Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling.

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  • Author(s): Prockop DJ;Prockop DJ; Sieron AL; Li SW
  • Source:
    Matrix biology : journal of the International Society for Matrix Biology [Matrix Biol] 1998 Feb; Vol. 16 (7), pp. 399-408.
  • Publication Type:
    Journal Article; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: Netherlands NLM ID: 9432592 Publication Model: Print Cited Medium: Print ISSN: 0945-053X (Print) Linking ISSN: 0945053X NLM ISO Abbreviation: Matrix Biol Subsets: MEDLINE
    • Publication Information:
      Publication: Amsterdam : Elsevier
      Original Publication: Stuttgart ; New York : Fischer, c1994-
    • Subject Terms:
      Signal Transduction*; Bone Morphogenetic Proteins/*metabolism ; Metalloendopeptidases/*metabolism ; Procollagen/*metabolism ; Procollagen N-Endopeptidase/*metabolism; Animals ; Bone Morphogenetic Protein 1 ; Humans
    • Abstract:
      As soon as procollagen precursors of fibrillar collagens were discovered in the early 1970s, it became apparent that connective tissues must contain proteolytic activities that cleave the N-propeptides and the C-propeptides from procollagens. Isolation and characterization of the enzymic activities, however, proved to be unexpectedly difficult. Both proteinases are large and are synthesized in several different forms with polypeptide chains ranging in size from 70 kDa to about 130 kDa. The N-proteinase has the unusual property of cleaving the N-propeptides from type I and type II procollagens if the proteins are in a native conformation, but not if the proteins are partially unfolded so that the N-telopeptides are no longer in a hair-pin configuration. The C-proteinase specifically cleaves native and denatured types I, II and III procollagens. It also specifically cleaves a precursor of lysyl oxidase and laminin 5. Both enzymes and their variants have structures that place them in a large and expanding super-family of over 200 zinc-binding metalloproteinases. The larger of two forms of the N-proteinase contains an RGD sequence for binding through integrins and properdin repeats similar to those found in thrombospondin. The shorter 70 kDa form of the C-proteinase is identical to the protein that was previously identified as bone morphogenic protein-1. Both the 70 kDa C-proteinase and two larger forms are homologous to proteins that are expressed early in development in a variety of organisms, including Drosophila, sea urchin, and fish. Therefore, the data suggest that both the N- and C-proteinases have important biological functions in addition to the roles in the processing of procollagens.
    • Number of References:
      67
    • Accession Number:
      0 (Bone Morphogenetic Proteins)
      0 (Procollagen)
      EC 3.4.24.- (Metalloendopeptidases)
      EC 3.4.24.14 (Procollagen N-Endopeptidase)
      EC 3.4.24.19 (BMP1 protein, human)
      EC 3.4.24.19 (Bone Morphogenetic Protein 1)
    • Publication Date:
      Date Created: 19980403 Date Completed: 19980514 Latest Revision: 20220224
    • Publication Date:
      20240513
    • Accession Number:
      10.1016/s0945-053x(98)90013-0
    • Accession Number:
      9524360