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J. Biol. Chem., Vol. 266, Issue 26, 17106-17111, 09, 1991
AL Frelinger 3d, XP Du, EF Plow and MH Ginsberg
Occupancy of integrin receptors induces conformational changes in the
receptor, resulting in exposure of novel interactive sites termed
ligand-induced binding sites (LIBS). We report here that Fab fragments of
certain antibodies against LIBS on integrin alpha IIb beta 3 (platelet
glycoprotein IIb-IIIa) block platelet aggregation. Thus, certain LIBS or
the regions surrounding them may participate in events required for
platelet aggregation. In addition, certain anti-alpha IIb beta 3 LIBS Fab
fragments stimulated platelet aggregation. This was due to induction of fg
binding to alpha IIb beta 3, apparently by shifting a conformational
equilibrium between a "resting" and an "activated" state of alpha IIb beta
3. Some of the activating anti-LIBS Fab fragments also induced high
affinity fibronectin binding to alpha IIb beta 3, whereas others did not.
Thus, changes in the conformation of this integrin modulate both the
specificity and affinity of ligand recognition.
Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
Research Institute of Scripps Clinic, La Jolla, California 92037.
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