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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1988-1-4
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pubmed:abstractText |
Experimental autoimmune myasthenia gravis (EAMG) and antibodies that modulate AChRs from cultured human muscle are induced by a disulfide-looped peptide comprising the human acetylcholine receptor (AChR) alpha-subunit residues 125-147 (H alpha 125-147). To delineate the essential antigenic requirements for induction of EAMG by this peptide, a series of peptides was synthesized: (a) a nonlooped analog (Cys 128 replaced by Ser) stimulated modulating autoantibodies, induced EAMG, and bound antibodies induced by native AChR; (b) H alpha 131-147, a heptadecylpeptide shorter by 6 N-terminal residues, induced modulating antibodies, EAMG, and T cells that responded to H alpha 125-147, but not to H alpha 137-147; (c) H alpha 137-147, an undecapeptide shorter than H alpha 125-147 by 12 N-terminal residues, did not stimulate T cells or induce antibody production, but it bound antibodies generated by the longer peptides. Thus, when coupled to an epitope that could stimulate helper T cells, the region 137-147 was able to stimulate B cells. This study has defined a myasthenogenic region of the human AChR's alpha-subunit, 17 amino acids long, that contains several distinct epitopes, including at least one N-terminal site inducing T-cell responses (region 131-136) and two possibly overlapping sites that induce antibodies (regions 131-136 and 137-147). Further definition of antigenic sites inducing helper and suppressor T-cell responses and stimulating production of autoantibodies to AChR is essential to the goal of antigen-specific immunotherapy for myasthenia gravis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nicotinic
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pubmed:status |
MEDLINE
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pubmed:issn |
0077-8923
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
505
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
439-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2446556-Action Potentials,
pubmed-meshheading:2446556-Animals,
pubmed-meshheading:2446556-Antibodies, Monoclonal,
pubmed-meshheading:2446556-Autoantibodies,
pubmed-meshheading:2446556-Autoantigens,
pubmed-meshheading:2446556-Epitopes,
pubmed-meshheading:2446556-Female,
pubmed-meshheading:2446556-Humans,
pubmed-meshheading:2446556-Motor Endplate,
pubmed-meshheading:2446556-Peptide Fragments,
pubmed-meshheading:2446556-Rats,
pubmed-meshheading:2446556-Rats, Inbred Lew,
pubmed-meshheading:2446556-Receptors, Nicotinic,
pubmed-meshheading:2446556-T-Lymphocytes
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pubmed:year |
1987
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pubmed:articleTitle |
Definition of myasthenogenic sites of the human acetylcholine receptor using synthetic peptides.
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pubmed:affiliation |
Department of Immunology, Mayo Clinic, Rochester, Minnesota 55905.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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