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Overview: Assays for Studying Integrin-Dependent Cell Adhesion

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Integrin and Cell Adhesion Molecules

Part of the book series: Methods in Molecular Biology ((MIMB,volume 757))

Abstract

Interaction of the integrin receptors with ligands determines the molecular basis of integrin-dependent cell adhesion. Integrin ligands are typically large proteins with relatively low binding affinities. This makes direct ligand-binding kinetic measurements somewhat difficult. Here we examine several real-time methods, aimed to overcome these experimental limitations and to distinguish the regulation of integrin conformation and affinity. This chapter includes: the use of a small ligand-mimetic probe for studies of inside-out regulation of integrin affinity and unbending, real-time cell aggregation and disaggregation kinetics to probe integrin conformational states and the number of integrin–ligand bonds, as well as the real-time monitoring of ligand-induced epitopes under signaling through G-protein-coupled receptors, and others. Experimental data obtained using these novel methods are summarized in terms of the current model of integrin activation.

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Acknowledgments

This work was supported by R01HL081062 and U54MH084690.

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Correspondence to Alexandre Chigaev .

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Chigaev, A., Sklar, L.A. (2011). Overview: Assays for Studying Integrin-Dependent Cell Adhesion. In: Shimaoka, M. (eds) Integrin and Cell Adhesion Molecules. Methods in Molecular Biology, vol 757. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-166-6_1

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  • DOI: https://doi.org/10.1007/978-1-61779-166-6_1

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-61779-165-9

  • Online ISBN: 978-1-61779-166-6

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