Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for alpha 2,8-sialyltransferase activity toward N-linked oligosaccharides

FEBS Lett. 1995 Feb 20;360(1):1-4. doi: 10.1016/0014-5793(95)00059-i.


We have detected sialyltransferase activity of recombinant mouse STX, which was cloned from rat brain as a new member of the sialyltransferase family, but sialyltransferase activity of which had not been detected previously [Livingston and Paulson, J. Biol. Chem. (1993) 268, 11504-11507]. The activity of mouse STX was specific toward sialylated glycoproteins. N-Glycanase treatment and linkage-specific sialidase treatment of glycoproteins revealed that STX transfers sialic acids through alpha 2,8-linkages to only N-linked oligosaccharides of glycoproteins. However, polymerase activity for polysialic acid synthesis was not detected for this sialyltransferase. Since this alpha 2,8-sialyltransferase gene is highly restricted in fetal and newborn brain, it may be involved in the polysialylation of glycoproteins, especially of N-CAM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Gene Expression Regulation, Enzymologic*
  • Mice
  • Molecular Sequence Data
  • Oligosaccharides / metabolism*
  • Sialyltransferases / genetics
  • Sialyltransferases / metabolism*


  • DNA, Complementary
  • Oligosaccharides
  • Sialyltransferases

Associated data

  • GENBANK/X83562