@article{83696,
  keywords = {Animals, Rats, signal transduction, Cell Line, Mice, rhoA GTP-Binding Protein, Mice, Knockout, DNA, Complementary, Membrane Glycoproteins, Fibronectins, Extracellular Matrix, Syndecan-4, Tenascin, Cricetinae, Fibrin, Proteoglycans},
  author = {Kim Midwood and Leyla Valenick and Henry Hsia and Jean Schwarzbauer},
  title = {Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4.},
  abstract = {<p>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.</p>
},
  year = {2004},
  journal = {Mol Biol Cell},
  volume = {15},
  pages = {5670-7},
  month = {12/2004},
  issn = {1059-1524},
  doi = {10.1091/mbc.E04-08-0759},
  language = {eng},
}