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Syndecan-4 is a ubiquitously expressed heparan sulfate proteoglycan that modulates cell interactions with the extracellular matrix. It is transiently up-regulated during tissue repair by cells that mediate wound healing. Here, we report that syndecan-4 is essential for optimal fibroblast response to the three-dimensional fibrin-fibronectin provisional matrix that is deposited upon tissue injury. Interference with syndecan-4 function inhibits matrix contraction by preventing cell spreading, actin stress fiber formation, and activation of focal adhesion kinase and RhoA mediated-intracellular signaling pathways. Tenascin-C is an extracellular matrix protein that regulates cell response to fibronectin within the provisional matrix. Syndecan-4 is also required for tenascin-C action. Inhibition of syndecan-4 function suppresses tenascin-C activity and overexpression of syndecan-4 circumvents the effects of tenascin-C. In this way, tenascin-C and syndecan-4 work together to control fibroblast morphology and signaling and regulate events such as matrix contraction that are essential for efficient tissue repair.

Original publication

DOI

10.1091/mbc.e04-08-0759

Type

Journal article

Journal

Mol Biol Cell

Publication Date

12/2004

Volume

15

Pages

5670 - 5677

Keywords

Animals, Cell Line, Cricetinae, DNA, Complementary, Extracellular Matrix, Fibrin, Fibronectins, Membrane Glycoproteins, Mice, Mice, Knockout, Proteoglycans, Rats, Signal Transduction, Syndecan-4, Tenascin, rhoA GTP-Binding Protein