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J Biol Chem, Vol. 273, Issue 52, 34710-34715, December 25, 1998

Two-stage Activation for alpha 5beta 1 Integrin Binding to Surface-adsorbed Fibronectin

Andrés J. García, Junichi Takagi, and David Boettiger

From the Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104 and the  Department of Biological Sciences, Tokyo Institute of Technology, Yokohama, Japan

By analyzing the functional binding of alpha 5beta 1 integrin to adsorbed fibronectin in intact cells, we demonstrate that integrin activation results in linear increases in adhesion strength as a function of ligand density, suggesting that modulation of the receptor-ligand interaction is the dominant mechanism for adhesion during the initial stages of adhesion and that cooperative binding contributes little to initial adhesion strength. Using this experimental framework, we show the existence of three distinct activation states for alpha 5beta 1 integrin binding to adsorbed fibronectin for both passive, antibody-induced and active, cell-controlled activation. During the initial phase of adhesion, alpha 5beta 1 integrin is activated in an energy-dependent process from the nonbinding ground state to an intermediate state in which the receptor binds fibronectin and provides significant mechanical coupling. In later stages of adhesion maturation, alpha 5beta 1 integrin is activated to a higher binding state, which provides significant increases in adhesion strength compared with the intermediate state. These multiple binding states most likely result from different integrin conformations and reflect distinct interactions between alpha 5beta 1 and sites on adsorbed fibronectin. Multiple activation states for alpha 5beta 1 suggest the existence of distinct stages in adhesion signaling and strengthening and can provide a versatile mechanism for the regulation of adhesive interactions.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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