Linked Life Data

1712073

Source:http://linkedlifedata.com/resource/pubmed/id/1712073

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pubmed-article:1712073pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:1712073pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:1712073pubmed:articleTitlePresentation of insulin and insulin A chain peptides to mouse T cells: involvement of cysteine residues.lld:pubmed
pubmed-article:1712073pubmed:affiliationInstitut für Immunologie der Joh. Gutenberg Universität, Mainz, Germany.lld:pubmed
pubmed-article:1712073pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:1712073pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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