Thromb Haemost 1998; 79(03): 609-613
DOI: 10.1055/s-0037-1614954
Review Articles
Schattauer GmbH

Alboaggregins A and B. Structure and Interaction with Human Platelets

Authors

  • Anna M. Kowalska*

    1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
  • Li Tan

    1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
  • John C. Holt

    2   Rhone Poulenc Rorer Research Laboratories, King of Prussia, PA, USA
  • Manling Peng

    1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
  • Jerzy Karczewski

    3   Merck Research Laboratories, West Point, PA, USA
  • Juan J. Calvete

    4   Institut für Reproduktionsmedizin, Tierärztliche Hochschule, Hannover, Germany
  • Stefan Niewiarowski

    1   Departments of Physiology and Biochemistry and Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, USA
Weitere Informationen

Publikationsverlauf

Received 16. Juni 1997

Accepted after revision 05. November 1997

Publikationsdatum:
07. Dezember 2017 (online)

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Summary

Viper venoms contain a variety of platelet binding proteins including those which bind to platelet GPIb/GPIX. Most of these proteins inhibit von Willebrand factor mediated platelet agglutination. Here we report the primary structures of unique members of this family, alboaggregins A and B, isolated from Trimeresurus albolabris, which have the ability to stimulate platelet agglutination and aggregation. Four chains of alboaggregin A and two chains of alboaggregin B share a high degree of homology and all cysteines in both alboaggregins are conserved. Both alboaggregins caused similar agglutination of fixed platelets. Alboaggregin A induced platelet aggregation and release reaction with EC50 = 10 and 30 nM, respectively, which is 20-fold lower than those for alboaggregin B. These observations suggest that the dimeric structure of alboaggregin B is sufficient to mediate its binding to GPIb and induce agglutination of platelets whereas aggregation and release reaction are significantly enhanced by tetrameric structure of alboaggregin A.

* Present address: M. A. Kowalska, Department of Hematology, Children’s Hospital of Philadelphia, Philadelphia, PA, USA