| pubmed-article:19954752 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C0003315 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C0108471 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:19954752 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:19954752 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19954752 | pubmed:dateCreated | 2010-2-17 | lld:pubmed |
| pubmed-article:19954752 | pubmed:abstractText | Cathepsins are expressed in antigen-presenting cells (APC). These cathepsins are known to regulate antigen processing and degradation of the invariant chain (Ii) into the class II-associated Ii peptide (CLIP), which occupies the peptide-binding groove of the major histocompatibility complex (MHC) class II molecule. Previous studies have identified the serine carboxypeptidase cathepsin A (CatA) in various tissues and cells; however, it is not clear whether CatA is also expressed in primary human APC. We demonstrate the expression of CatA in B lymphoblastoid cells (BLC), primary human B cells, both subsets of myeloid dendritic cells (mDC1 and mDC2), as well as in plasmacytoid DC. PMSF or lactacystin-mediated inhibition of serine proteases in BLC-derived lysosomal proteases resulted in the inhibition of amino acid release from the C-terminal end of two model peptides. This inhibition did not occur by using a proline rich peptide. Our data suggest that CatA is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human APC. | lld:pubmed |
| pubmed-article:19954752 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19954752 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19954752 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19954752 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19954752 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19954752 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19954752 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19954752 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19954752 | pubmed:issn | 1879-0542 | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:ReichMichaelM | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:KalbacherHube... | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:BoehmBernhard... | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:BursterTimoT | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:SpindlerKlaus... | lld:pubmed |
| pubmed-article:19954752 | pubmed:author | pubmed-author:BurretMichael... | lld:pubmed |
| pubmed-article:19954752 | pubmed:copyrightInfo | Copyright (c) 2009 Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:19954752 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19954752 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:19954752 | pubmed:volume | 128 | lld:pubmed |
| pubmed-article:19954752 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19954752 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19954752 | pubmed:pagination | 143-7 | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:meshHeading | pubmed-meshheading:19954752... | lld:pubmed |
| pubmed-article:19954752 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19954752 | pubmed:articleTitle | Cathepsin A is expressed in primary human antigen-presenting cells. | lld:pubmed |
| pubmed-article:19954752 | pubmed:affiliation | Division of Endocrinology and Diabetes, Center for Internal Medicine, University Medical Center Ulm, Ulm, Albert-Einstein-Allee 23, 89081 Ulm, Germany. | lld:pubmed |
| pubmed-article:19954752 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19954752 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5476 | entrezgene:pubmed | pubmed-article:19954752 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19954752 | lld:entrezgene |
