STUDIES WITH A MURINE MONOCLONAL-ANTIBODY THAT ABOLISHES RISTOCETIN-INDUCED BINDING OF VONWILLEBRAND-FACTOR TO PLATELETS - ADDITIONAL EVIDENCE IN SUPPORT OF GPIB AS A PLATELET RECEPTOR FOR VONWILLEBRAND-FACTOR

Authors:
  • BCBS COLLER
    BS COLLER
  • EPEI PEERSCHKE
    EI PEERSCHKE
  • LSLE SCUDDER
    LE SCUDDER
  • CSCA SULLIVAN
    CA SULLIVAN
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  • 1 January 1983
    • journal article
    • research article
    • Vol. 61  (1) , 99-110
    • PMID:6336654
Abstract
A murine monoclonal antibody directed at or near a platelet membrane receptor for the von Willebrand factor was produced by the hybridoma technique. Purified F(ab'')2 fragments and/or intact antibody completely blocked the agglutination of platelets induced by both ristocetin and bovine von Willebrand factor and the binding of von Willebrand factor antigen to platelets. The antibody also decreased platelet retention, prevented the reduction in platelet electrophoretic mobility caused by bovine von Willebrand factor, and decreased the serum prothrombin time. Radiolabeled F(ab'')2 fragments bound to .apprx. 2.5 .times. 104 sites on normal platelets with high affinity (Kd .apprx. 1.5 .times. 10-8 M); there was no binding to platelets from 2 patients with the Bernard-Soulier syndrome. Immunoprecipitation and affinity chromatography studies indicated that the antibody binds to glycoprotein [GP] lb at a site contained on the externally oriented portion of the GPlb.alpha. chain (glycocalicin). An unidentified MW .apprx. 20,000 [dalton] molecule labeled by periodate/NaB3H4 coprecipitated and copurified with GPlb.