Anatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptor

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dc.contributor.authorTzartos, S. J.en
dc.contributor.authorBarkas, T.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorMamalaki, A.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorOrlewski, P.en
dc.contributor.authorPapanastasiou, D.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorTsantili, P.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:50:00Z
dc.date.available2015-11-24T16:50:00Z
dc.identifier.issn0105-2896-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9555
dc.rightsDefault Licence-
dc.subjectmain immunogenic regionen
dc.subjectautoimmune myasthenia-gravisen
dc.subjectalpha-bungarotoxin bindingen
dc.subjectpenicillamine-induced myastheniaen
dc.subjectprotein-a immunoadsorptionen
dc.subjectanti-idiotypic antibodiesen
dc.subjectrat monoclonal-antibodyen
dc.subjectsite-specific probesen
dc.subjectamino-acid-residuesen
dc.subjectsynthetic peptidesen
dc.titleAnatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptoren
heal.abstractThe neuromuscular junction nicotinic acetylcholine receptor (AChR), a pentameric membrane glycoprotein, is the autoantigen involved in the autoimmune disease myasthenia gravis (MG).In animals immunized with intact AChR and in human MG, the anti-AChR antibody response is polyclonal. However, a small extracellular region of the AChR alpha-subunit, the main immunogenic region (MIR), seems to be a major target for anti-AChR antibodies. A major loop containing overlapping epitopes for several anti-MIR monoclonal antibodies (mAbs) lies within residues alpha 67-76 at the extreme synaptic end of each alpha-subunit; however, anti-MIR mAbs are functionally and structurally quite heterogeneous. Anti-MIR mAbs do not affect channel gating, but are very effective in the passive transfer of MG to animals; in contrast, their Fab or Fv fragments protect the AChR from the pathogenic effects of the intact antibodies. Antibodies against the cytoplasmic region of the AChR can be elicited by immunization with denatured AChR and the precise epitopes of many such mAbs have been identified; however, it is unlikely that such antibodies are present in significant amounts in human MG. Antibodies to other extracellular epitopes on all AChR subunits are present in both experimental and human MG; these include antibodies to the acetylcholine-binding site which affect AChR function in various ways and also induce acute experimental MG. Finally, anti-AChR antibodies cross-reactive with non-AChR antigens exist, suggesting that MG may result from molecular mimicry. Despite extensive studies, many gaps remain in our understanding of the antigenic structure of the AChR, especially in relation to human MG. A thorough understanding of the antigenic structure of the AChR is required for an in-depth understanding, and for possible specific immunotherapy, of MG.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primary10.1111/j.1600-065X.1998.tb01190.x-
heal.identifier.secondary<Go to ISI>://000074973900008-
heal.journalNameImmunological Reviewsen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate1998-
heal.publisherMunksgaard Int Publ Ltd.en
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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