The IIb-IIIa glycoprotein complex that mediates platelet aggregation is directly implicated in leukocyte adhesion |
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| Authors: | G F Burns L Cosgrove T Triglia J A Beall A F López J A Werkmeister C G Begley A P Haddad A J d'Apice M A Vadas |
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| Institution: | 1. Academic Medical Center, University of Amsterdam, Department of Internal Medicine, Geriatrics section, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands;2. Gelre Hospitals, Department of Geriatrics, Albert Schweitzerlaan 31, 7334 DZ Apeldoorn, The Netherlands;3. Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;4. University Medical Center Groningen, University Centre for Geriatric Medicine, Hanzeplein 1, 9713 GZ Groningen, The Netherlands;1. Fondation Ophtalmologique A. de Rothschild, Unité de Chronobiologie, 25 rue Manin, 75019 Paris, France;2. UHSA - Groupe Hospitalier Paul Guiraud, 54, avenue de la République, 94806 Villejuif, France |
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| Abstract: | Evidence is presented that the IIb-IIIa glycoprotein complex, which functions as the receptor for fibrinogen on platelets and is central to platelet aggregation, is expressed on the surface of leukocytes where it may function as a receptor for fibronectin. F(ab')2 fragments of a monoclonal antibody, 25E11, raised against activated large granular lymphocytes, inhibited killing by natural killer cells, blocked the binding of fibronectin-coated particles by monocytes, and stimulated neutrophils to exhibit increased antibody-dependent killing. Immunoprecipitation studies of leukocytes and platelets, and the ability of 25E11 to inhibit platelet aggregation, identified the antigen as an epitope on the IIb-IIIa complex. This glycoprotein thus constitutes the first example of a receptor mediating both platelet aggregation and leukocyte adhesion. |
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