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Am J Physiol Cell Physiol 275: C1081-C1086, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 4, C1081-C1086, October 1998

A role for MAP kinase in differentiated smooth muscle contraction evoked by alpha -adrenoceptor stimulation

Chantal Dessy1, Inkyeom Kim1, Carrie L. Sougnez1, Regent Laporte1,2, and Kathleen G. Morgan1,3

1 Signal Transduction Group, Boston Biomedical Research Institute, Boston 02114; and 3 Department of Medicine and 2 Department of Obstetrics and Gynecology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215

The purpose of this study was to investigate the potential role of mitogen-activated protein (MAP) kinase in smooth muscle contraction by monitoring MAP kinase activation, caldesmon phosphorylation, and contractile force during agonist stimulation. Isometric tension in response to KCl and phenylephrine (PE) was measured from strips of ferret aorta. MAP kinase activation was monitored by Western blot using a phosphospecific p44/p42 MAP kinase antibody. Caldesmon phosphorylation was assessed using specific phosphocaldesmon antibodies. We report here that treatment of smooth muscle strips with PD-098059, a specific inhibitor of MAP kinase kinase, did not detectably modify the KCl-evoked contraction but significantly inhibited the contraction to PE in the absence of extracellular Ca2+. In this experimental condition, where the contraction occurs in the absence of increases in 20-kDa myosin light chain phosphorylation, PD-098059 also inhibited significantly MAP kinase and caldesmon phosphorylation. Collectively, these results demonstrate a direct cause-and-effect relationship between MAP kinase activation and Ca2+-independent smooth muscle contraction and support the concept of caldesmon phosphorylation as the missing link between both events.

mitogen-activated protein kinase; caldesmon; calcium-independent contraction; phenylephrine; ferret aorta; thin-filament regulation


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