hemorrhagic protease that acts as a potent inhibitor of collagen-induced adhesion by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. Cleaves at Leu-|-Met bonds (PubMed:11368322). Disintegrin alternagin-C: potent inhibitor of the collagen binding to alpha-2/beta-1 (ITGA2/ITGB1) integrin. Has a chemotactic activity on neutrophils and this effect involves actin cytoskeleton rearrangement, FAK, PI3-kinase and Erk-2 activities. Induces endothelial cell proliferation, and these effects are mediated at least in part by an increased expression of vascular endothelial growth factor (VEGF). In injured muscles, reduces both MMP-2 mRNA and gelatinolytic activity, suggesting that it changes the overall balance of extracellular matrix protein turnover during muscle regeneration. In low concentrations, induces formation of new vessels and up-regulates the expression of VEGF receptor 2 (KDR) without affecting VEGF receptor 1 (FLT1) expression. In high concentrations, strongly inhibits angiogenesis, and the expression of both receptors is down-regulated. Has very low plasma clotting activity. Binds 1 zinc ion per subunit. Inhibited by EDTA. Monomer. Expressed by the venom gland. The N-terminus of alternagin is blocked. does not present any fibrinogen-clotting activity and does not bind to alpha-IIb/beta-3 (ITGA2B/ITGB3), alpha-1/beta-1 (ITGA1/ITGB1), alpha-5/beta-1 (ITGA5/ITGB1), alpha-4/beta-1 (ITGA4/ITGB1), alpha-V/beta-3 (ITGAV/ITGB3) and alpha-9/beta-1 (ITGA9/ITGB1) integrins. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIb sub-subfamily.