Bone morphogenetic protein 1 (BMP1) is a member of the astacin family (MEROPS family M12A) of metalloproteinases which plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins []. During ECM formation, this protein is involved in the cleavage of the C-terminal propeptides of procollagen I, II and III and the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers [, , ]. BMP1 participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair[, ]. BMP1 is essential for human type I collagen fibrillogenesis []and induces cartilage and bone formation [, ]. Additional BMP1 substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation [].
This entry includes the zinc-dependent metalloprotease domain of BMP1 and tolloid-like proteins. Procollagen C-peptidase (BMP1, Bone morphogenetic protein 1; MEROPS identifier M12.005) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The Drosophila protein tolloid (MEROPS identifier M12.010) and its Xenopus homologue xolloid (MEROPS identifier M12.015) cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning[, , ].
