The isoenzyme of protein kinase c induces a ca2+-independent contraction in vascular smooth muscle. Horowitz, Arie, Odile Cl[acute]ement-Chomienne, Michael P. Walsh, and Kathleen G. Morgan. Program in Smooth Muscle Research, Charles A. Dana Research Institute, Harvard-Thorndike Laboratory, Cardiovascular Division, Beth Israel Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02215; Boston Biomedical Research Institute, Boston, MA 02114; Department of Medical Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1, Canada
APStracts 3:0076C, 1996.
We provide here the first direct evidence for in situ functional specificity of PKC as a regulator of smooth muscle contractility. Protein kinase C (PKC) is known to cause a Ca2+-independent contraction of ferret aorta smooth muscle, and the expression of two Ca2+-independent PKC isoenzymes, and z, has been demonstrated in this tissue. To test directly the hypothesis that one of these isoenzymes regulates contractility, constitutively active forms of PKC and PKCz were applied to saponin-permeabilized single ferret aortic smooth muscle cells. PKCz caused no significant force response, but PKC induced contraction of a magnitude (105 +/- 8 [mu]g) similar to that produced by phenylephrine (110 +/-10 [mu]g), a relatively selective 1-adrenergic agonist that triggers a PKC-dependent contraction. The PKC -induced contraction was reversed by the PKC pseudosubstrate inhibitory peptide, PKC19-31. The myosin light chain kinase inhibitor ML-9 did not affect the force response of PKC -activated cells, suggesting that PKC may induce this contraction solely via thin filament disinhibition. In support of this conclusion, calponin and caldesmon were shown to be good in vitro substrates of PKC but not of PKCz.

Received 28 September 1995; accepted in final form 26 February
1996.
APS Manuscript Number C595-5.
Article publication pending Am. J. Physiol. (Cell Physiology).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 20 March 96