Bone morphogenic protein-1 (BMP-1) was originally identified as one of several BMPs that induced new bone formation when implanted into ectopic sites in rodents. BMP-1, however, differed from other BMPs in that it its structure was not similar to transforming growth factor beta. Instead, it had a large domain homologous to a metalloendopeptidase isolated from crayfish, an epidermal growth-factor-like domain, and three regions of internal sequence homology referred to as CUB domains. Therefore, BMP-1 was a member of the "astacin families" of zinc-requiring endopeptidases. Many astacins have been shown to play critical roles in embryonic hatching, dorsal/ventral patterning, and early developmental decisions. Here, we have obtained amino acid sequences and isolated cDNA clones for procollagen C-proteinase (EC 3.4.24.19), an enzyme that is essential for the processing of procollagens to fibrillar collagens. The results demonstrate that procollagen C-proteinase is identical to BMP-1.
Proc Natl Acad Sci U S A
- Collagen
- Metalloendopeptidases
- Cloning, Molecular
- Rodentia
- Bone Morphogenetic Protein 1
- Molecular Sequence Data
- Bone Morphogenetic Proteins
- DNA, Complementary
- Animals
- Procollagen
- Humans
- Protein Processing, Post-Translational
- Growth Substances
- Proteins
- Chick Embryo
- DNA Primers
- Base Sequence
- Astacoidea
- Amino Acid Sequence
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