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  • 1
    Electronic Resource
    Electronic Resource
    Human chondrosarcoma cells stably transfected with a stromelysin (MMP-3) promoter reporter construct provide a method of assessing transcriptional inhibitors (1997)
    Springer
    Inflammation research 46 (1997), S. 159-160 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050157
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cartilage proteoglycan degradation by a mouse transformed macrophage cell line is mediated by macrophage metalloelastase (1999)
    Springer
    Inflammation research 48 (1999), S. 280-288 
    Details
    ISSN: 1420-908X
    Keywords: Key words: Macrophage metalloelastase — Activation — Cartilage degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Objective and Design: Identify and characterize the matrix metalloproteinase responsible for cartilage proteoglycan degradation mediated by a macrophage cell line in a cell culture model that resembles some aspects of rheumatoid pannus.¶Materials or Subjects: Supernatants from the transformed mouse macrophage cell line J774A.1 were used to purify the proteoglycan degrading activity.¶Methods: J774A.1 macrophage culture supernatants were purified by sequential column chromatography and proteins were identified by zymography, western blotting and amino acid sequence analysis. Cartilage degradation was measured using 35S labeled bovine nasal cartilage.¶Results: The cartilage degrading proteolytic activity in the mouse macrophage supernatants proved to be due to two major proteins with approximate molecular masses of 48 kDa and 22 kDa that were identified as macrophage metalloelastase (MME). Incubation of purified MME at 37°C for up to 16 h resulted in the processing of the 48 kDa protein to several novel bands including a previously undescribed protein of ∼25 kDa without accumulation of fully processed 22 kDa protein. A number of proteinases increased the rate of this processing. J774A.1 macrophage metalloelastase degraded cartilage proteoglycan with an efficiency approximately equal to human macrophage metalloelastase (MMP-12) and matrilysin (MMP-7) and twice that of stromelysin-1 (MMP-3).¶Conclusions: These data identify the cartilage proteoglycan degrading metalloproteinase secreted by J774A.1 macrophages in this cell culture model as MME, and describes mechanisms of activation and processing of this enzyme that may play an important role in cartilage degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050460
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition of cartilage degradation in rat collagen-induced arthritis but not adjuvant arthritis by the neutrophil elastase inhibitor MDL 101,146 (1997)
    Springer
    Inflammation research 46 (1997), S. 503-508 
    Details
    ISSN: 1420-908X
    Keywords: Key words: Neutrophil elastase — Adjuvant arthritis — Collagen arthritis — MDL 101,146 — Cartilage degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Objective and Design: The neutrophil elastase inhibitor MDL 101,146 was examined for its anti-arthritic effect and to determine the role of neutrophil elastase in collagen-induced arthritis and adjuvant arthritis.¶Material: The collagen-induced arthritis model was performed in female DA rats immunized on day 0 and 7 with chick type II collagen in Freund's incomplete adjuvant. Adjuvant arthritis was induced in female Lewis rats by an intradermal injection of heat-killed Mycobacterium tuberculosis H37RA.¶Methods: The clinical signs of arthritis were assessed, joint swelling was measured using calipers and bone degradation, new bone proliferation, pannus formation and cartilage degradation were evaluated histologically.¶Results: MDL 101,146 administered orally inhibited the severity of collagen-induced arthritis as measured by a reduction in clinical score and joint swelling. Histological evaluation demonstrated a bone and cartilage sparing effect of MDL 101,146 in the tibio-tarsal joint of animals with collagen-induced arthritis.¶Conclusions: These results suggest that destruction of the joint in collagen-induced arthritis is at least partially due to neutrophil elastase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000110050233
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of muralytic enzyme degradation of streptococcal cell wall on complement activation in vivo and in vitro (1987)
    Springer
    Inflammation 11 (1987), S. 73-85 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Rats given a single intraperitoneal injection of an aqueous suspension of peptidoglycan-polysaccharide polymers derived from group A streptococcal cell wall (PG-APS) develop a severe, chronic, erosive arthritis which resembles human rheumatoid arthritis. The treatment of PG-APS-mjected rats with a single intravenous injection of 0.4 mg of mutanolysin prevents the development of chronic arthritis, even when administration of the enzyme is delayed until severe acute arthritis has developed. PG-APS activates complement both in vitro and in vivo. Digestion of PG-APS with mutanolysin in vitro destroys the ability to activate both the alternate and classical pathways of human serum complement, and the loss of complement activation parallels the extent of PG-APS degradation. There is also a reduction in the in vivo complexing of C3 with PG-APS in the limbs of PG-APS-injected rats treated with mutanolysin, compared to control rats injected with PG-APS and treated with phosphate-buffered saline. This association between loss of arthropathic activity and loss of activation of complement is consistent with the hypothesis that activated complement products form a part of the inflammatory mediators involved in the acute and chronic phases of bacterial cell wall-induced arthritis. This may also partially explain how mutanolysin treatment alleviates cell wall-induced arthritis in the rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00917773
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    Paper (German National Licenses)
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