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Vol. 15, Issue 12, 5670-5677, December 2004
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Department of Molecular Biology, Princeton University, Princeton, NJ 08544-1014
Submitted August 31, 2004;
Accepted September 22, 2004
Monitoring Editor: Mark Ginsberg
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.
Abbreviations used: CHO, Chinese hamster ovary; CSPG, chondroitin sulfate proteoglycan; ECM, extracellular matrix; FAK, focal adhesion kinase; FN, fibronectin; GAG, glycosaminoglycans; HSPG, heparan sulfate proteoglycan; REF, rat embryo fibroblasts.
* Present address: Kennedy Institute of Rheumatology Division, Imperial College London, 1 Aspenlea Road, Hammersmith, London W6 8LH, UK.
Corresponding author. E-mail address: jschwarzbauer{at}molbio.princeton.edu.
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