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000049189 0247_ $$2DOI$$a10.1074/jbc.M511826200
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000049189 1001_ $$0P:(DE-HGF)0$$aSewell, R.$$b0
000049189 245__ $$aThe ST6GalNAc-l sialyltransferase localises throughout the Golgi and is responsible for the synthesis of the tumour associated sialyl Tn O-glycan in human breast cancer
000049189 260__ $$aBethesda, Md.$$bSoc.$$c2006
000049189 300__ $$a3586 - 3594
000049189 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000049189 440_0 $$03091$$aJournal of Biological Chemistry$$v281$$x0021-9258$$y6
000049189 500__ $$aRecord converted from VDB: 12.11.2012
000049189 520__ $$aThe functional properties of glycoproteins are strongly influenced by their profile of glycosylation, and changes in this profile are seen in malignancy. In mucin-type O-linked glycosylation these changes can result in the production of mucins such as MUC1, carrying shorter sialylated O-glycans, and with different site occupancy. Of the tumor-associated sialylated O-glycans, the disaccharide, sialyl-Tn (sialic acid alpha2,6GalNAc), is expressed by 30% of breast carcinomas and is the most tumor-specific. The ST6GalNAc-I glycosyltransferase, which can catalyze the transfer of sialic acid to GalNAc, shows a highly restricted pattern of expression in normal adult tissues, being largely limited to the gastrointestinal tract and absent in mammary gland. In breast carcinomas, however, a complete correlation between the expression of RNA-encoding ST6GalNAc-I and the expression of sialyl-Tn is evident, demonstrating that the expression of sialyl-Tn results from switching on expression of hST6GalNAc-I. Endogenous or exogenous expression of hST6GalNAc-I (but not ST6GalNAc-II) always results in the expression of sialyl-Tn. This ability to override core 1/core 2 pathways of O- linked glycosylation is explained by the localization of ST6GalNAc-I, which is found throughout the Golgi stacks. The development of a Chinese hamster ovary (CHO) cell line expressing MUC1 and ST6GalNAc-I allowed the large scale production of MUC1 carrying 83% sialyl-Tn O-glycans. The presence of ST6GalNAc-I in the CHO cells reduced the number of O-glycosylation sites occupied in MUC1, from an average of 4.3 to 3.8 per tandem repeat. The availability of large quantities of this MUC1 glycoform will allow the evaluation of its efficacy as an immunogen for immunotherapy of MUC1/STn-expressing tumors.
000049189 536__ $$0G:(DE-Juel1)FUEK410$$2G:(DE-HGF)$$aBiotechnologie$$cPBT$$x0
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000049189 650_2 $$2MeSH$$aAnimals
000049189 650_2 $$2MeSH$$aAntigens, Neoplasm: chemistry
000049189 650_2 $$2MeSH$$aAntigens, Tumor-Associated, Carbohydrate: chemistry
000049189 650_2 $$2MeSH$$aBlotting, Northern
000049189 650_2 $$2MeSH$$aBlotting, Western
000049189 650_2 $$2MeSH$$aBreast Neoplasms: enzymology
000049189 650_2 $$2MeSH$$aBreast Neoplasms: pathology
000049189 650_2 $$2MeSH$$aCHO Cells
000049189 650_2 $$2MeSH$$aCell Line, Tumor
000049189 650_2 $$2MeSH$$aChromatography, Liquid
000049189 650_2 $$2MeSH$$aCloning, Molecular
000049189 650_2 $$2MeSH$$aCricetinae
000049189 650_2 $$2MeSH$$aFemale
000049189 650_2 $$2MeSH$$aFlow Cytometry
000049189 650_2 $$2MeSH$$aGlycosylation
000049189 650_2 $$2MeSH$$aGolgi Apparatus: enzymology
000049189 650_2 $$2MeSH$$aGolgi Apparatus: metabolism
000049189 650_2 $$2MeSH$$aHumans
000049189 650_2 $$2MeSH$$aImmunotherapy: methods
000049189 650_2 $$2MeSH$$aK562 Cells
000049189 650_2 $$2MeSH$$aMammary Glands, Human: metabolism
000049189 650_2 $$2MeSH$$aMicroscopy, Fluorescence
000049189 650_2 $$2MeSH$$aMicroscopy, Immunoelectron
000049189 650_2 $$2MeSH$$aModels, Chemical
000049189 650_2 $$2MeSH$$aPolysaccharides: chemistry
000049189 650_2 $$2MeSH$$aPolysaccharides: metabolism
000049189 650_2 $$2MeSH$$aRecombinant Fusion Proteins: chemistry
000049189 650_2 $$2MeSH$$aReverse Transcriptase Polymerase Chain Reaction
000049189 650_2 $$2MeSH$$aSialyltransferases: chemistry
000049189 650_2 $$2MeSH$$aSialyltransferases: metabolism
000049189 650_2 $$2MeSH$$aSpectrometry, Mass, Electrospray Ionization
000049189 650_2 $$2MeSH$$aTransfection
000049189 650_7 $$00$$2NLM Chemicals$$aAntigens, Neoplasm
000049189 650_7 $$00$$2NLM Chemicals$$aAntigens, Tumor-Associated, Carbohydrate
000049189 650_7 $$00$$2NLM Chemicals$$aPolysaccharides
000049189 650_7 $$00$$2NLM Chemicals$$aRecombinant Fusion Proteins
000049189 650_7 $$00$$2NLM Chemicals$$asialosyl-Tn antigen
000049189 650_7 $$0EC 2.4.99.-$$2NLM Chemicals$$aSialyltransferases
000049189 650_7 $$0EC 2.4.99.3$$2NLM Chemicals$$aCMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
000049189 7001_ $$0P:(DE-HGF)0$$aBäckstrom, M.$$b1
000049189 7001_ $$0P:(DE-HGF)0$$aDalziel, M.$$b2
000049189 7001_ $$0P:(DE-HGF)0$$aGschmeissner, S.$$b3
000049189 7001_ $$0P:(DE-HGF)0$$aKarlsson, H.$$b4
000049189 7001_ $$0P:(DE-Juel1)VDB1170$$aNoll, T.$$b5$$uFZJ
000049189 7001_ $$0P:(DE-Juel1)VDB7932$$aGätgens, J.$$b6$$uFZJ
000049189 7001_ $$0P:(DE-HGF)0$$aClausen, H.$$b7
000049189 7001_ $$0P:(DE-HGF)0$$aHansson, G.$$b8
000049189 7001_ $$0P:(DE-HGF)0$$aBurchell, J.$$b9
000049189 7001_ $$0P:(DE-HGF)0$$aTaylor-Papadimitriou, J.$$b10
000049189 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M511826200$$gVol. 281, p. 3586 - 3594$$p3586 - 3594$$q281<3586 - 3594$$tThe @journal of biological chemistry$$v281$$x0021-9258$$y2006
000049189 8567_ $$uhttp://hdl.handle.net/2128/2839$$uhttp://dx.doi.org/10.1074/jbc.M511826200
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