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Translocation and association of ROCK-II with RhoA and HSP27 during contraction of rabbit colon smooth muscle cells.
Patil, Suresh B; Tsunoda, Yasuhiro; Pawar, Mercy D; Bitar, Khalil N.
Affiliation
  • Patil SB; Department of Pediatrics, University of Michigan, Ann Arbor, MI 48109, USA.
Biochem Biophys Res Commun ; 319(1): 95-102, 2004 Jun 18.
Article in En | MEDLINE | ID: mdl-15158447
ABSTRACT
The focus of the paper is to understand the role of HSP27 in mediating the association of RhoA with ROCK-II in sustained contraction of smooth muscle cells from the rabbit colon. In circular smooth muscle cells; acetylcholine-induced contraction (10(-7)M) was associated with translocation of ROCK-II to the particulate fraction, which remained sustained at 4 min after stimulation (135.1+/-8.1% increase, P association of ROCK-II with RhoA particulate fraction (147.46+/-9.31 and 148.22+/-9.41, n = 3, P cells with Y27632 resulted in the inhibition of the association of ROCK-II with RhoA in the particulate fraction. Acetylcholine (10(-7)M) induced sustained phosphorylation of MLC (122.75+/-9.97%, P association of ROCK-II with RhoA is mediated by HSP27. Maintenance of the functional association of RhoA with ROCK-II in the particulate fraction mediated by HSP27 appears to be important to retain MLC in the phosphorylated state and hence the sustained contraction.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Protein Serine-Threonine Kinases / Colon / RhoA GTP-Binding Protein / Heat-Shock Proteins / Muscle Contraction / Muscle, Smooth / Neoplasm Proteins Type of study: Prognostic_studies / Risk_factors_studies Limits: Animals Language: En Journal: Biochem Biophys Res Commun Year: 2004 Document type: Article Affiliation country: Estados Unidos
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Collection: 01-internacional Database: MEDLINE Main subject: Protein Serine-Threonine Kinases / Colon / RhoA GTP-Binding Protein / Heat-Shock Proteins / Muscle Contraction / Muscle, Smooth / Neoplasm Proteins Type of study: Prognostic_studies / Risk_factors_studies Limits: Animals Language: En Journal: Biochem Biophys Res Commun Year: 2004 Document type: Article Affiliation country: Estados Unidos
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