The Structure and Biological Functions of the M12B Metalloproteinase Family

M12B metalloprotease belongs to the MMP protein family, which is zinc-dependent endopeptidases that degrade the extracellular matrix, mainly includes ADAM, ADAMTS and SVMP. M12B has four different functional domains, including a conserved metalloprotease catalytic domain, a class of integrin-like domain, aspecific ADAM_CR domain and a domain rich in cysteine. Different modular structures give M12B protease different functional activities, which are responsible for the shedding of cell surface proteins, ECM degradation and themaintenance of the haemorrhagic activity of snake venom proteins. M12B proteins are involved in different diseaseregulation through different specific functions. This article systematically describes the structural characteristics,functions, related diseases and regulatory mechanisms of different M12B members, and discusses the research progress of medical treatment and drug development.

CSTR: 32200.14.cjcb.2026.06.0014