Cloning of a complementary dna for rabbit proactivator. a metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase

Cloning of a complementary dna for rabbit proactivator. a metalloproteinase that activates... Rabbit proactivator is a neutral metalloproteinase that activates another metalloproteinase, procollagenase, and degrades noncollagenous matrix. We describe the construction of an activator complementary DNA (cDNA) clone, which is 1.9 kb, that selects a 2.1‐kb messenger RNA (mRNA) in Northern blot hybridizations. Nucleic acid sequence studies of the activator cDNA indicate 1) that it encodes protein Mr 53,881, 2) that this protein exhibits ˜80% homology with rat transin, an oncogene‐induced protein with a previously unknown function, and 3) that, in the first 172 residues, it is virtually identical to the rabbit metalloproteinase, stromelysin. Homology between rabbit activator and human skin collagenase is approximately 50%. Activator and collagenase mRNA are coordinately regulated; untreated cultures of rabbit synovial fibroblasts produce low levels of each protein, but addition of phorbol myristate acetate (10–8M) results in an increase in mRNA for both proteins by 2.5–5 hours. Adding all‐trans‐retinoic acid (10–6M) or dexamethasone (10–7M) to phorbol‐stimulated cells coordinately suppresses both activator and collagenase mRNA. Our data suggest the existence of coordinately regulated metalloproteinases that are important in the modulation of connective tissue metabolism. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Arthritis & Rheumatology Wiley

Cloning of a complementary dna for rabbit proactivator. a metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase

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Publisher
Wiley
Copyright
Copyright © 1987 American College of Rheumatology
ISSN
0004-3591
eISSN
1529-0131
DOI
10.1002/art.1780301108
Publisher site
See Article on Publisher Site

Abstract

Rabbit proactivator is a neutral metalloproteinase that activates another metalloproteinase, procollagenase, and degrades noncollagenous matrix. We describe the construction of an activator complementary DNA (cDNA) clone, which is 1.9 kb, that selects a 2.1‐kb messenger RNA (mRNA) in Northern blot hybridizations. Nucleic acid sequence studies of the activator cDNA indicate 1) that it encodes protein Mr 53,881, 2) that this protein exhibits ˜80% homology with rat transin, an oncogene‐induced protein with a previously unknown function, and 3) that, in the first 172 residues, it is virtually identical to the rabbit metalloproteinase, stromelysin. Homology between rabbit activator and human skin collagenase is approximately 50%. Activator and collagenase mRNA are coordinately regulated; untreated cultures of rabbit synovial fibroblasts produce low levels of each protein, but addition of phorbol myristate acetate (10–8M) results in an increase in mRNA for both proteins by 2.5–5 hours. Adding all‐trans‐retinoic acid (10–6M) or dexamethasone (10–7M) to phorbol‐stimulated cells coordinately suppresses both activator and collagenase mRNA. Our data suggest the existence of coordinately regulated metalloproteinases that are important in the modulation of connective tissue metabolism.

Journal

Arthritis & RheumatologyWiley

Published: Nov 1, 1987

References

  • Collagenase production by synovial fibroblasts treated with phorbol myristate acetate
    Brinckerhoff, Brinckerhoff; McMillan, McMillan; Fahey, Fahey; Harris, Harris
  • Induction of collagenase and prostaglandin synthesis in synovial fibroblasts treated with monosodium urate crystals
    McMillan, McMillan; Vater, Vater; Hasselbacher, Hasselbacher; Hahn, Hahn; Harris, Harris
  • Characterization of rabbit genes for synovial cell collagenase
    Fini, Fini; Gross, Gross; Brinckerhoff, Brinckerhoff
  • Collagenase production by cultures containing multinucleated cells derived from synovial fibroblasts
    Brinckerhoff, Brinckerhoff; Harris, Harris
  • Heterogeneity among human collagenases demonstrated by monoclonal antibody that selectively recognizes and inhibits human neutrophil collagenase
    Hasty, Hasty; Hibbs, Hibbs; Kang, Kang; Mainardi, Mainardi

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