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Integrin-fibronectin interactions at the cell-material interface: initial integrin binding and signaling


Integrin-fibronectin interactions at the cell-material interface: initial integrin binding and signaling



Biomaterials 20(23-24): 2427-2433



ISSN/ISBN: 0142-9612

PMID: 10614947

DOI: 10.1016/s0142-9612(99)00170-2

Integrin receptors mediate cell adhesion to extracellular matrices and provide signals that direct proliferation and differentiation. Integrin binding involves receptor-ligand interactions at the cell-substrate interface and assembly and reorganization of structural and signaling elements at the cytoplasmic face. Using a cross-linking/extraction/reversal method to quantify bound integrins, we demonstrate that the density of alpha5beta1 integrin-fibronectin bonds increases linearly with ligand density, as predicted by simple receptor-ligand equilibrium. This linear relationship is consistent with linear increases in cell adhesion strength with receptor and ligand surface densities. Furthermore, we show that phosphorylation of FAK, a tyrosine kinase involved in early integrin-mediated signaling, increases linearly with the number of integrin-Fn bonds. These linear relationships suggest the absence of cooperative effects in the initial stages of mechanical coupling and adhesion-mediated signaling.

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Accession: 010859598

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