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

Abstract

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.

Statistics

0102030'00'02'04'06'08'10'12'14'16
Citations per Year

58 Citations

Semantic Scholar estimates that this publication has 58 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@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} }