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描述:
Bone morphogenetic protein 1 (BMP-1), also known as procollagen C-proteinase (PCP), is a
zinc protease of the astacin family. BMP-1/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 BMP-1/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 1-
22) 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 furin-like proprotein convertase. The
purified BMP-1/PCP is an active protease and its peptidase activity can be determined as
described above. The purified BMP-1/PCP is predicted to possess procollagen C-proteinase
activity because it contains the minimal domain structure required.
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