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Thromb Haemost 1998; 79(03): 609-613
DOI: 10.1055/s-0037-1614954
Review Articles
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Alboaggregins A and B. Structure and Interaction with Human Platelets

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
› Author Affiliations
Further Information

Publication History

Received 16 June 1997

Accepted after revision 05 November 1997

Publication Date:
07 December 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


 

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