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  • 1
    Electronic Resource
    Electronic Resource
    Immunohistochemical localisation of terminal complement component C9 in experimental allergic encephalomyelitis (1989)
    Springer
    Acta neuropathologica 79 (1989), S. 78-85 
    Details
    ISSN: 1432-0533
    Keywords: Complement component C9 ; Experimental allergic encephalomyelitis ; Demyelination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The deposition of terminal complement component C9 within the central nervous system (CNS) has been studied immunohistochemically in three models of experimental allergic encephalomyelitis (EAE) in the rat; inflammatory EAE induced by the passive transfer of myelin basic protein-specific T cells (tEAE), antibody-mediated, demyelinating tEAE and a subacute/chronic model induced by active immunisation with guinea pig spinal cord tissue in adjuvant. Two distinct patterns of C9 reactivity were observed, a diffuse staining of the tissue adjacent to inflammatory lesions, similar to that seen for other extra-vasculated serum proteins, and also granular, sometimes fibrillar C9 deposits around some inflammed vessels and in areas of active demyelination. The latter staining pattern was most pronounced in animals with acute antibody-mediated demyelinating tEAE, in which extensive, but transient, subpial and perivascular granular deposits of C9 were associated with regions of acute demyelination. A similar pattern of granular C9 reactivity was also associated with demyelinating lesions in animals with actively induced chronic progressive EAE. However, these C9 deposits were not observed in rats with purely inflammatory, clinically mild tEAE, although C9 deposition was occasionally observed around a small number of inflammed vessels in animals with hyperacute, lethal tEAE. These observations demonstrate that deposition of C9, the major component of the cytolytic membrane attack complex, in EAE is related to myelin injury rather than CNS inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00308961
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  • 2
    Electronic Resource
    Electronic Resource
    Experimental allergic encephalomyelitis: the balance between encephalitogenic T lymphocytes and demyelinating antibodies determines size and structure of demyelinated lesions (1988)
    Springer
    Acta neuropathologica 75 (1988), S. 566-576 
    Details
    ISSN: 1432-0533
    Keywords: Experimental allergic encephalomyelitis ; Demyelination ; Myelin/oligodendroglia glycoprotein ; T cells ; Antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effect of a circulating monoclonal antibody recognizing an antigen located on the surface of myelin sheaths (myelin/oligodendroglia glycoprotein, MOG) on clinical and histopathological expression of experimental allergic encephalomyelitis (EAE) was tested in a model of EAE passively transferred by monospecific T lymphocytes. Intravenous injection of anti-MOG antibody at the onset of the disease massively augmented clinical impairment as well as primary demyelination. The structure of the CNS lesions depended on the balance between encephalitogenic T cells and anti-MOG antibody: when EAE was induced with high numbers of T cells, circulating anti-MOG antibody resulted in ubiquitous perivenous demyelination in the spinal cord and medulla oblongata. On the contrary, focal confluent demyelinated lesions were observed in animals injected with low numbers of T cells (even as few as 104) and anti-MOG antibody. Our studies, thus, indicate that the formation of inflammatory demyelinating lesions may be due to a synergistic action of cellular and humoral immune mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00686201
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  • 3
    Electronic Resource
    Electronic Resource
    Peripheral Nervous System Myelin Assembly In Vitro: Perturbation by the Ionophore Monensin (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 41 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Sciatic nerves from 13-day-old rats were incubated in vitro with [35S]methionine in the presence or absence of 0.22 μM monensin and total paniculate and myelin fractions prepared. The total particulate was further subfractionated by continuous density gradient centrifugation, after which the maximal specific activities of three marker enzymes, 2′,3′-cyclic nucleotide phospho-diesterase (myelin), 5′-nucleotidase (plasma membrane), and cerebroside sulphotransferase were recovered at 0.72, 0.82, and 0.92 M sucrose, respectively. The radiolabelled proteins present in the gradient subtractions were analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography, and bands corresponding to the P0 and myelin basic proteins were identified by co-migration with unlabelled myelin marker proteins on both one-dimensional SDS-PAGE and two-dimensional nonequilibrium isoelectric focussing/SDS-PAGE systems. Following a 90-min incubation with [35S]methionine, newly synthesized myelin basic proteins were recovered in fractions between 0.5 and 0.7 M sucrose; this distribution was unaltered by monensin. In contrast, the distribution of newly synthesized P0 protein across the gradients was influenced by monensin: a bimodal distribution across the control gradients with peaks of recovery of 0.60 and 0.82 M sucrose was altered to give a single peak at an intermediate density of 0.72 M sucrose. The total proportions of newly synthesized P0 and myelin basic proteins (MBP) present across the entire gradients were calculated from the fluorograms, and the ratio was found to be 2.8 P0: (LBP + SBP), in both the presence and absence of the ionophore. However, only 70% and 50% of the control levels of MBP and P0 were recovered with a purified myelin fraction after incubation with monensin. The results are discussed with reference to different intracellular transport processes for the P0 glycoprotein and the MBP within the Schwann cell, and also to the differential compartmentation of the sites of synthesis and membrane export within the Golgi body.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb04759.x
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  • 4
    Electronic Resource
    Electronic Resource
    Conservation of the Carboxyl Terminal Epitope of Myelin Proteolipid Protein in the Tetrapods and Lobe-Finned Fish (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 54 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Immunochemical analysis of the myelin proteolipid protein (PLP) has identified the carboxyl terminal amino acid phenylalanine276 as the only PLP epitope conserved between the PLP components of rat and lungfish, species representing the phylogenetically most widely separated groups that synthesise typical CNS myelin. Immunoblotting using a rabbit antiserum raised against the carboxyl terminal sequence of rat PLP (residues 257–276) identified this epitope on the PLP components of both tetrapod (rat, chicken, lizard, and frog) and lobe-finned fish (coelacanth and lungfish) CNS myelin, including the DM-20 isoform of PLP, which is restricted to rat, chicken, and lizard CNS myelin. The conservation of the carboxyl terminus of PLP during evolution suggests this structure may play an important role in maintaining the organisation and function of PLP in the myelin membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb01969.x
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  • 5
    Electronic Resource
    Electronic Resource
    Accessibility of Galactosyl Ceramides to Probe Reagents in Central Nervous System Myelin (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 35 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The suitability of isolated central nerve myelin preparations for probe labelling studies was assessed and the accessibility of galactosyl ceramides in myelin to galactose oxidase and sodium periodate was determined. Isolated myelin preparations present a uniform external membrane surface to added probes because lamellae in the myelin sheath separate at their external apposition surfaces exclusively during isolation. The cytoplasmic apposition remains intact in isolated myelin. Cationised ferritin can gain access along external apposition regions of inner lamellae in multilamellar fragments of isolated myelin, indicating that proteins and lipids on the external membrane surface will be accessible to probes. Over 50% of the total galactosyl ceramides of myelin are accessible to galactose oxidase attack; hydroxy fatty acid- and nonhydroxy fatty acid-containing cerebrosides are equally attacked. Sodium periodate attacks over 90% of the galactosyl ceramides in isolated myelin at 20°C and electron micrographs of the periodate-treated myelin reveal changes at the external apposition only. Galactosyl ceramides in vesicles of myelin lipid vesicles are not so readily attacked by periodate. The disposition of galactosyl ceramides in the myelin lamellae is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb07098.x
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  • 6
    Electronic Resource
    Electronic Resource
    Fc Receptors are Critical for Autoimmune Inflammatory Damage to the Central Nervous System in Experimental Autoimmune Encephalomyelitis (2002)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 55 (2002), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Multiple sclerosis (MS) is simulated by various forms of experimental autoimmune encephalomyelitis, in which T cells, antibodies, cytokines and complementary factors interact with the central nervous system (CNS) myelin proteins and lead to inflammatory damage. We investigated the role of Fc receptors (FcRs), which link the cellular and humoral branches of the immune system, in myelin oligodendrocyte glycoprotein (MOG)-induced experimental autoimmune encephalomyelitis (EAE), using two different FcRγ knockout DBA/1 mice. The first knockout were the FcRγ chain-deficient mice, which lack FcγRI, FcγRIII and FcεRI, while the second knockout mice lack only FcγRII. The lack of FcγRII enhanced the disease susceptibility with associated increased CNS demyelination. While FcRγ+/+ DBA/1 mice also developed pronounced CNS infiltration and myelin destruction, FcRγ−/− littermates were protected despite initial peripheral autoimmune responses to MOG. In vitro analyses revealed equivalent potentials of fluid phase phagocytosis of myelin and MOG in bone-marrow macrophages derived from both FcRγ+/+ and FcRγ−/− mice, while MOG-immunoglobulin (Ig)G immune complexes were only internalized by FcRγ+/+ macrophages. This was associated with cellular activation in FcRγ+/+ but not FcRγ−/− macrophages, as assessed by the activation of intracellular mitogen activated protein (MAP)-kinase signalling elements. We propose that protection from EAE in FcRγ-deficient mice is due to the inefficient antigen processing/presentation of myelin proteins during the induction of secondary immune responses locally in the CNS, which leads to demyelination. This demonstrates the importance of FcR in the promotion of autoimmune inflammation of the CNS and highlights the therapeutic possibility of treatment of MS with FcR-directed modalities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.2002.01024.x
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  • 7
    Electronic Resource
    Electronic Resource
    Synergism in the Pathogenesis of EAE Induced by an MBP-Specific T-Cell Line and Monoclonal Antibodies to Galactocerebroside or a Myelin Oligodendroglial Glycoprotein (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 540 (1988), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1988.tb27099.x
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  • 8
    Electronic Resource
    Electronic Resource
    Vesicular removal by oligodendrocytes of membrane attack complexes formed by activated complement (1989)
    [s.l.] : Nature Publishing Group
    Nature 339 (1989), S. 620-622 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Our preliminary studies extended reports of complement activation by purified myelin8'9, and showed that exposure of intact neonatal rat optic nerve oligodendrocytes to homologous serum resulted in classical pathway complement activation in the absence of antimyelin antibodies7. Bipotential ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/339620a0
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  • 9
    Electronic Resource
    Electronic Resource
    T lymphocyte autoimmunity in peripheral nervous system autoimmune disease (1986)
    Springer
    Inflammation research 19 (1986), S. 256-265 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Conclusion Autoaggressive T cells specific for the PNS myelin P2 protein play a central role in the initiation of EAN in the Lewis rat, although there is as yet no direct experimental evidence that the T cells can themselves mediate demyelination in vivo. However, the striking similarities in the pathogenesis of EAN and the Guillain-Barré syndrome suggest that T cell mediated EAN provides an excellent model to study the immunological mechanisms of inflammation and demyelination that are relevant to human PNS disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01971223
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