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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 74 (1987), S. 158-162 
    ISSN: 1432-0533
    Keywords: Animal model ; Polymyositis ; Myosin B ; Myosin ; Microsome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Of 32 guinea pigs (Hartley and strain 13), 20 were immunised with whole muscle homogenate, microsome or myosin B fraction of rabbit skeletal muscle with Freund's complete adjuvant (FCA); the purified myosin fraction was also used as an antigen in four animals at a concentration lower than other antigens; four were injected with normal saline and FCA; other four had no injection. Five histological changes, namely necrosis, phagocytosis, central nuclei, inflammation and vacuoles, in the quadriceps femoris muscle were compared by quantitative analysis. The group immunised with myosin B fraction showed necrosis, phagocytosis and inflammation more frequently than those immunised with other preparations (p〈0.05). The changes were more frequent in the strain 13 than in Hartley (p〈0.05).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Myositis ; Animal model ; Immunoglobulin G ; Complement ; Class II antigen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Experimental allergic myositis (EAM) was produced in SJL/J mice by inoculation with the myosin B fraction of the rabbit skeletal muscle, and the pathological changes were quantified. The myosin B fraction contains actin, myosin, tropomyosin and many other proteins, and has been known to induce severe EAM in guinea pigs. In the present model, macrophages and CD4+ lymphocytes predominated among the infiltrating cells. On the surface of muscle fibers and in the regions of cell infiltration deposition of the immunoglobulin G (IgG) and complement factor 3 was observed. EAM was transferred to normal mice by injecting the serum IgG of EAM. Depleting the recipients of complement before the transfer resulted in less-severe pathological changes. Morphologically, the EAM IgG showed an affinity for the nuclei, myofilaments, sarcolemma and blood vessels of mouse skeletal muscle. Biochemically EAM IgG contained antibodies against myosin, actin, troponin, M protein and other muscle proteins. These results indicated that IgG and complement play important roles in this model.
    Type of Medium: Electronic Resource
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