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Issue 3, 2007
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Integrins and syndecan-4 make distinct, but critical, contributions to adhesion contact formation

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Abstract

During cell adhesion to fibronectin there is a major reorganisation of the actin cytoskeleton and concomitant formation of adhesion complexes. Conflicting studies of adhesion receptors report that either integrin alone, or both integrin and syndecan-4 mediate the formation of vinculin-containing adhesions, and differences in these studies have been attributed to the density and conformational integrity of ligands used. We have endeavoured to resolve these issues by ELISA analysis of immobilised polypeptides, and found that ligands of both integrin α5β1 and syndecan-4 are necessary for focal adhesion formation under conditions of equivalent density of folded ligand. We also demonstrate that integrin and syndecan-4 play quite distinct roles in adhesion contact maturation and are not interchangeable. These results help us to understand how cells respond efficiently to changes in matrix environment, which should prove useful for developing approaches to aid wound healing.

Graphical abstract: Integrins and syndecan-4 make distinct, but critical, contributions to adhesion contact formation

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Article information


Submitted
09 Oct 2006
Accepted
05 Dec 2006
First published
03 Jan 2007

Soft Matter, 2007,3, 372-376
Article type
Paper

Integrins and syndecan-4 make distinct, but critical, contributions to adhesion contact formation

M. D. Bass, M. R. Morgan and M. J. Humphries, Soft Matter, 2007, 3, 372
DOI: 10.1039/B614610D

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