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

author list (cited authors)
Li, S. W., Sieron, A. L., Fertala, A., Hojima, Y., Arnold, W. V., & Prockop, D. J.
publication date
1996
keywords
  • 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
altmetric score

12.0

citation count

170