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Am J Physiol Gastrointest Liver Physiol 279: G201-G210, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 1, G201-G210, July 2000

Sustained muscle contraction induced by agonists, growth factors, and Ca2+ mediated by distinct PKC isozymes

K. S. Murthy, J. R. Grider, J. F. Kuemmerle, and G. M. Makhlouf

Departments of Medicine and Physiology, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298

The role of protein kinase C (PKC) in sustained contraction was examined in intestinal circular and longitudinal muscle cells. Initial contraction induced by agonists (CCK-8 and neuromedin C) was abolished by 1) inhibitors of Ca2+ mobilization (neomycin and dimethyleicosadienoic acid), 2) calmidazolium, and 3) myosin light chain (MLC) kinase (MLCK) inhibitor KT-5926. In contrast, sustained contraction was not affected by these inhibitors but was abolished by 1) the PKC inhibitors chelerythrine and calphostin C, 2) PKC-epsilon antibody, and 3) a pseudosubstrate PKC-epsilon inhibitor. GDPbeta S abolished both initial and sustained contraction, whereas a Galpha q/11 antibody inhibited only initial contraction, implying that sustained contraction was dependent on activation of a distinct G protein. Sustained contraction induced by epidermal growth factor was inhibited by calphostin C, PKC-alpha ,beta ,gamma antibody, and a pseudosubstrate PKC-alpha inhibitor. Ca2+ (0.4 µM) induced an initial contraction in permeabilized muscle cells that was blocked by calmodulin and MLCK inhibitors and a sustained contraction that was blocked by calphostin C and a PKC-alpha ,beta ,gamma antibody. Thus initial contraction induced by Ca2+, agonists, and growth factors is mediated by MLCK, whereas sustained contraction is mediated by specific Ca2+-dependent and -independent PKC isozymes. G protein-coupled receptors are linked to PKC activation via distinct G proteins.

calcium sensitization; intestinal smooth muscle; protein kinase C; myosin light chain kinase


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