Translocation and association of ROCK-II with RhoA and HSP27 during contraction of rabbit colon smooth muscle cells.
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 = 0.05). There was also an increased association of ROCK-II with RhoA particulate fraction (147.46+/-9.31 and 148.22+/-9.41, n = 3, P = 0.05) and with HSP27 (155.6+/-10.7% increase, P = 0.05) in the particulate fraction. Pre-incubation of 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 = 0.05 and 174.65+/-28.36%, P = 0.05 increase in the di phospho-MLC at 30s and 4 min, respectively), which was inhibited upon pre-incubation with Y27632. Results suggest that ROCK-II undergoes a translocation to the particulate fraction with RhoA and with HSP27, suggesting that translocation and 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.
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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