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  • 1
    ISSN: 1420-908X
    Keywords: Key words: Sephadex beads — Rat — Strain — Airway hyperresponsiveness — Airway inflammation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Objective: The aim of this study was to compare Sephadex G-200 (Sephadex)-induced airway hyperresponsiveness (AHR) and pulmonary eosinophilia among some rat strains.¶Materials: Sprague-Dawley (SD), Brown-Norway (BN), Fischer 344 (Fischer), Lewis and Wistar-Kyoto (WKY) rats were used.¶Methods: Sephadex (0.5 mg/animal) was intravenously administered on days 0, 2 and 5. Measurement of AHR using serotonin and bronchoalveolar lavage (BAL) was performed on day 7.¶Results: The Lewis strain exhibited significant AHR to Sephadex but the BN, Fischer and WKY strains did not. Additionally, the degree of AHR in Lewis rats was smaller than in SD rats throughout the study. Eosinophils in BAL fluid, however, increased in each strain, and the magnitude of the response was BN 〉 Lewis 〉 WKY 〉 Fischer. Both the AHR and pulmonary eosinophilia in Lewis rats were inhibited by dexamethasone (0.1 mg/kg, p.o. × 3).¶Conclusion: These results indicate that the Lewis rat is a useful strain for analysis of the mechanism of Sephadex-induced AHR and airway inflammation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 74 (1987), S. 151-157 
    ISSN: 1432-0533
    Keywords: Autoantibody ; Immunohistochemistry ; Immunoblotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The quadriceps femoris muscles of experimental allergic myositis, in strain 13 guinea pigs immunised with rabbit myosin B fraction, were subjected to histochemical, immunohistochemical and electron microscopic studies. They demonstrated a variety of degenerative changes of muscle fibres, infiltration of lymphocytes and macrophages along with deposition of immunoglobulin G (IgG) and complement factor 3 on the surface of the muscle fibres. One third of the infiltrating cells were macrophages with acid phosphatase activity in the cytoplasm. The serum IgG of the model had an affinity for the surface of normal guinea pig muscle fibres and for thick filaments and other organelles. Its affinity for the heavy and light chains of myosin, actin, troponin T and for other proteins was shown by the immunoblotting method combined with one- and two-dimensional electrophoreses.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 61 (1983), S. 43-51 
    ISSN: 1432-0533
    Keywords: Hereditary motor neuropathy ; Wohlfart ; Kugelberg-Welander syndrome ; Chronic spinal muscular atrophy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Forty cases of chronic hereditary motor neuropathy (CHMN) were divided into five categories according to the distribution of muscle atrophy; they were proximal, facioscapulohumeral, bulbospinal, distal and scapuloperoneal forms. Their clinical features and laboratory data were analysed, and muscle biopsies from 32 of them were studied by histological, histochemical and electron microscopical methods. An attempt at quantitative assessment of the histological changes was also made. All muscle biopsies showed a mixture of neurogenic and ‘myopathic’ changes in varying proportions. They showed more ‘myopathic’ changes than Werdnig-Hoffmann's disease, amyotrophic lateral sclerosis and other neurogenic atrophies except Charcot-Marie-Tooth disease. There was marked variation in the average number of atrophied muscle fibers contained in grouped atrophy. Frequently, deranged internal structure of the muscle fibres was revealed both by histochemical and electron microscopical methods. Based on the evidence of heterogeneity of CHMN in respect of genetics, clinical features and histological changes, it was speculated that CHMN represents a group of diseases which involves primarily different parts of the motor units.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 81 (1990), S. 223-227 
    ISSN: 1432-0533
    Keywords: Myositis ; Toxoplasmosis ; Macrophages ; T lymphocytes ; Major histocompatibility complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The occurrence is reported of acute myositis in a man with meningoencephalitis due to toxoplasmosis. The ultrastructure and immunohistochemistry of a muscle biopsy of the patient were investigated. Toxoplasma organisms were not found in the muscle biopsy. The perivascular inflammatory cells in the muscle were mainly CD4+ T cells and the inflammatory cells in and around the muscle fibres were chiefly macrophages. Expression of major histocompatibility complex class I and II antigens was observed in the infiltrating cells and endothelial cells of the blood vessels. A small proportion of the infiltrating cells expressed interferon-γ. A possible role of the immune mechanism in the evolution of myositis is discussed.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 176 (1991), S. 792-797 
    ISSN: 0006-291X
    Keywords: [abr] FGF; fibroblast growth factor ; [abr] HB-GAM; heparin-binding growth-associated molecule ; [abr] MK; midkine ; [abr] Rl-HB; retinoic acid-induced heparin binding protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Cell Differentiation and Development 27 (1989), S. 119 
    ISSN: 0922-3371
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    BBA - Protein Structure 446 (1976), S. 321-324 
    ISSN: 0005-2795
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0920-9964
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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