This chapter describes the biochemical, structural, and biological characteristics of the hemorrhagic metalloproteinases present in Bothrops asper venom, mainly BaH1, BaH4, and BaP1. These enzymes belong to the M12 family of zinc-dependent metalloproteinases and are responsible for the local and systemic hemorrhagic effects induced by the venom. BaH1 and BaH4 exhibit high hemorrhagic activity, whereas BaP1 shows a milder effect. These proteins hydrolyze several substrates, including type IV collagen, laminin, and fibronectin—key components of the capillary basement membrane. Their proteolytic action leads to blood vessel degradation, muscle necrosis, inflammation, and blister formation in the skin. Structural studies indicate that BaH1 and BaH4 are 64–69 kDa proteins (class III), while BaP1, at 24 kDa, belongs to class I. These enzymes are inhibited by chelating agents and natural antihemorrhagic proteins found in snake and mammalian sera. Research on these metalloproteinases has enhanced the understanding of the pathogenic mechanisms underlying venom-induced tissue damage and contributed to the development of therapeutic strategies complementary to traditional antivenom treatments.

UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)

Capitulo 208 del libro: Handbook of Proteolytic Enzymes