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  • Botulinum toxin  (1)
  • Isoform  (1)
  • Myasthenia gravis thymus  (1)
  • 1
    ISSN: 0014-5793
    Keywords: AChR: α-Subunit ; Isoform ; TE671 cell ; Translation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of neurology 238 (1991), S. 256-261 
    ISSN: 1432-1459
    Keywords: Myasthenia gravis thymus ; Thymic hyperplasia ; Thymitis ; Seronegative myasthenia gravis ; Human lymphocyte cultures
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In 5–10% of all patients with typical generalised myasthenia gravis (MG), serum antibody to the acetylcholine receptor (AChR) is undetectable. To determine whether these represent a distinct subgroup, we have compared the thymuses of 14 seronegatives, 70 seropositives and 12 non-myasthenic controls. By quantitative immunohistology on coded sections, the 7 seronegative samples were clearly distinguishable from the controls by the pronounced lymph node-type T-cell areas in the medulla. While these closely resembled those in the seropositive cases, germinal centres were significantly sparser, and total in vitro IgG production was disproportionately low (per B cell) in the 12 cases tested. Furthermore, specific anti-AChR production was never detected in any of these cultures. The data support the view that the medullary T-cell areas are the most consistent abnormalitiy in the MG thymus (though it may not be primary), and they strongly imply that seronegative and seropositive MG are distinct entities.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1435-1463
    Keywords: Botulinum toxin ; antibody ; transmitter release ; neuromuscular junction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The interaction between two presynaptically acting agents, Lambert-Eaton myasthenic syndrome (LEMS) immunoglobulin G (IgG) and purified botulinum neurotoxin (BoNT) type A, was studied. Intracellular microelectrode recordings were carried out on mouse muscles after injection with LEMS IgG. BoNT was either injected before recordings were made or applied in vitro. The time course of the in vitro actions of BoNT on miniature end-plate potential and end-plate potential parameters were not affected by pretreatment with LEMS IgG. After in vivo injection of BoNT, end-plate potential quantal content was reduced to less than 2% of control values, whether or not LEMS IgG had also been previously given. Quantitative electron-microscope autoradiographical analysis showed that neither the binding of125I-BoNT to acceptors on the nerve terminal membrane nor the pattern of its internalisation were affected by pretreatment with LEMS IgG. We conclude that the effects of BoNT are not affected by LEMS IgG, suggesting different presynaptic binding sites for the two agents.
    Type of Medium: Electronic Resource
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