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5ß1 Integrin–Fibronectin Interaction
* Department of Physiology and Biophysics, University of Miami School of Medicine, Miami, Florida 33136 and Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710
Correspondence: Address reprint requests to Vincent T. Moy, Dept. of Physiology and Biophysics, University of Miami School of Medicine, 1600 N.W. 10th Avenue, Miami, FL 33136. Tel.: 305-243-3201; Fax: 305-243-5931; E-mail: vmoy{at}newssun.med.miami.edu.
The interaction of the 
5ß1 integrin and its ligand, fibronectin (FN), plays a crucial role in the adhesion of cells to the extracellular matrix. An important intrinsic property of the 5ß1/FN interaction is the dynamic response of the complex to a pulling force. We have carried out atomic force microscopy measurements of the interaction between 5ß1 and a fibronectin fragment derived from the seventh through tenth type III repeats of FN (i.e., FN7-10) containing both the arg-gly-asp (RGD) sequence and the synergy site. Direct force measurements obtained from an experimental system consisting of an 5ß1 expressing K562 cell attached to the atomic force microscopy cantilever and FN7-10 adsorbed on a substrate were used to determine the dynamic response of the 5ß1/FN7-10 complex to a pulling force. The experiments were carried out over a three-orders-of-magnitude change in loading rate and under conditions that allowed for detection of individual 5ß1/FN7-10 interactions. The dynamic rupture force of the 5ß1/FN7-10 complex revealed two regimes of loading: a fast loading regime (>10,000 pN/s) and a slow loading regime (<10,000 pN/s) that characterize the inner and outer activation barriers of the complex, respectively. Activation by TS2/16 antibody increased both the frequency of adhesion and elevated the rupture force of the 5ß1/wild type FN7-10 complex to higher values in the slow loading regime. In experiments carried out with a FN7-10 RGD deleted mutant, the force measurements revealed that both inner and outer activation barriers were suppressed by the mutation. Mutations to the synergy site of FN, however, suppressed only the outer barrier activation of the complex. For both the RGD and synergy deletions, the frequency of adhesion was less than that of the wild type FN7-10, but was increased by integrin activation. The rupture force of these mutants was only slightly less than that of the wild type, and was not increased by activation. These results suggest that integrin activation involved a cooperative interaction with both the RGD and synergy sites.
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