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Am J Physiol Cell Physiol 286: C8-C21, 2004. First published September 10, 2003; doi:10.1152/ajpcell.00428.2002
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PROTEIN AND VESICLE TRAFFICKING, CYTOSKELETON

Rho-kinase-mediated Ca2+-independent contraction in rat embryo fibroblasts

Daniel A. Emmert,1,* Judy A. Fee,2,* Zoe M. Goeckeler,1 Jeremy M. Grojean,1 Tetsuro Wakatsuki,2 Elliot L. Elson,2 B. Paul Herring,3 Patricia J. Gallagher,3 and Robert B. Wysolmerski1

1Departments of Pathology, Saint Louis University School of Medicine, St. Louis 63104; 2Department of Biochemistry & Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110; and 3Department of Physiology, Indiana University School of Medicine, Indianapolis, Indiana 46202

Submitted 16 September 2002 ; accepted in final form 22 August 2003

Thus far, determining the relative contribution of Ca2+/calmodulin-dependent myosin light chain kinase (MLCK) and Ca2+-independent Rho-kinase pathways to myosin II activation and contraction has been difficult. In this study, we characterize the role of Rho-kinase in a rat embryo fibroblast cell line (REF-52), which contains no detectable MLCK. No endogenous MLCK could be detected in REF-52 cells by either Western or Northern blot analysis. In the presence or absence of Ca2+, thrombin or lysophosphatidic acid (LPA) increased RhoA activity and Rhokinase activity, correlating with isometric tension development and myosin II regulatory light chain (RLC) phosphorylation. Resting tension is associated with a basal phosphorylation of 0.31 ± 0.02 mol PO4/mol RLC, whereas upon LPA or thrombin treatment myosin II RLC phosphorylation increases to 1.08 ± 0.05 and 0.82 ± 0.05 mol PO4/mol RLC, respectively, within 2.5 min. Ca2+ chelation has minimal effect on the kinetics and magnitude of isometric tension development and RLC phosphorylation. Treatment of REF-52 cells with the Rho-kinase-specific inhibitor Y-27632 abolished thrombin- and LPA-stimulated contraction and RLC phosphorylation. These results suggest that Rho-kinase is sufficient to activate myosin II motor activity and contraction in REF-52 cells.

myosin light chain kinase; RhoA; myosin II regulatory light chain phosphorylation


Address for reprint requests and other correspondence: R. B. Wysolmerski, Dept. of Pathology, Saint Louis Univ. School of Medicine, 1402 S. Grand Blvd., St. Louis, MO 63104 (E-mail: wysolmer{at}slucare1.sluh.edu).




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