/restrictedAccess
Pozostałe numery :
UCDLC oai:dial.uclouvain.be:boreal:89752
boreal:89752
info:doi/10.1152/ajpcell.00175.2010
info:pmid/20926777
urn:ISSN:0363-6143
1130526597
Źródło wspomagające :
UNIVERSITE CATHOLIQUE DE LOUVAIN
From OAIster®, provided by the OCLC Cooperative.
Numer akcesji :
edsoai.on1130526597
Zasób elektroniczny
Ezrin, radixin, and moesin (ERM) proteins are known to be substrates of Rho kinase (ROCK), a key player in vascular smooth muscle regulation. Their function in arteries remains to be elucidated. The objective of the present study was to investigate ERM phosphorylation and function in rat aorta and mesenteric artery and the influence of ERM-binding phosphoprotein 50 (EBP50), a scaffold partner of ERM proteins in several cell types. In isolated arteries, ERM proteins are phosphorylated by PKC and ROCK with different kinetics after either agonist stimulation or KCl-induced depolarization. Immunoprecipitation of EBP50 in noradrenaline-stimulated arteries allowed identification of its interaction with moesin and several other proteins involved in cytoskeleton regulation. This interaction was inhibited by Y27632, a ROCK inhibitor. Moesin or EBP50 depletion after small interfering RNA transfection by reverse permeabilization in intact mesenteric arteries both potentiated the contractility in response to agonist stimulation without any effect on contractile response induced by high KCl. This effect was preserved in ionomycin-permeabilized arteries. These results indicate that, in agonist-stimulated arteries, the activation of ROCK leads to the binding of moesin to EBP50, which interacts with several components of the cytoskeleton, resulting in a decrease in the contractile response.

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