Alboaggregins A and B. Structure and Interaction with Human Platelets

Anna M. Kowalska; Li Tan; John C. Holt; Manling Peng; Jerzy Karczewski; Juan J. Calvete; Stefan Niewiarowski

doi:10.1055/s-0037-1614954

Thrombosis and Haemostasis, Table of Contents

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^*

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

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

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

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

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

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

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

Abstract

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.

Full Text

References

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