Structural highlights
Function
VM1LA_BOTLC Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM.[1] [2]
References
- ↑ Bello CA, Hermogenes AL, Magalhaes A, Veiga SS, Gremski LH, Richardson M, Sanchez EF. Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom. Biochimie. 2006 Feb;88(2):189-200. Epub 2005 Aug 19. PMID:16139412 doi:https://dx.doi.org/10.1016/j.biochi.2005.07.008
- ↑ Gremski LH, Chaim OM, Paludo KS, Sade YB, Otuki MF, Richardson M, Gremski W, Sanchez EF, Veiga SS. Cytotoxic, thrombolytic and edematogenic activities of leucurolysin-a, a metalloproteinase from Bothrops leucurus snake venom. Toxicon. 2007 Jul;50(1):120-34. Epub 2007 Mar 14. PMID:17482228 doi:https://dx.doi.org/10.1016/j.toxicon.2007.03.002
