The biologic activity of aggretin/rhodocytin, a snake venom C-type lectin protein (snaclec)

Abstract

Aggretin (or rhodocytin), an ab-heterodimeric snake venom C-type lectin (snaclec), was originally found to activate platelets through specific binding to integrin α2β1, leading to activation of phospholipase C, platelet activation and subsequent thrombocytopenia in vivo. Recent reports suggest that the CLEC-2 receptor, involving the Src, Syk and PLCg pathway is critical for mediating platelet activation by aggretin. In this review, we discuss the use of aggretin to explore the role of α2β1 and/or CLEC-2 in different cell types, namely (i) induction of platelet aggregation (α2β1 or CLEC-2), (ii) induction of angiogenesis in endothelial cells (α2β1), (iii) promotion of proliferation, migration of smooth muscle cells and keratinocytes, and induction of cytokine release through CLEC-2 ligation, and also possible signal transduction pathways involving ligation of integrin α2β1 or CLEC-2.