Fucosyltransferase 7. GDP-Fucose Lactosamine α1,3-Fucosyltransferase. Sialyl-Lex Specific (FUT7)

  • Takashi Kudo
  • Hisashi Narimatsu
Reference work entry


α1,3-Fucosyltransferase-IV (FUT7, Fuc-TVII) was cloned independently by two groups at almost the same time (Natsuka et al. 1994; Sasaki et al. 1994). Sasaki et al. first cloned the FUT7 cDNA from a THP-1 cell cDNA library by an expression cloning method using an anti-sLex mAb KM93. Natsuka et al. employed a cross-hybridization method for cloning the FUT7 cDNA. Flow cytometric analysis on the cells stably expressing FUT7 demonstrated that FUT7 can form sLex but not Lex on the cell surface. FUT7 can transfer fucose only to the GlcNAc residue of the sialylated type-2 chain but not to that of type-1 chain. Thus, FUT7 can synthesize only the sLex epitope and not the other Lewis antigens such as Lex, Lea, Leb, and sLea. The tissue distribution of FUT7 is limited to leukocytes and high-endothelial venules (HEV) (Clarke et al. 1996; Kaneko et al. 1999; Le Marer et al. 1997; Maly et al. 1996).


GlcNAc Residue Leukocyte Adhesion Deficiency Lewis Antigen Selectin Ligand FUT7 Expression 
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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.University of TsukubaTsukubaJapan
  2. 2.Research Center for Medical GlycoscienceNational Institute of Advanced Industrial Science and Technology (AIST)TsukubaJapan

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