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3-Integrins
That Regulates the Dissociation Rate for RGD Ligands
(Received for publication, February 23, 1996, and in revised form, May 1, 1996)
,
From the Here we use a model RGD-containing ligand to
study how Ca2+ and Mg2+ regulate ligand binding
to 
Program on Cell Adhesion, Cancer Research
Center, The Burnham Institute, La Jolla, California 92037 and the
¶ Department of Molecular Biology (MB11), The Scripps Research
Institute, La Jolla, California 92037
3-integrins. Fab-9, an antibody that contains an optimized RGD
loop in its antigen binding site (Barbas, C. F., Languino, L., and
Smith, J. W. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 10003-10007), was used as the model ligand. Across a physiologic range
of Mg2+, Fab-9 bound to both 
v3 and IIb3 with a
monophasic binding isotherm. Across the same range of Ca2+,
the binding of Fab-9 to the 3-integrins was biphasic. Low
concentrations of Ca2+ (µM) promoted the
binding of Fab-9. Higher concentrations of Ca2+
(mM) blocked Fab-9 binding. These data suggest that
Ca2+ binds to two distinct classes of sites on the
3-integrins, with the low affinity Ca2+ binding site(s)
being an inhibitory site. We designate this inhibitory site(s) as the I
site. Further biochemical characterization showed that the I site has
the following characteristics: 1) it is specific for Ca2+;
2) it is allosteric to the ligand binding site; 3) its occupation
increases the dissociation rate between integrin and RGD ligand; and 4)
occupation of the I site can induce cellular deadhesion.
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