pubmed-article:12000758 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0006142 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0026682 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C1417490 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C1979963 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0178587 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C2003903 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
pubmed-article:12000758 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
pubmed-article:12000758 | pubmed:issue | 29 | lld:pubmed |
pubmed-article:12000758 | pubmed:dateCreated | 2002-7-15 | lld:pubmed |
pubmed-article:12000758 | pubmed:abstractText | Knowledge about the O-linked glycan chains of tumor-associated MUC1 is primarily based on enzymatic and immunochemical evidence. To obtain structural information and to overcome limitations by the scarcity of endogenous mucin, we expressed a recombinant glycosylation probe corresponding to six MUC1 tandem repeats in four breast cancer cell lines. Comparative analyses of the O-glycan profiles were performed after hydrazinolysis and normal phase chromatography of 2-aminobenzamide-labeled glycans. Except for a general reduction in the O-glycan chain lengths and a high density glycosylation, no common structural pattern was revealed. T47D fusion protein exhibits an almost complete shift from core 2 to core 1 expression with a preponderance of sialylated glycans. By contrast, MCF-7, MDA-MB231, and ZR75-1 cells glycosylate the MUC1 repeat peptide preferentially with core 2-based glycans terminating mostly with alpha 3-linked sialic acid (MDA-MB231, ZR75-1) or alpha 2/3-linked fucose (MCF-7). Endogenous MUC1 from T47D and MCF-7 cell supernatants revealed almost identical O-glycosylation profiles compared with the respective recombinant probes, indicating that the fusion proteins reflected the authentic O-glycan profiles of the cells. The structural patterns in the majority of cells under study are in conflict with biosynthetic models of MUC1 O-glycosylation in breast cancer, which claim that the truncation of normal core 2-based polylactosamine structures to short sialylated core 1-based glycans is due to the reduced activity of core 2-forming beta 6-N-acetylglucosaminyltransferases and/or to overexpression of competitive alpha 3- sialyltransferase. | lld:pubmed |
pubmed-article:12000758 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12000758 | pubmed:language | eng | lld:pubmed |
pubmed-article:12000758 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12000758 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12000758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12000758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12000758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12000758 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12000758 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12000758 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12000758 | pubmed:author | pubmed-author:MüllerStefanS | lld:pubmed |
pubmed-article:12000758 | pubmed:author | pubmed-author:HanischFranz-... | lld:pubmed |
pubmed-article:12000758 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12000758 | pubmed:day | 19 | lld:pubmed |
pubmed-article:12000758 | pubmed:volume | 277 | lld:pubmed |
pubmed-article:12000758 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12000758 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12000758 | pubmed:pagination | 26103-12 | lld:pubmed |
pubmed-article:12000758 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:12000758 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12000758 | pubmed:articleTitle | Recombinant MUC1 probe authentically reflects cell-specific O-glycosylation profiles of endogenous breast cancer mucin. High density and prevalent core 2-based glycosylation. | lld:pubmed |
pubmed-article:12000758 | pubmed:affiliation | Institute of Biochemistry II, Medical Faculty of the University, Joseph-Stelzmann-Str. 52, Köln D-50931, Germany. stefan.mueller@uni-koeln.de | lld:pubmed |
pubmed-article:12000758 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12000758 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12000758 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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