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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4-5
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pubmed:dateCreated |
1991-8-7
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pubmed:abstractText |
The requirements for insulin presentation and recognition by A alpha b A beta b- and A alpha b A beta k-restricted mouse T cells were studied using a variety of derivatives of the insulin A chain. It was found that A chain peptides with irreversibly blocked Cys residues are non-stimulatory for the T cells. This suggests that at least one of the Cys residues is essential for recognition. On the other hand, all A chain peptides containing Cys residues modified in a way reversible by reaction with thiols are stimulatory yet differ in antigenic potency. All these A chain derivatives including a 14 amino acid fragment require uptake by antigen presenting cells (APC) for efficient presentation. Differences in stimulatory potency between the A chain peptides derived from the same insulin appear to be mainly due to the efficiency of uptake and/or processing by APC. Based on these findings we propose that processing in the case of insulin and its A chain derivatives involves the reductive deblocking of Cys residues or the rearrangement of disulfide bonds apart from a possible proteolytic cleavage. The same may apply to other proteins if Cys residues in the presented peptides are important for the interaction with Ia or the T cell receptor.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chloroquine,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell
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pubmed:status |
MEDLINE
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pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
479-87
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1712073-Animals,
pubmed-meshheading:1712073-Antigen-Presenting Cells,
pubmed-meshheading:1712073-Cattle,
pubmed-meshheading:1712073-Cell Line,
pubmed-meshheading:1712073-Chloroquine,
pubmed-meshheading:1712073-Cysteine,
pubmed-meshheading:1712073-Epitopes,
pubmed-meshheading:1712073-Histocompatibility Antigens Class II,
pubmed-meshheading:1712073-Insulin,
pubmed-meshheading:1712073-Interleukin-3,
pubmed-meshheading:1712073-Mice,
pubmed-meshheading:1712073-Mice, Inbred Strains,
pubmed-meshheading:1712073-Peptides,
pubmed-meshheading:1712073-Receptors, Antigen, T-Cell,
pubmed-meshheading:1712073-Swine,
pubmed-meshheading:1712073-T-Lymphocytes
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pubmed:articleTitle |
Presentation of insulin and insulin A chain peptides to mouse T cells: involvement of cysteine residues.
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pubmed:affiliation |
Institut für Immunologie der Joh. Gutenberg Universität, Mainz, Germany.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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