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First published online 23 May 2006
doi: 10.1242/jcs.02970
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Research Article |
vß5 integrin activity in B82L fibroblasts
1 Graduate Programs in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, WI 53706, USA
2 Graduate Programs in Molecular and Cellular Pharmacology, University of Wisconsin-Madison, Madison, WI 53706, USA
3 Graduate Programs in Department of Pathology and Laboratory Medicine, University of Wisconsin-Madison, Madison, WI 53706, USA
Author for correspondence (e-mail: acraprae{at}wisc.edu)
Accepted 7 March 2006
B82L mouse fibroblasts respond to fibronectin or vitronectin via a syndecan-1-mediated activation of the 
vß5 integrin. Cells attached to syndecan-1-specific antibody display only filopodial extension. However, the syndecan-anchored cells extend lamellipodia when the antibody-substratum is supplemented with serum, or low concentrations of adsorbed vitronectin or fibronectin, that are not sufficient to activate the integrin when plated alone. Integrin activation is blocked by treatment with (Arg-Gly-Asp)-containing peptides and function-blocking antibodies that target v integrins, as well as by siRNA-mediated silencing of ß5 integrin expression. In addition, vß5-mediated cell attachment and spreading on high concentrations of vitronectin is blocked by competition with recombinant syndecan-1 ectodomain core protein and by downregulation of mouse syndecan-1 expression by mouse-specific siRNA. Taking advantage of the species-specificity of the siRNA, rescue experiments in which human syndecan-1 constructs are expressed trace the activation site to the syndecan-1 ectodomain. Moreover, both full-length mouse and human syndecan-1 co-immunoprecipitate with the ß5 integrin subunit, but fail to do so if the syndecan is displaced by competition with soluble, recombinant syndecan-1 ectodomain. These results suggest that the ectodomain of the syndecan-1 core protein contains an active site that assembles into a complex with the vß5 integrin and regulates vß5 integrin activity.
Key words: Syndecan-1, vß5 integrin, Cell adhesion, Extracellular matrix, Vitronectin, Proteoglycan
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