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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 352 (1994), S. 216-218 
    ISSN: 0014-5793
    Keywords: Matrix metalloproteinase ; Serine proteinase ; Tenascin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Modern rheumatology 10 (2000), S. 121-128 
    ISSN: 1439-7609
    Keywords: Key words Rheumatoid arthritis ; Osteoarthritis ; Matrix metalloproteinase ; A disintegrin and metalloproteinase ; Joint destruction ; Matrix degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Progressive degradation of the extracellular matrix (ECM) of articular cartilage and bone by enhanced activities of proteinases is an essential step for joint destruction in rheumatoid arthritis (RA) and osteoarthritis (OA). Among the proteinases, matrix-degrading metalloproteinases play a key role in joint destruction. Recent studies have indicated that these metalloproteinases comprise members of the matrix metalloproteinase (MMP) and a disintegrin and metalloproteinase (ADAM) gene families. The MMP family is composed of 19 different members and classified into five subgroups of collagenases, gelatinases, stromelysins, membrane-type MMPs, and other MMPs. They have the ability to digest almost all ECM components in human tissues when they act in concert. Their prospective roles in RA and OA joint destruction have been well established. On the other hand, the ADAM family members are classified into ADAM metalloproteinases and catalytically inactive nonproteolytic homologues. The ADAM metalloproteinases contain ADAM with a transmembrane domain (membrane-type ADAM) and ADAM with thrombospondin motifs (ADAMTS). Although members in both groups are known to degrade ECM components, ADAMTS species may be especially important for the aggrecan (cartilage proteoglycan) degradation of articular cartilage in RA and OA, since aggrecanases-1 and -2 are included in this group. This review outlines the characters of the MMP and ADAM gene family members and their roles in joint destruction in RA and OA.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2307
    Keywords: Osteosarcoma ; Invasion ; Metastasis ; Matrix metalloproteinase ; Tumour necrosis factor α
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have examined the correlation between matrix metalloproteinase (MMP) expression and metastatic properties of a low metastatic osteosarcoma cell line, osteosarcoma takase (OST), under stimulation by tumour necrosis factor α (TNFα). In vivo, OST cells exhibited significantly increased colonization in the lungs of nude mice in a dose-dependent manner when they were treated by TNFα prior to injection. In vitro, TNFα enhanced tumour cell invasion through the reconstituted basement membrane in a transwell chamber up to 2.5-fold. Gelatin zymography and sandwich enzyme immunoassays demonstrated marked production of MMP-9 [92-kDa gelatinase/type IV collagenase (gelatinase B)] but not MMP-2 [72-kDa gelatinase/type IV collagenase (gelatinase A)], MMP-3 (stromelysin-1) or MMP-7 (matrilysin). Motility of the tumour cells and adhesion to cultured endothelial cells were slightly increased by the TNFα treatment up to 1.6-fold and 1.4-fold, respectively, while the growth rate was decreased. These results suggest that upregulation of MMP-9 together with enhanced motility and endothelial adhesion contribute to the increased metastatic ability of OST cells induced by TNFα treatment.
    Type of Medium: Electronic Resource
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