The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. Academic Article uri icon

abstract

  • 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.

published proceedings

  • Proc Natl Acad Sci U S A

altmetric score

  • 12

author list (cited authors)

  • Li, S. W., Sieron, A. L., Fertala, A., Hojima, Y., Arnold, W. V., & Prockop, D. J.

citation count

  • 183

complete list of authors

  • Li, SW||Sieron, AL||Fertala, A||Hojima, Y||Arnold, WV||Prockop, DJ

publication date

  • May 1996