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@ARTICLE{Sewell:49189,
      author       = {Sewell, R. and Bäckstrom, M. and Dalziel, M. and
                      Gschmeissner, S. and Karlsson, H. and Noll, T. and Gätgens,
                      J. and Clausen, H. and Hansson, G. and Burchell, J. and
                      Taylor-Papadimitriou, J.},
      title        = {{T}he {ST}6{G}al{NA}c-l sialyltransferase localises
                      throughout the {G}olgi and is responsible for the synthesis
                      of the tumour associated sialyl {T}n {O}-glycan in human
                      breast cancer},
      journal      = {The journal of biological chemistry},
      volume       = {281},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-49189},
      pages        = {3586 - 3594},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Animals / Antigens, Neoplasm: chemistry / Antigens,
                      Tumor-Associated, Carbohydrate: chemistry / Blotting,
                      Northern / Blotting, Western / Breast Neoplasms: enzymology
                      / Breast Neoplasms: pathology / CHO Cells / Cell Line, Tumor
                      / Chromatography, Liquid / Cloning, Molecular / Cricetinae /
                      Female / Flow Cytometry / Glycosylation / Golgi Apparatus:
                      enzymology / Golgi Apparatus: metabolism / Humans /
                      Immunotherapy: methods / K562 Cells / Mammary Glands, Human:
                      metabolism / Microscopy, Fluorescence / Microscopy,
                      Immunoelectron / Models, Chemical / Polysaccharides:
                      chemistry / Polysaccharides: metabolism / Recombinant Fusion
                      Proteins: chemistry / Reverse Transcriptase Polymerase Chain
                      Reaction / Sialyltransferases: chemistry /
                      Sialyltransferases: metabolism / Spectrometry, Mass,
                      Electrospray Ionization / Transfection / Antigens, Neoplasm
                      (NLM Chemicals) / Antigens, Tumor-Associated, Carbohydrate
                      (NLM Chemicals) / Polysaccharides (NLM Chemicals) /
                      Recombinant Fusion Proteins (NLM Chemicals) / sialosyl-Tn
                      antigen (NLM Chemicals) / Sialyltransferases (NLM Chemicals)
                      / CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
                      alpha-2,6-sialyltransferase (NLM Chemicals)},
      cin          = {IBT-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB56},
      pnm          = {Biotechnologie},
      pid          = {G:(DE-Juel1)FUEK410},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16319059},
      UT           = {WOS:000235128200070},
      doi          = {10.1074/jbc.M511826200},
      url          = {https://juser.fz-juelich.de/record/49189},
}