BMP-1

Bone morphogenetic protein 1 (BMP1), also known as procollagen Cproteinase (PCP), is a zinc protease of the astacin family. BMP1/ PCP plays a key role in formation of extracellular matrix (ECM) by converting precursor proteins into their mature and functional forms. The precursor proteins identified as substrates for BMP1/ PCP include collagens, biglycan, laminin 5, dentin matrix protein1, and lysyl oxidase. There are six alternatively spliced forms known to be derived from the BMP 1 gene, and isoform 1 consisting of residues 1 to 730 was expressed. The secreted and purified protein does not contain the signal peptide (amino acid residues 122) and pro domain (residues 23-120), but contain protease (residues 121-321), CUB I (residues 322-434), CUB II (residues 435-546), EGFlike (residues 547-588) and CUB III (residues 591-703) domains. The pro domain is apparently cleaved by a furinlike proprotein convertase. The purified BMP1/ PCP is an active protease and its peptidase activity can be determined as described above. The purified BMP1/ PCP is predicted to possess procollagen C proteinase activity because it contains the minimal domain structure required.