| pubmed-article:17548631 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0021699 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0042219 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C1299583 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0449450 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C1608386 | lld:lifeskim |
| pubmed-article:17548631 | lifeskim:mentions | umls-concept:C1549571 | lld:lifeskim |
| pubmed-article:17548631 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17548631 | pubmed:dateCreated | 2007-6-5 | lld:pubmed |
| pubmed-article:17548631 | pubmed:abstractText | MHC class I molecules present peptides derived from the ectodomains of endogenous transmembrane proteins; however, the processing of these Ags is incompletely understood. As model transmembrane Ags we investigated the processing of MHC-I-derived fusion proteins containing the N-terminally extended K(b)-restricted OVA epitope SIINFEKL in the extracytoplasmic domain. In TAP-deficient, nonprofessional APCs, the epitope was cleaved out of various sequence contexts and presented to T cells. Ag presentation was inhibited by acidophilic amines and inhibitors of the vacuolar proton pump, indicating processing in endosomes. Endosomal aspartic-type cathepsins, and to some extent also the trans-Golgi network protease furin, were involved in processing. Clathrin-dependent and independent internalization from the cell surface targeted MHC-I fusion proteins to early and late endosomes, where SIINFEKL/K(b) complexes were detected by immunofluorescence microscopy. Targeting of MHC-I fusion proteins to processing compartments was independent of sequence motifs in the cytoplasmic tail. Not only TAP-deficient cells, but also TAP-competent APCs used the vacuolar pathway for processing of MHC-I fusion proteins. Thus, endosomal processing of internalized endogenous transmembrane proteins represents a novel alternate pathway for the generation of MHC-I-binding peptides. | lld:pubmed |
| pubmed-article:17548631 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17548631 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17548631 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17548631 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17548631 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:GarbiNatalioN | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:MomburgFrankF | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:HämmerlingGün... | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:ReinheckelTho... | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:MoldenhauerGe... | lld:pubmed |
| pubmed-article:17548631 | pubmed:author | pubmed-author:TiwariNeerajN | lld:pubmed |
| pubmed-article:17548631 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17548631 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17548631 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:17548631 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17548631 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17548631 | pubmed:pagination | 7932-42 | lld:pubmed |
| pubmed-article:17548631 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:17548631 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17548631 | pubmed:articleTitle | A transporter associated with antigen-processing independent vacuolar pathway for the MHC class I-mediated presentation of endogenous transmembrane proteins. | lld:pubmed |
| pubmed-article:17548631 | pubmed:affiliation | Department of Molecular Immunology, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany. | lld:pubmed |
| pubmed-article:17548631 | pubmed:publicationType | Journal Article | lld:pubmed |
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