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Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells

  • Milan Raska
  • Zina Moldoveanu
  • Hitoshi Suzuki
  • Rhubell Brown
  • Rose Kulhavy
  • Judit Andrasi
  • Stacy Hall
  • Huong L Vu
  • Fredric Carlsson
  • Gunnar Lindahl
  • Milan Tomana
  • Bruce A Julian
  • Robert J Wyatt
  • Jiri Mestecky
  • Jan Novak
Publishing year: 2007
Language: English
Pages: 69-78
Publication/Series: Journal of Molecular Biology
Volume: 369
Issue: 1
Document type: Journal article
Publisher: Elsevier

Abstract english

Glycosylation defects occur in several human diseases. In IgA nephropathy, IgA1 contains O-glycans that are galactose-deficient and consist mostly of core 1 alpha2,6 sialylated N-acetylgalactosamine, a configuration suspected to prevent beta1,3 galactosylation. We confirmed the same aberrancy in IgA1 secreted by the human DAKIKI B cell line. Biochemical assays indicated CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase activity in this cell line. However, a candidate enzyme, ST6-GalNAcI, was not transcribed in DAKIKI cells, B cells isolated from blood, or Epstein-Barr virus (EBV)-immortalized IgA1-producing cells from the blood of IgAN patients and healthy controls. Instead, ST6-GalNAcII transcription was detected at a high level. Expression of the ST6-GalNAcII gene and activity of the CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase were higher in IgA1-producing cell lines from IgAN patients than in such cells from healthy controls. These data are the first evidence that human cells that lack ST6-GalNAcI can sialylate core 1 GalNAc-Ser/Thr.


  • Microbiology in the medical area


  • ISSN: 1089-8638
E-mail: fredric [dot] carlsson [at] biol [dot] lu [dot] se

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