HSP27 is a mediator of sustained smooth muscle contraction in response to bombesin

We have identified the low MW 27 kD heat shock protein as a major phosphoprotein constituent of smooth muscle and have investigated its potential role in agonist induced smooth muscle contraction. The neuropeptides bombesin and substance P, which are present in neurons of the anorectal region, induc...

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Published inBiochemical and biophysical research communications Vol. 181; no. 3; pp. 1192 - 1200
Main Authors Bitar, Khalil N., Kaminski, Mark S., Hailat, Nabil, Cease, Kemp B., Strahler, John R.
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 31.12.1991
Elsevier
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Summary:We have identified the low MW 27 kD heat shock protein as a major phosphoprotein constituent of smooth muscle and have investigated its potential role in agonist induced smooth muscle contraction. The neuropeptides bombesin and substance P, which are present in neurons of the anorectal region, induce contraction of isolated smooth muscle cells from this region by activating different intracellular pathways. Substance P-induced contraction is 1,4,5-inositol trisphosphate (IP 3)/calmodulin dependent, while contraction induced by bombesin is mediated by a protein kinase C (PKC)-dependent pathway. The sustained contraction induced by bombesin or exogenous PKC was blocked by preincubation of cells with monoclonal antibodies to hsp27, while the transient contraction induced by substance P or IP 3 was unaffected by the antibodies. Preincubation with isotype matched control antibodies had no inhibitory effect on contraction induced in response to the agents used. These data support a novel role for hsp27 in the non calmodulin mediated sustained contraction induced by bombesin or PKC.
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(91)92065-R