001     49189
005     20200423204256.0
024 7 _ |a pmid:16319059
|2 pmid
024 7 _ |a 10.1074/jbc.M511826200
|2 DOI
024 7 _ |a 2128/2839
|2 Handle
024 7 _ |a WOS:000235128200070
|2 WOS
024 7 _ |a altmetric:3551132
|2 altmetric
037 _ _ |a PreJuSER-49189
041 _ _ |a eng
082 _ _ |a 570
100 1 _ |a Sewell, R.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a The 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
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2006
300 _ _ |a 3586 - 3594
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Biological Chemistry
|x 0021-9258
|0 3091
|y 6
|v 281
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Biotechnologie
|c PBT
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK410
|x 0
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Antigens, Neoplasm: chemistry
650 _ 2 |2 MeSH
|a Antigens, Tumor-Associated, Carbohydrate: chemistry
650 _ 2 |2 MeSH
|a Blotting, Northern
650 _ 2 |2 MeSH
|a Blotting, Western
650 _ 2 |2 MeSH
|a Breast Neoplasms: enzymology
650 _ 2 |2 MeSH
|a Breast Neoplasms: pathology
650 _ 2 |2 MeSH
|a CHO Cells
650 _ 2 |2 MeSH
|a Cell Line, Tumor
650 _ 2 |2 MeSH
|a Chromatography, Liquid
650 _ 2 |2 MeSH
|a Cloning, Molecular
650 _ 2 |2 MeSH
|a Cricetinae
650 _ 2 |2 MeSH
|a Female
650 _ 2 |2 MeSH
|a Flow Cytometry
650 _ 2 |2 MeSH
|a Glycosylation
650 _ 2 |2 MeSH
|a Golgi Apparatus: enzymology
650 _ 2 |2 MeSH
|a Golgi Apparatus: metabolism
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Immunotherapy: methods
650 _ 2 |2 MeSH
|a K562 Cells
650 _ 2 |2 MeSH
|a Mammary Glands, Human: metabolism
650 _ 2 |2 MeSH
|a Microscopy, Fluorescence
650 _ 2 |2 MeSH
|a Microscopy, Immunoelectron
650 _ 2 |2 MeSH
|a Models, Chemical
650 _ 2 |2 MeSH
|a Polysaccharides: chemistry
650 _ 2 |2 MeSH
|a Polysaccharides: metabolism
650 _ 2 |2 MeSH
|a Recombinant Fusion Proteins: chemistry
650 _ 2 |2 MeSH
|a Reverse Transcriptase Polymerase Chain Reaction
650 _ 2 |2 MeSH
|a Sialyltransferases: chemistry
650 _ 2 |2 MeSH
|a Sialyltransferases: metabolism
650 _ 2 |2 MeSH
|a Spectrometry, Mass, Electrospray Ionization
650 _ 2 |2 MeSH
|a Transfection
650 _ 7 |0 0
|2 NLM Chemicals
|a Antigens, Neoplasm
650 _ 7 |0 0
|2 NLM Chemicals
|a Antigens, Tumor-Associated, Carbohydrate
650 _ 7 |0 0
|2 NLM Chemicals
|a Polysaccharides
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Fusion Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a sialosyl-Tn antigen
650 _ 7 |0 EC 2.4.99.-
|2 NLM Chemicals
|a Sialyltransferases
650 _ 7 |0 EC 2.4.99.3
|2 NLM Chemicals
|a CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
700 1 _ |a Bäckstrom, M.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Dalziel, M.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Gschmeissner, S.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Karlsson, H.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Noll, T.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB1170
700 1 _ |a Gätgens, J.
|b 6
|u FZJ
|0 P:(DE-Juel1)VDB7932
700 1 _ |a Clausen, H.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Hansson, G.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Burchell, J.
|b 9
|0 P:(DE-HGF)0
700 1 _ |a Taylor-Papadimitriou, J.
|b 10
|0 P:(DE-HGF)0
773 _ _ |a 10.1074/jbc.M511826200
|g Vol. 281, p. 3586 - 3594
|p 3586 - 3594
|q 281<3586 - 3594
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 281
|y 2006
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbc.M511826200
|u http://hdl.handle.net/2128/2839
856 4 _ |u https://juser.fz-juelich.de/record/49189/files/77061.pdf
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909 C O |o oai:juser.fz-juelich.de:49189
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913 1 _ |k PBT
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914 1 _ |y 2006
915 _ _ |0 StatID:(DE-HGF)0010
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980 _ _ |a UNRESTRICTED
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