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Originally published In Press as doi:10.1074/jbc.M010091200 on November 27, 2000

J. Biol. Chem., Vol. 276, Issue 8, 5605-5612, February 23, 2001
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A Model of Platelet Aggregation Involving Multiple Interactions of Thrombospondin-1, Fibrinogen, and GPIIbIIIa Receptor*

Arnaud BonnefoyDagger §, Roy Hantgan||, Chantal LegrandDagger , and Mony M. Frojmovic§**

From the Dagger  Unité 353 INSERM, Institut d'Hématologie, Université Paris VII, Hôpital St Louis, Cedex 10, Paris, France, the § Department of Physiology, McGill University, Montreal, Quebec H3G 1Y6, Canada, and the || Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157-1072

Thrombospondin-1 (TSP) may, after secretion from platelet alpha  granules, participate in platelet aggregation, but its mode of action is poorly understood. We evaluated the capacity of TSP to form inter-platelet cross-bridges through its interaction with fibrinogen (Fg), using either Fg-coated beads or Fg bound to the activated GPIIbIIIa integrin (GPIIbIIIa*) immobilized on beads or on activated fixed platelets (AFP), i.e. in a system free of platelet signaling and secretion mechanisms. Aggregation at physiological shear rates (100-2000 s-1) was studied in a microcouette device and monitored by flow cytometry. Soluble TSP bound to and induced aggregation of Fg-coated beads dose-dependently, which could be blocked by the amino-terminal heparin-binding domain of TSP, TSP18. Soluble TSP did not bind to GPIIbIIIa*-coated beads or AFP, unless they were preincubated with Fg. The interaction of soluble TSP with Fg-GPIIbIIIa*-coated beads or Fg-AFP resulted in the formation of aggregates via Fg-TSP-Fg cross-bridges, as demonstrated in a system where direct cross-bridges mediated by GPIIbIIIa*-Fg on one particle and free GPIIbIIIa* on a second particle were blocked by the RGD mimetic Ro 44-9883. Soluble TSP increased the efficiency of Fg-mediated aggregation of AFP by 30-110% over all shear rates and GPIIbIIIa* occupancies evaluated. Surprisingly, TSP binding to Fg already bound to its GPIIbIIIa* receptor appears to block the ability of this occupied Fg to recognize another GPIIbIIIa* receptor, but this TSP can indeed cross-bridge to another Fg molecule on a second platelet. Finally, TSP-coated beads could directly coaggregate at shear rates from 100 to 2000 s-1. Our studies provide a model for the contribution of secreted TSP in reinforcing inter-platelet interactions in flowing blood, through direct Fg-TSP-Fg and TSP-TSP cross-bridges.

* This work was supported by the Medical Research Council of Canada, the Heart and Stroke Foundation of Quebec, and the National Science Foundation.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.

Recipient of salary support from Sanofi-Thrombose, the International Council for Canadian Studies, the Heart and Stroke Foundation of Quebec, and from the Société Française d'Hématologie, with travel money from the Quebec-France exchange program of FRSQ-INSERM, which supported exchange between our two laboratories.

** To whom correspondence should be addressed: Dept of Physiology, McGill University, 3655 Drummond Ave., #1137, Montreal, Quebec H3G 1Y6, Canada. Tel.: 514-398-4326; Fax: 514-398-7452; E-mail: mony@med.mcgill.ca.

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