| pubmed-article:15100291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C0024369 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C0014063 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C0054868 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:15100291 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:15100291 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:15100291 | pubmed:dateCreated | 2004-4-21 | lld:pubmed |
| pubmed-article:15100291 | pubmed:abstractText | The asparagine-specific endoprotease (AEP) controls lysosomal processing of the potential autoantigen myelin basic protein (MBP) by human B lymphoblastoid cells, a feature implicated in the immunopathogenesis of multiple sclerosis. In this study, we demonstrate that freshly isolated human B lymphocytes lack significant AEP activity and that cleavage by AEP is dispensable for proteolytic processing of MBP in this type of cell. Instead, cathepsin (Cat) G, a serine protease that is not endogenously synthesized by B lymphocytes, is internalized from the plasma membrane and present in lysosomes from human B cells where it represents a major functional constituent of the proteolytic machinery. CatG initialized and dominated the destruction of intact MBP by B cell-derived lysosomal extracts, degrading the immunodominant MBP epitope and eliminating both its binding to MHC class II and a MBP-specific T cell response. Degradation of intact MBP by CatG was not restricted to a lysosomal environment, but was also performed by soluble CatG. Thus, the abundant protease CatG might participate in eliminating the immunodominant determinant of MBP. Internalization of exogenous CatG represents a novel mechanism of professional APC to acquire functionally dominant proteolytic activity that complements the panel of endogenous lysosomal enzymes. | lld:pubmed |
| pubmed-article:15100291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15100291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15100291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15100291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15100291 | pubmed:month | May | lld:pubmed |
| pubmed-article:15100291 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:FalkKirstenK | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:ReichMichaelM | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:KalbacherHube... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:DriessenChris... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:StevanovicSte... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:WiendlHeinzH | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:SchwarzGerold... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:MelmsArthurA | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:BeckAlexander... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:BursterTimoT | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:LautweinAlfre... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:RötzschkeOlaf... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:BrandenburgJe... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:LehmannRainer... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:Marin-Esteban... | lld:pubmed |
| pubmed-article:15100291 | pubmed:author | pubmed-author:TolosaEvaE | lld:pubmed |
| pubmed-article:15100291 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15100291 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15100291 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:15100291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15100291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15100291 | pubmed:pagination | 5495-503 | lld:pubmed |
| pubmed-article:15100291 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15100291 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15100291 | pubmed:articleTitle | Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. | lld:pubmed |
| pubmed-article:15100291 | pubmed:affiliation | Department of Medicine II, University of Tübingen, Tübingen, Germany. | lld:pubmed |
| pubmed-article:15100291 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15100291 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15100291 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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