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J Biol Chem, Vol. 273, Issue 18, 10988-10993, May 1, 1998
5
1
Integrin-Fibronectin Bonds in Intact Adherent Cells Is Sensitive to
Integrin Activation State
From the Department of Microbiology, University of Pennsylvania,
Philadelphia, Pennsylvania 19104
Binding of integrin receptors to extracellular
ligands is a complex process involving receptor-ligand interactions at
the cell-substrate interface, signals activating the receptors, and assembly of cytoskeletal and adhesion plaque proteins at the
cytoplasmic face. To analyze the contribution of these elements to
overall cell adhesion, we have developed a model system that
characterizes the functional binding characteristic for adhesion
receptors as the force required to separate the integrin-ligand bond. A
spinning disk device was used to apply a range of controlled
hydrodynamic forces to adherent cells. The adhesion of K562
erythroleukemia cells, a cell line expressing a single fibronectin
receptor, integrin 
5
1, which was
uniformly activated with the monoclonal antibody TS2/16, to defined
fibronectin surface densities was examined. Cell adhesion strength
increased linearly with receptor and ligand densities. Based on
chemical equilibrium principles, it is shown that adhesion strength is
directly proportional to the number of receptor-ligand bonds. This
analysis provides for the definition of a new physical parameter, the
adhesion constant 
, which is related to the bond strength and
binding equilibrium constant and has units of
force-length2. This parameter can be measured by the
experimental system presented and is governed by the activation state
of integrin receptors. This simplified model isolates the integrin
receptor-ligand binding parameters and provides a basis for analysis of
the functions of signaling and cytoskeletal elements in the adhesion
process.
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