title: Overview: assays for studying integrin-dependent cell adhesion.
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.
authors: Department of Pathology and Cancer Center, University of New Mexico Health Sciences Center, Albuquerque, NM, USA. achigaev@salud.unm.edu
authors: Alexandre
authors: A
authors: Chigaev
authors: Larry A
authors: LA
authors: Sklar
mesh_terms: D000911:Antibodies, Monoclonal / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology*; D005434:Flow Cytometry; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D000911:Antibodies, Monoclonal; D016023:Integrins; D008024:Ligands