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Articles in PresS, published online ahead of print October 2, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00188.2002
Submitted on April 24, 2002
Accepted on September 24, 2002
1 Molecular and Cellular Physiology, University of Cincinnati, College of Medicine, Cincinnati, OH, USA
2 Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL, USA
* To whom correspondence should be addressed. E-mail: Richard.Paul{at}uc.edu.
Fibroblasts form fibers when grown in culture media containing native type 1 collagen. The contractile forces generated can be precisely quantified and used to analyze the signal transduction pathways regulating fibroblast contraction. 30% calf serum induces a sustained contraction that is accompanied by a transient increase in intracellular calcium ([Ca2+]i). W-7, a calmodulin inhibitor, KN-62, an inhibitor of calcium/calmodulin dependent protein kinase, or ML-7, a myosin light chain kinase inhibitor, had no effects on either the contraction or the [Ca2+]i responses. Neither genistein, a tyrosine kinase inhibitor, nor calphostin C, a protein kinase C inhibitor had major effects on force or [Ca2+]i. In contrast, the Rho kinase inhibitors, Y-27632, or HA1077, depressed the contraction in a dose-dependent manner without affecting the [Ca2+]i response. Stress fiber formation was also suppressed by Y-27632. Surprisingly, calf serum, Y-27632, or calf serum plus Y-27632 did not alter mono- or di-phosphorylation of the myosin regulatory light chain (MRLC) compared to control untreated fibers. These results suggest that the sustained contraction of NIH 3T3 fibroblast fibers induced by calf serum is mediated by Rho kinase, but independent of a sustained increase in [Ca2+]i, calcium/calmodulin or C-kinase dependent pathways, or increases in MRLC phosphorylation.
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