Document Detail

Identification and functional implication of a Rho kinase-dependent moesin-EBP50 interaction in noradrenaline-stimulated artery.
MedLine Citation:
PMID:  20926777     Owner:  NLM     Status:  MEDLINE    
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.
Nicolas Baeyens; Sandrine Horman; Didier Vertommen; Mark Rider; Nicole Morel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-10-06
Journal Detail:
Title:  American journal of physiology. Cell physiology     Volume:  299     ISSN:  1522-1563     ISO Abbreviation:  Am. J. Physiol., Cell Physiol.     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-12-01     Completed Date:  2011-01-04     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100901225     Medline TA:  Am J Physiol Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  C1530-40     Citation Subset:  IM    
Laboratory of Cell Physiology, Institute of Neuroscience, Université Catholique de Louvain, Brussels, Belgium.
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MeSH Terms
Amides / pharmacology
Antihypertensive Agents / metabolism
Aorta / drug effects,  metabolism
Carrier Proteins / metabolism*
Ionomycin / pharmacology
Mesenteric Arteries / drug effects,  metabolism*
Microfilament Proteins / metabolism*
Muscle Contraction / drug effects
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, Wistar
rho-Associated Kinases / antagonists & inhibitors,  metabolism*
Reg. No./Substance:
0/Amides; 0/Antihypertensive Agents; 0/Carrier Proteins; 0/EBP50 protein, rat; 0/Microfilament Proteins; 0/Phosphoproteins; 0/Pyridines; 0/RNA, Small Interfering; 138381-45-0/Y 27632; 144131-77-1/moesin; 51-41-2/Norepinephrine; 56092-81-0/Ionomycin; 7447-40-7/Potassium Chloride; EC Kinases; EC Kinase C

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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