Alboaggregins A and B. Structure and interaction with human platelets.


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.


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@article{Kowalska1998AlboaggreginsAA, title={Alboaggregins A and B. Structure and interaction with human platelets.}, author={Maria Anna Kowalska and L Tan and John M C Holt and Mindy Peng and Jan Kazimierz Karczewski and Juan J Calvete and Stefan Niewiarowski}, journal={Thrombosis and haemostasis}, year={1998}, volume={79 3}, pages={609-13} }