| pubmed-article:7545875 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0033362 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0443146 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7545875 | lifeskim:mentions | umls-concept:C1517004 | lld:lifeskim |
| pubmed-article:7545875 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7545875 | pubmed:dateCreated | 1995-10-17 | lld:pubmed |
| pubmed-article:7545875 | pubmed:abstractText | Type I diabetes, an autoimmune disease that occurs in humans and animals, is characterized by the destruction of insulin-secreting islet beta-cells of the pancreas. Antibodies directed toward multiple islet protein can be detected before diagnosis of type I diabetes; however, the identity of the inciting autoantigen(s) that targets beta-cells for destruction has not been defined. Autorecognition of many self-proteins by CD4+ T lymphocytes is restricted by the products of class II immune response genes of the major histocompatibility complex (MHC), and in human type I diabetes such a MHC association has been described. The present study uses a rat MHC class II (RT1.Bl) peptide binding motif to predict potentially autoreactive CD4+ T cell epitopes in two key islet beta-cell constituents: the enzyme glutamic acid decarboxylase (GAD) and the insulin precursor hormone proinsulin (PI). Seventeen-amino-acid-long peptide fragments of GAD and PI containing the binding motif were synthesized and used to generate peptide-specific, MHC class II-restricted, CD4+ T cell lines. Once established, the T cell lines specific for rat islet GAD and PI were adoptively transferred to naive, MHC-compatible rats. At 10 days after transfer, insulitis had developed in rats receiving PI-specific T cells, whereas no insulitis was observed in pancreata of rats receiving GAD-specific T cells. Of particular interest is the finding that the pathogenic T cell epitope identified in PI spans the endogenous cleavage site between the B-chain and C-peptide of insulin. Moreover, the PI-specific T cells were able to react specifically with material produced in vitro by a rat insulinoma cell line. These results demonstrate that pathogenic T cell epitopes can be located in portions of molecules that are subsequently degraded during normal enzymatic processing. As PI is found highest concentrations in the beta-cells of pancreatic islets, it is possible that this molecule and not its individual degradation products (ie, insulin and C-peptide) might serve as an autoantigen in the pathogenesis of type I diabetes. | lld:pubmed |
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| pubmed-article:7545875 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7545875 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7545875 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:7545875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7545875 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7545875 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7545875 | pubmed:issn | 0002-9440 | lld:pubmed |
| pubmed-article:7545875 | pubmed:author | pubmed-author:GriffinA CAC | lld:pubmed |
| pubmed-article:7545875 | pubmed:author | pubmed-author:WegmannK WKW | lld:pubmed |
| pubmed-article:7545875 | pubmed:author | pubmed-author:ZhakSS | lld:pubmed |
| pubmed-article:7545875 | pubmed:author | pubmed-author:HickleyW FWF | lld:pubmed |
