• Shou Takashima
  • Shuichi Tsuji


ST6GalNAc-III is a relatively small sialyltransferase (305 amino acids in length) compared with other sialyltransferases characterized to date. Like other sialyltransferases, ST6GalNAc-III exhibits type II membrane protein topology and has characteristic motifs for sialyltransferases called sialylmotifs L, S, and VS. ST6GalNAc-III-VI are the members of one ST6GalNAc subfamily that can synthesize the ganglioside GDIα from GM1b (Sjoberg et al. 1996; Lee et al. 1999; Okajima et al. 1999, 2000; Ikehara et al. 1999). GD1α has been implicated as a molecular component of a variety of important biological processes. The overall amino acid sequence identity of mouse ST6GalNAc- III is 94.4% to rat ST6GalNAc-III, 43.0% to mouse ST6GalNAc-IV, 42.6% to mouse ST6GalNAc-V, and 41.4% to mouse ST6GalNAc-VI, but ST6GalNAc-III shows no significant similarity to other sialyltransferases except in sialylmotifs. This ST6GalNAc subfamily (ST6GalNAc-III-VI) has been suggested to have a different domain structure to other sialyltransferases (Lee et al. 1999; Okajima et al. 1999, 2000; Ikehara et al. 1999). ST6GalNAc-III, -V, and -VI prefer glycolipids to O-glycans as substrates, while ST6GalNAc-IV prefers O-glycans to glycolipids. Each gene has different tissue- specific expression patterns, suggesting that there may be several tissue-specific ST6GalNAc members capable of synthesizing GD1α.


Sialic Acid Competitive Polymerase Chain Reaction Embryonal Carcinoma Cell Line Mouse Embryonal Carcinoma Cell Ganglioside GD1a 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Ikehara Y, Shimizu N, Kono M, Nishihara S, Nakanishi H, Kitamura T, Narimatsu H, Tsuji S, Tatematsu M (1999) A novel glycosyltransferase with a polyglutamine repeat: a new candidate for GD1α synthase (ST6GalNAc-V) FEBS Lett 463:92–96PubMedCrossRefGoogle Scholar
  2. Lee YC, Kaufmann M, Kitazume-Kawaguchi S, Kono M, Takashima S, Kurosawa N, Liu H, Pircher H, Tsuji S (1999) Molecular cloning and functional expression of two members of mouse NeuAcα2,3Galβ1,3GalNAc GalNAcα2,6-sialyltransferase family, ST6GalNAc-III and-IV. J Biol Chem 274:11958–11967PubMedCrossRefGoogle Scholar
  3. Okajima T, Fukumoto S, Ito H, Kiso M, Hirabayashi Y, Urano T, Furukawa K, Furukawa K (1999) Molecular cloning of brain-specific GD1α synthase (ST6GalNAc-V) containing CAG/glutamine repeats. J Biol Chem 274:30557–30562PubMedCrossRefGoogle Scholar
  4. Okajima T, Chen HH, Ito H, Kiso M, Tai T, Furukawa K, Urano T, Furukawa K (2000) Molecular cloning and expression of mouse GD1α/GT1aα/GQ1bα synthase (ST6GalNAc-VI) gene. J Biol Chem 275:6717–6723PubMedCrossRefGoogle Scholar
  5. Sjoberg ER, Kitagawa H, Glushka J, van Halbeek H, Paulson JC (1996) Molecular cloning of a developmentally regulated N-acetylgalactosamine α2,6-sialyltransferase specific for sialylated glycoconjugates. J Biol Chem 271:7450–7459PubMedCrossRefGoogle Scholar
  6. Takashima S, Kurosawa N, Tachida Y, Inoue M, Tsuji S (2000) Comparative analysis of the genomic structures and promoter activities of mouse Siaα2,3Galβ1,3GalNAc GalNAcα2,6-sialyltransferase genes (ST6GalNAc-III and-IV): characterization of their Sp1 binding sites. J Biochem 127:399–409PubMedCrossRefGoogle Scholar
  7. Tsuji S, Datta AK, Paulson JC (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6(7):v–viiPubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Shou Takashima
    • 1
  • Shuichi Tsuji
    • 2
  1. 1.Cellular Biochemistry LaboratoryInstitute of Physical and Chemical Research (RIKEN), WakoSaitamaJapan
  2. 2.Department of Chemistry, Faculty of ScienceOchanomizu University, Otsuka, Bunkyo-kuTokyoJapan

Personalised recommendations