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  • 1
    ISSN: 1437-160X
    Schlagwort(e): Synovium ; Arthritis ; Collagenase ; Proteinases ; Inhibitor
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary During 5 days of culture, explants of normal rabbit synovium produced no active collagenase, negligible latent collagenase, but significant levels of free collagenase inhibitor. Synovium from joints exhibiting a proliferative arthritis produced greatly elevated levels of collagenase; the appearance of active enzyme in the medium during the second day of culture was associated with the disappearance of free inhibitor. Enzyme levels in the media correlated well with the arthritic status of joints, when explants were prepared up to 10 weeks after the induction of the model arthritis. Synovium from the contralateral joints of rabbits with unilaterally induced arthritis produced no active collagenase, but approximately one-third as much latent collagenase as found with arthritic joints. Enzymatic activities against gelatin and cartilage proteoglycan substrates were demonstrated in synovial culture media in addition to collagenolytic activity. Gel filtration showed that these activities were not due to a single enzyme, and further characterisation confirmed that the enzymes were metalloproteinases. The results are considered in the light of published data, and the involvement of metalloproteinases and their specific inhibitor in the development of arthritic lesions is discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1437-160X
    Schlagwort(e): Cartilage ; Arthritis ; Collagenase ; Proteinase ; Inhibitor
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary During the development of proliferative arthritis in the knee joints of rabbits, there was a large increase in the ability of articular cartilage explants to produce latent collagenase in culture. In parallel, the normally high levels of collagenase inhibitor produced by cartilage in culture fell, but active collagenase was never detectable. Characterisation of the collagenase and other proteinase activities produced by rabbit articular cartilage in culture showed that two activities could be separated by gel filtration, one with activities on gelatin and cartilage proteoglycan and the other degrading collagen. Under the conditions employed in this paper no resolution of the gelatin and proteoglycan activities could be achieved. All the activities were in a latent form, activated by 4-aminophenylmercuric acetate (APMA), and inhibited by 1,10-phenanthroline or EDTA, but not by di-isopropylfluorophosphate (DFP), indicating that they are metalloproteinases. Characterization of the collagenase inhibitor showed a single peak of activity of apparent molecular weight of 28,000 on gel filtration. The inhibitor was sensitive to APMA and also inhibited other rabbit metalloproteinases, analogous to the system described for rabbit bone. The physiological significance of the synthesis by articular cartilage of proteinases that destroy connective tissue macromolecules and the presence of an enzyme-inhibitor control system is discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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