pubmed-article:17805347 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C2350332 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
pubmed-article:17805347 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
pubmed-article:17805347 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:17805347 | pubmed:dateCreated | 2007-10-3 | lld:pubmed |
pubmed-article:17805347 | pubmed:abstractText | Antigen-specific interactions between B cells and T cells are essential for the generation of an efficient immune response. Since this requires peptide-MHC class II complexes (pMHC-II) on the B cell to interact with TCR on antigen-specific T cells, we have examined the mechanisms regulating the persistence, loss, and secretion of specific pMHC-II complexes on activated B cells. Using a mAb that recognizes specific pMHC-II, we found that activated B cells degrade approximately 50% of pMHC-II every day and release 12% of these pMHC-II from the cell on small membrane vesicles termed exosomes. These exosomes directly stimulate primed, but not naïve, CD4 T cells. Interestingly, engagement of antigen-loaded B cells with specific CD4 T cells stimulates exosome release in a manner that can be mimicked by pMHC-II crosslinking. Biochemical studies revealed that the pMHC-II released on exosomes was previously expressed on the plasma membrane of the B cells, suggesting that regulated exosome release from activated B cells is a mechanism to allow pMHC-II to escape intracellular degradation and decorate secondary lymphoid organs with membrane-associated pMHC-II complexes. | lld:pubmed |
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pubmed-article:17805347 | pubmed:language | eng | lld:pubmed |
pubmed-article:17805347 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17805347 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17805347 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17805347 | pubmed:month | Oct | lld:pubmed |
pubmed-article:17805347 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:17805347 | pubmed:author | pubmed-author:RochePaul APA | lld:pubmed |
pubmed-article:17805347 | pubmed:author | pubmed-author:MuntasellAura... | lld:pubmed |
pubmed-article:17805347 | pubmed:author | pubmed-author:BergerAdam... | lld:pubmed |
pubmed-article:17805347 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17805347 | pubmed:day | 3 | lld:pubmed |
pubmed-article:17805347 | pubmed:volume | 26 | lld:pubmed |
pubmed-article:17805347 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17805347 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17805347 | pubmed:pagination | 4263-72 | lld:pubmed |
pubmed-article:17805347 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:17805347 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17805347 | pubmed:articleTitle | T cell-induced secretion of MHC class II-peptide complexes on B cell exosomes. | lld:pubmed |
pubmed-article:17805347 | pubmed:affiliation | Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
pubmed-article:17805347 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17805347 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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