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J. Biol. Chem., Vol. 275, Issue 22, 16779-16787, June 2, 2000
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Signaling across the Platelet Adhesion Receptor Glycoprotein Ib-IX Induces alpha IIbbeta 3 Activation Both in Platelets and a Transfected Chinese Hamster Ovary Cell System*

Yona ZaffranDagger , Sylvie C. MeyerDagger , Emil NegrescuDagger , Kumar B. ReddyDagger , and Joan E. B. FoxDagger §

From the Dagger  Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195 and § Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106

In platelets, alpha IIbbeta 3 exists in a form that cannot bind adhesive proteins in the plasma; although it can interact with immobilized fibrinogen it cannot interact with immobilized von Willebrand factor in the vessel wall. Soluble agonists such as thrombin convert alpha IIbbeta 3 to a form that recognizes soluble and immobilized ligands. Attempts to reconstitute alpha IIbbeta 3 activation in a non-hematopoietic, nucleated cell system have been unsuccessful. In the present study, we have developed a transfected Chinese hamster ovary cell model in which alpha IIbbeta 3 activation is induced by signaling across glycoprotein (GP) Ib-IX by its ligand, von Willebrand factor. GPIb-IX activates not only the transfected alpha IIbbeta 3 but also endogenous alpha vbeta 3. Activation of the pathways leading to integrin activation occurred even in cells transfected with GPIb-IX lacking the domain on GPIbalpha that binds 14-3-3 or that which binds actin-binding protein. These studies demonstrate that signals induced by interaction of GPIb-IX with von Willebrand factor lead to alpha IIbbeta 3 activation and suggest that the signaling pathways by which GPIb-IX induces alpha IIbbeta 3 activation are different to those used by thrombin. Elucidation of these differences may provide insights into therapeutic ways in which to inhibit integrin activation in selective clinical settings.

* This work was supported by Research Grants HL30657 and HL56264 (to J. E. B. F.) from the National Institutes of Health.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: Joseph J. Jacobs Centre for Thrombosis and Vascular Biology (NB 50), The Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Tel. 216-445-3874; Fax: 216-445-2051.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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