Fucosyltransferase 8. GDP-Fucose N-Glycan Core α6-Fucosyltransferase (FUT8)

  • Hideyuki Ihara
  • Hiroki Tsukamoto
  • Jianguo Gu
  • Eiji Miyoshi
  • Naoyuki Taniguchi
  • Yoshitaka Ikeda
Reference work entry


α1,6-Fucosylation of asparagine-linked oligosaccharides (N-glycans) is ubiquitously observed in eukaryote except plant and fungi. This type of fucosylation is catalyzed by eukaryotic α1,6-fucosyltransferase, and this enzyme is called as FUT8, notably in mammalian. FUT8 transfers fucose moiety from GDP-β-L-fucose to the innermost GlcNAc residue in N-glycan (Fig. 59.1). FUT8 was purified from porcine brain (Uozumi et al. 1996b) and MKN45 cells, a human gastric cancer cell line (Yanagidani et al. 1997). The cDNAs were successfully cloned from porcine and human (Uozumi et al. 1996b; Yanagidani et al. 1997). α1,6-Fucosylation catalyzed by FUT8 and the resulting α1,6-fucose residue is denoted as core fucosylation and core fucose, respectively.


MKN45 Cell Human Gastric Cancer Cell Line Porcine Brain Fucose Residue Terminal GlcNAc 
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.


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Copyright information

© Springer Japan 2014

Authors and Affiliations

  • Hideyuki Ihara
    • 1
  • Hiroki Tsukamoto
    • 1
  • Jianguo Gu
    • 2
  • Eiji Miyoshi
    • 3
  • Naoyuki Taniguchi
    • 4
  • Yoshitaka Ikeda
    • 1
  1. 1.Division of Molecular Cell Biology, Department of Biomolecular Sciences, Faculty of MedicineSaga UniversitySagaJapan
  2. 2.Division of Regulatory Glycobiology, Institute of Molecular Biomembrane and GlycobiologyTohoku Pharmaceutical UniversityAoba-kuJapan
  3. 3.Department of Molecular Biochemistry and Clinical InvestigationOsaka University Graduate School of MedicineSuitaJapan
  4. 4.Disease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Global Research ClusterRIKENWako, SaitamaJapan

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