@article{83586,
  keywords = {Animals, Humans, Rats, signal transduction, Enzyme Activation, Mice, Fibroblasts, Fibronectins, Extracellular Matrix, Cell Adhesion, NIH 3T3 Cells, Calcium-Binding Proteins, Cell Shape, Extracellular Signal-Regulated MAP Kinases, Lysophospholipids, Syndecan-4, Tenascin},
  author = {Selwyn Williams and Jean Schwarzbauer},
  title = {A shared mechanism of adhesion modulation for tenascin-C and fibulin-1.},
  abstract = {<p>Adhesion modulatory proteins are important effectors of cell-matrix interactions during tissue remodeling and regeneration. They comprise a diverse group of matricellular proteins that confer antiadhesive properties to the extracellular matrix (ECM). We compared the inhibitory effects of two adhesion modulatory proteins, fibulin-1 and tenascin-C, both of which bind to the C-terminal heparin-binding (HepII) domain of fibronectin (FN) but are structurally distinct. Here, we report that, like tenascin-C, fibulin-1 inhibits fibroblast spreading and cell-mediated contraction of a fibrin-FN matrix. These proteins act by modulation of focal adhesion kinase and extracellular signal-regulated kinase signaling. The inhibitory effects were bypassed by lysophosphatidic acid, an activator of RhoA GTPase. Fibroblast response to fibulin-1, similar to tenascin-C, was dependent on expression of the heparan sulfate proteoglycan syndecan-4, which also binds to the HepII domain. Therefore, blockade of HepII-mediated signaling by competitive binding of fibulin-1 or tenascin-C represents a shared mechanism of adhesion modulation among disparate modulatory proteins.</p>
},
  year = {2009},
  journal = {Mol Biol Cell},
  volume = {20},
  pages = {1141-9},
  month = {02/2009},
  issn = {1939-4586},
  doi = {10.1091/mbc.E08-06-0621},
  language = {eng},
}