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rdf:type |
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lifeskim:mentions |
umls-concept:C0030956,
umls-concept:C0040113,
umls-concept:C0206431,
umls-concept:C0337112,
umls-concept:C0386280,
umls-concept:C0542341,
umls-concept:C0619541,
umls-concept:C0621732,
umls-concept:C0621734,
umls-concept:C1334043,
umls-concept:C1524075,
umls-concept:C1704419,
umls-concept:C2697616
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pubmed:issue |
6
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pubmed:dateCreated |
1989-7-19
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pubmed:abstractText |
The B chain of mammalian insulins contains appropriately spaced amino acids that predict recognition by T cells. However, all T cell clones from an HLA-DR1, Dw6 diabetic donor recognize epitopes associated with the A chain, and the B chain was found to inhibit these responses. Effective intramolecular competition at the level of the APC, not a direct effect on the T cell, is responsible for the inhibition. Insulin B chain contains two clusters of amino acid homology with the TCR beta chain and B chain peptides lacking these clusters do not compete for antigen presentation. A hole in the repertoire for T cells that recognize this portion of the insulin molecule may arise in the thymus by deletion of T cells that recognize similar peptides.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2414111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2433769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2435001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2443855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2445817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2447156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2451692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2460529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-2963699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-3075590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-3261393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-3459185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-3490919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-3494522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-6161958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2471779-6795263
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
169
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2251-6
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2471779-Amino Acid Sequence,
pubmed-meshheading:2471779-Animals,
pubmed-meshheading:2471779-Antigen-Presenting Cells,
pubmed-meshheading:2471779-Binding, Competitive,
pubmed-meshheading:2471779-Cattle,
pubmed-meshheading:2471779-Epitopes,
pubmed-meshheading:2471779-Humans,
pubmed-meshheading:2471779-Immunoglobulin Constant Regions,
pubmed-meshheading:2471779-Insulin,
pubmed-meshheading:2471779-Molecular Sequence Data,
pubmed-meshheading:2471779-Peptide Fragments,
pubmed-meshheading:2471779-Receptors, Antigen, T-Cell,
pubmed-meshheading:2471779-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2471779-Thymus Gland
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pubmed:year |
1989
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pubmed:articleTitle |
Insulin B chain functions as an effective competitor of antigen presentation via peptide homologies present in the thymus.
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pubmed:affiliation |
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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