CMP-NeuAc:Galβ1→4GlcNAc α2→6sialyltransferase catalyzes NeuAc transfer to glycolipids

Mitsuru Nakamura, Atsuko Tsunoda, Ken Yanagisawa, Yusuke Furukawa, Jiro Kikuchi, Satsuki Iwase, Takao Sakai, Göran Larson, Masaki Saito

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6 Citations (Scopus)


Using mammalian gene-overexpression system, in vitro catalytic activities of CMP-NeuAc:Galβ1→4GlcNAc α2→6sialyltransferase on glycosphingolipid acceptors were analyzed. We transfected the mammalian expression vector containing the cDNA that was cloned from Daudi cells into COS-1 cells, and selected monoclonal transfectants in the presence of G418. Although the transfectedα2→6sialyltransferase can catalyze NeuAc transfer onto glycoprotein acceptors more than glycolipids based on kinetic analyses, the substantial synthesis of IV6NeuAc-nLcOse4Cer was observed and the activities were 7-to 9-times higher in the transfected cells than in the mock transfectants. In addition, the transfected COS-1 cells with α2→6sialyltransferase cDNA were revealed to contain a higher amount of ganglioside that has the terminal NeuAcα2→6Gal sequence in the in situ situation than the mock transfectants. These results using transfectants, together with those using the purified enzyme protein, suggest that the α2→6sialyltransferase enzyme from Daudi cells can also catalyze NeuAc transfer in α2→6 linkage onto glycosphingolipid acceptors.

Original languageEnglish
Pages (from-to)1795-1806
Number of pages12
JournalJournal of Lipid Research
Issue number9
Publication statusPublished - 09-1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology
  • Cell Biology


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