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. 1978 May 1;171(2):493–496. doi: 10.1042/bj1710493

Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.

A Sellers, J J Reynolds, M C Meikle
PMCID: PMC1183981  PMID: 207263

Abstract

Rabbit bones in culture produce specific collagenase and neutral metallo-proteinase activity in latent forms that can be activated by either 4-aminophenylmercuric acetate or trypsin. Latent neutral metallo-proteinase activity was resolved by gel filtration into two enzymes, distinct from collagenase, that degrade gelatin and cartilage proteoglycans.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burleigh M. C., Werb Z., Reynolds J. J. Evidence that species specificity and rate of collagen degradation are properties of collagen, not collagenase. Biochim Biophys Acta. 1977 Sep 27;494(1):198–208. doi: 10.1016/0005-2795(77)90148-9. [DOI] [PubMed] [Google Scholar]
  2. Dingle J. T., Blow A. M., Barrett A. J., Martin P. E. Proteoglycan-degrading enzymes. A radiochemical assay method and the detection of a new enzyme cathepsin F. Biochem J. 1977 Dec 1;167(3):775–785. doi: 10.1042/bj1670775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Harris E. D., Jr, Krane S. M. An endopeptidase from rheumatoid synovial tissue culture. Biochim Biophys Acta. 1972 Feb 28;258(2):566–576. doi: 10.1016/0005-2744(72)90249-5. [DOI] [PubMed] [Google Scholar]
  4. Murphy G., Cartwright E. C., Sellers A., Reynolds J. J. The detection and characterisation of collagenase inhibitors from rabbit tissues in culture. Biochim Biophys Acta. 1977 Aug 11;483(2):493–498. doi: 10.1016/0005-2744(77)90080-8. [DOI] [PubMed] [Google Scholar]
  5. Reynolds J. J., Murphy G., Sellers A., Cartwright E. A new factor that may control collagen resorption. Lancet. 1977 Aug 13;2(8033):333–335. doi: 10.1016/s0140-6736(77)91490-8. [DOI] [PubMed] [Google Scholar]
  6. Sapolsky A. I., Keiser H., Howell D. S., Woessner J. F., Jr Metalloproteases of human articular cartilage that digest cartilage proteoglycan at neutral and acid pH. J Clin Invest. 1976 Oct;58(4):1030–1041. doi: 10.1172/JCI108526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Sellers A., Cartwright E., Murphy G., Reynolds J. J. Evidence that latent collagenases are enzyme-inhibitor complexes. Biochem J. 1977 May 1;163(2):303–307. doi: 10.1042/bj1630303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Sellers A., Reynolds J. J. Identification and partial characterization of an inhibitor of collagenase from rabbit bone. Biochem J. 1977 Nov 1;167(2):353–360. doi: 10.1042/bj1670353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Werb Z., Burleigh M. C., Barrett A. J., Starkey P. M. The interaction of alpha2-macroglobulin with proteinases. Binding and inhibition of mammalian collagenases and other metal proteinases. Biochem J. 1974 May;139(2):359–368. doi: 10.1042/bj1390359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Werb Z., Reynolds J. J. Immunochemical studies with a specific antiserum to rabbit fibroblast collagenase. Biochem J. 1975 Dec;151(3):655–663. doi: 10.1042/bj1510655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Werb Z., Reynolds J. J. Stimulation by endocytosis of the secretion of collagenase and neutral proteinase from rabbit synovial fibroblasts. J Exp Med. 1974 Dec 1;140(6):1482–1497. doi: 10.1084/jem.140.6.1482. [DOI] [PMC free article] [PubMed] [Google Scholar]

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