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Originally published In Press as doi:10.1074/jbc.M011511200 on January 18, 2001

J. Biol. Chem., Vol. 276, Issue 17, 13975-13981, April 27, 2001
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RGD-containing Peptides Inhibit Fibrinogen Binding to Platelet alpha IIbbeta 3 by Inducing an Allosteric Change in the Amino-terminal Portion of alpha IIb*

Ramesh B. BasaniDagger §, Giovanna D'AndreaDagger , Neal Mitra||, Gaston Vilaire||, Mark Richberg§, M. Anna KowalskaDagger , Joel S. Bennett||, and Mortimer PonczDagger §**

From the Dagger  Children's Hospital of Philadelphia and the Departments of § Pediatrics and || Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and the  Istituto di Ricovero e Cura a Carattere Scientifico Casa Sollievo della Sofferenza, Unitá di Aterosclerosi e Trombosi, Foggia 71013, Italy

To determine the molecular basis for the insensitivity of rat alpha IIbbeta 3 to inhibition by RGD-containing peptides, hybrids of human and rat alpha IIbbeta 3 and chimeras of alpha IIbbeta 3 in which alpha IIb was composed of portions of human and rat alpha IIb were expressed in Chinese hamster ovary cells and B lymphocytes, and the ability of the tetrapeptide RGDS to inhibit fibrinogen binding to the various forms of alpha IIbbeta 3 was measured. These measurements indicated that sequences regulating the sensitivity of alpha IIbbeta 3 to RGDS are located in the seven amino-terminal repeats of alpha IIb. Moreover, replacing the first three or four (but not the first two) repeats of rat alpha IIb with the corresponding human sequences enhanced sensitivity to RGDS, whereas replacing the first two or three repeats of human alpha IIb with the corresponding rat sequences had little or no effect. Nevertheless, RGDS bound to Chinese hamster ovary cells expressing alpha IIbbeta 3 regardless whether the alpha IIb in the heterodimers was human, rat, or a rat-human chimera. These results indicate that the sequences determining the sensitivity of alpha IIbbeta 3 to RGD-containing peptides are located in the third and fourth amino-terminal repeats of alpha IIb. Because RGDS binds to both human and rat alpha IIbbeta 3, the results suggest that differences in RGDS sensitivity result from differences in the allosteric changes induced in these repeats following RGDS binding.

* This work was supported in part by Grant HL40387 from the National Institutes of Health (to J. S. B. and M. P.) and by a generous contribution from the Plummer Family (to M. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Children's Hospital of Philadelphia, 34th St. and Civic Center Blvd., Philadelphia, PA 19104. Tel.: 215-590-3574; Fax: 215-590-3889; E-mail: poncz@email.chop.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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