Purification of the Porcine Platelet GP IIb-IIIa Complex and the Propolypeptide of von Willebrand Factor

Teresa Royo; Matilde Vidal; Lina Badimon

doi:10.1055/s-0037-1615192

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1998; 80(02): 302-309
DOI: 10.1055/s-0037-1615192

Rapid Communication

Schattauer GmbH

Purification of the Porcine Platelet GP IIb-IIIa Complex and the Propolypeptide of von Willebrand Factor

Teresa Royo

¹Cardiovascular Research Center, IIBBCSIC-Hospital de la Santa Creu i Sant Pau-UAB. Research Institute Sant Pau, Barcelona, Spain

,

Matilde Vidal

¹Cardiovascular Research Center, IIBBCSIC-Hospital de la Santa Creu i Sant Pau-UAB. Research Institute Sant Pau, Barcelona, Spain

,

Lina Badimon

¹Cardiovascular Research Center, IIBBCSIC-Hospital de la Santa Creu i Sant Pau-UAB. Research Institute Sant Pau, Barcelona, Spain

› Institutsangaben

Abstract

Summary

Platelet membrane glycoproteins (GP) are involved in platelet adhesion and aggregation. The glycoprotein IIb-IIIa complex (GP IIbIIIa) is a Ca²⁺-dependent heterodimer that binds fibrinogen and other adhesive proteins, thereby mediating platelet aggregation and adhesion. We have purified two major glycoproteins from pig platelets by Concanavalin A-Sepharose, Heparin-Sepharose and Sephacryl S-300 HR chromatography (Fitzgerald et al. Anal Biochem, 1985): i) the GP IIb-IIIa complex, GP IIb Mr = 140,000 and GP IIIa a single chain of Mr = 95,000-100,000; and ii) a predominant glycoprotein of high molecular weight, the propolypeptide of von Willebrand factor (Mr = 80,000-100,000). Western-blot analysis of the purified GP IIb-IIIa showed that only certain monoclonal antibodies against the human receptor specifically recognize the porcine complex. Differences between the porcine and human GP IIb-IIIa glycoproteins could partially explain the decreased inhibitory effects of GP IIb/IIIa-antagonists (against the human receptor) in porcine platelets.

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