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  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Key words: Macrophage metalloelastase — Activation — Cartilage degradation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s000110050460
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  • 2
    Digitale Medien
    Digitale Medien
    Congenital complete atrioventricular block in an infant with Miller-Dieker syndrome (1994)
    Springer
    Pediatric cardiology 15 (1994), S. 209-209 
    Details
    ISSN: 1432-1971
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00800679
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  • 3
    Digitale Medien
    Digitale Medien
    Clinical heterogeneity in the tricho-dento-osseous syndrome (1983)
    Springer
    Human genetics 〈Berlin〉 64 (1983), S. 116-121 
    Details
    ISSN: 1432-1203
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary The tricho-dento-osseous syndrome (TDO syndrome) involves morphologic abnormalities of hair, teeth, and skeleton. Clinical findings of the TDO syndrome are excessively curly (fuzzy) hair, enamel hypoplasia, and skeletal findings of a generalized pattern of osseous sclerosis. We report an autosomal dominant syndrome with similar hair and teeth morphology, but with a skeletal dysplasia consisting of sclerosis and thickening of the calvarium with long bones that show subtle undertubulation but no sclerosis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00327105
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  • 4
    Digitale Medien
    Digitale Medien
    Genomic organization and chromosomal localization of mouse proteinase 3 (Myeloblastin) (1999)
    Springer
    Mammalian genome 10 (1999), S. 210-212 
    Details
    ISSN: 1432-1777
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract. Proteinase 3 (PR3), is a matrix-degrading serine proteinase expressed in different hematopoietic cell lineages. The PR3 protein appears to regulate the myeloid differentiation and was found to be the autoantigen associated with Wegener granulomatosis. We have isolated and characterized the gene for mouse PR3 (mPR3) and determined its chromosomal location. The gene has been localized to Chromosome (Chr) 10. Comparison of mouse PR3 genomic structure with that of its human counterpart indicates that: 1) the mPR3 gene spans 7 kb organized in 5 exons and 4 introns, 2) the codons of His-Asp-Ser of the catalytic site are conserved and spread out over different exons, similar to the human gene, and 3) the gene product encodes a pre-proform of the protein. Knowledge of the structure and chromosomal location of the mPR3 gene may help better the understanding of the temporal and cell-specific expression of mouse PR3.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s003359900974
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