Releasing or expression modulating mediator involved in hemostasis by Berythractivase and Jararhagin (SVMPs).

PIII snake venom metalloproteases (SVMPs) are structurally related to ADAMs (a disintegrin and metalloprotease human family of proteins). Berythractivase and Jararhagin are PIII SVMPs with 69% homology with different hemostatic properties. In order to clarify these differences and further characterize the biological effects of these proteins, we compared the effect of both proteases on human umbilical vein endothelial cell (HUVEC) for evaluating the release and modulation of coagulation and fibrinolysis mechanisms as well as the expression of their correlated genes. We found that both proteins increase the von Willebrand factor liberation, but did not modulate gene expression. Berythractivase, differently from Jararhagin increased the expression of tissue factor. Our results showed that both SVMPs (Berythractivase and Jararhagin) activate HUVEC releasing or modulating mediators involved in hemostasis. Meanwhile, we can suggest through the up-regulation of TF gene that the studied SVMP acts in a specific manner, suggesting that Jararhagin has preferentially a local action, while Berythractivase can be assumed as a systemic pro-coagulant protein with activity on the surface of HUVECs.