N-Acetylglucosamine 6-O-Sulfotransferase

  • Kenji Uchimura
  • Takashi Muramatsu


6-O-Sulfation of GlcNAc is found not only in keratan sulfate but also in asparagine- linked and mucin-type glycans, such as thyroglobulin (Spiro and Bhoyroo 1988), human immunodeficiency virus envelope glycoprotein,gp120 (Shilatifard et al. 1993), respiratory mucosa mucin (Lo-Guidice et al. 1994), and GlyCAM-1, an endothelial ligand of the L-selectin, which is a cell-adhesion molecule implicated in lymphocyte homing to lymph nodes (Rosen 1999). N-Acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) was cloned in the mouse and humans (Uchimura et al. 1998b,c). The expressed enzyme transferred sulfate to nonreducing GlcNAc but not to internally located GlcNAc. This specificity is consistent with that of the enzyme previously reported (Spiro et al. 1996; Degroote et al. 1997). It has been concluded that the cloned GlcNAc6ST participates in synthesis of 6-sulfo sialyl Lewis X structure, suggesting that the enzyme is involved in formation of L-selectin ligand (Uchimura et al. 1998b; Kimura et al. 1999). cDNAs encoding various molecular species of GlcNAc6STs was cloned subsequently (Bistrup et al. 1999; Hiraoka et al. 1999; Lee et al. 1999).


Human Immunodeficiency Virus Type High Endothelial Venule Phospho Adenosine Endothelial Ligand mRNA AF131235 
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Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Kenji Uchimura
    • 1
  • Takashi Muramatsu
    • 1
  1. 1.Department of BiochemistryNagoya University School of MedicineNagoyaJapan

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