Bone morphogenetic protein 1 (BMP1)

Bone morphogenetic protein 1 (BMP1) is a secreted metalloprotease distinct from other BMP family members and does not belong to the TGF-β superfamily[1][2][3][4]. Instead, it is the founding member of an astacin-like family of zinc-dependent proteases. BMP1 is responsible for cleaving the C-terminal propeptides of procollagen types I, II, and III, enabling their assembly into mature collagen fibrils, and thus plays a critical role in extracellular matrix formation and tissue morphogenesis[1][3][5][8]. It is also implicated in activation of certain growth factors through proteolytic processing, with effects on bone, cartilage, and wound healing[3]. Mutation or dysregulation of BMP1 activity is linked to disorders of connective tissues such as osteogenesis imperfecta and fibrosis[3][5]. BMP1 and the related enzyme “procollagen C-proteinase” are identical proteins[5]. BMP1 is a recognized research and potential therapeutic target, but currently lacks selective drugs in clinical use[6].

Other names

Procollagen C-proteinaseBMP-1Bone morphogenetic protein-1PCP

Inhibitors suppress BMP1-mediated cleavage of procollagen and extracellular matrix proteins, potentially altering tissue fibrosis and bone formation.