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J Biol Chem, Vol. 274, Issue 2, 918-923, January 8, 1999
From the Department of Cell Biology and Neuroscience, University of
Texas Southwestern Medical School, Dallas, Texas 75235
To learn more about the regulation of contraction
of collagen matrices by fibroblasts, we compared the ability of
lysophosphatidic acid (LPA) and platelet-derived growth factor (PDGF)
to stimulate contraction of floating and stressed collagen matrices. In
floating collagen matrices, PDGF and LPA stimulated contraction with
similar kinetics, but appeared to utilize complementary signaling
pathways since contraction obtained by the combination of growth
factors exceeded that observed with saturating concentrations of either alone. The PDGF-simulated pathway was selectively inhibited by the
protein kinase inhibitor KT5926. In stressed collagen matrices, PDGF
and LPA stimulated contraction with different kinetics, with LPA acting
rapidly and PDGF acting only after an ~1-h lag period. Pertussis
toxin, known to block signaling through the Gi class of heterotrimeric G-proteins, inhibited LPA-stimulated contraction of
floating but not stressed matrices, suggesting that LPA-stimulated contraction depends on receptors coupled to different G-proteins in
floating and stressed matrices. On the other hand, the Rho inhibitor C3
exotransferase blocked contraction of both floating and stressed
collagen matrices. These results suggest the possibility that distinct
signaling mechanisms regulate contraction of floating and stressed
collagen matrices.
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