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

Paper ID Volume ID Publish Year Pages File Format Full-Text
13936 974 1999 7 PDF Available
Title
Integrin–fibronectin interactions at the cell-material interface: initial integrin binding and signaling
Abstract

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 α5β1 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.

Keywords
Fibronectin; Integrins; Cell adhesion; Signaling; FAK
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Integrin–fibronectin interactions at the cell-material interface: initial integrin binding and signaling
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 20, Issues 23–24, December 1999, Pages 2427–2433
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us