Thromb Haemost 2002; 87(04): 692-698
DOI: 10.1055/s-0037-1613067
Review Article
Schattauer GmbH

Alboluxin, a Snake C-type Lectin from Trimeresurus albolabris Venom is a Potent Platelet Agonist acting via GPIb and GPVI

Xiao-Yan Du
1   Theodor Kocher Institute, University of Berne, Berne, Switzerland
,
Edith Magnenat
2   Serono Pharmaceutical Research Institute SA, Plan-les-Ouates, Geneva, Switzerland
,
Timothy N. C. Wells
2   Serono Pharmaceutical Research Institute SA, Plan-les-Ouates, Geneva, Switzerland
,
Kenneth J. Clemetson
1   Theodor Kocher Institute, University of Berne, Berne, Switzerland
› Author Affiliations
Further Information

Publication History

Received 10 September 2001

Accepted after resubmission 28 December 2001

Publication Date:
08 December 2017 (online)

Summary

Alboluxin, a potent platelet activator, was purified from Trimeresurus albolabris venom with a mass of 120 kDa non-reduced and, after reduction, subunits of 17 and 24 kDa. Alboluxin induced a tyrosine phosphorylation profile in platelets that resembles those produced by collagen and convulxin, involving the time dependent tyrosine phosphorylation of Fc receptor γ chain (Fcγ), phospholipase Cγ2 (PLCγ2), LAT and p72SYK. Antibodies against both GPIb and GPVI inhibited platelet aggregation induced by alboluxin, whereas antibodies against α2β1 had no effect. Inhibition of αIIbβ3 reduced the aggregation response to alboluxin, as well as tyrosine phosphorylation of platelet proteins, showing that activation of αIIbβ3 and binding of fibrinogen are involved in alboluxin-induced platelet aggregation and it is not simply agglutination. N-terminal sequence data from the β-subunit of alboluxin indicates that it belongs to the snake C-type lectin family. The C-type lectin subunits are larger than usual possibly due to post-translational modifications such as glycosylation. Alboluxin is a hexameric (αβ)3 snake C-type lectin which activates platelets via both GPIb and GPVI.

 
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