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ST3Gal-IV

  • Shinobu Kitazume-Kawaguchi
  • Shuichi Tsuji

Abstract

ST3Gal-IV is a CMP-N-acetylneuraminate: β-galacotside α2-3-sialyltransferase (Galβ1-4(3)GlcNAc α2-3-sialyltransferase) (Tsuji et al. 1996). Expression cloning with cytotoxic lectin resistance selection has successfully isolated a cDNA encoding human ST3Gal-IV. ST3Gal-IV is a type II membrane protein, as are most other glycosyl- transferases. It has three conserved motifs, sialylmotif L, S, and VS, within the active domain. ST3Gal-IV also has a Kurosawa motif, as seen in the ST3Gal family and two members of the ST6GalNAc family (Tsuji 1999). ST3Gal-IV mainly catalyzes the α2- 3-sialylation of type II (Galβ1-4GlcNAc) sequence in N-linked glycan chains. Subsequent α1-3-fucosylation to the GlcNAc residue results in the formation of sialyl Lewis X, which is recognized by the selectin family, cell adhesion molecules. ST3Gal-IV also catalyzes the α2-3-sialylation of a type I (Galβ1-3GlcNAc) sequence in N-linked glycan chains. In contrast, ST3Gal-III prefers a type I sequence to a type II sequence. Both enzymes rarely utilize a glycolipid such as paragloboside (Galβ1-4GlcNAcβ1-3Galβ1- 4Glc-Cer).

Keywords

Expression Cloning Acceptor Substrate GlcNAc Residue Namalwa Cell Ricinus Communis Agglutinin 
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 2002

Authors and Affiliations

  • Shinobu Kitazume-Kawaguchi
    • 1
  • Shuichi Tsuji
    • 2
  1. 1.Frontier Research ProgramRIKEN InstituteSaitamaJapan
  2. 2.Department of Chemistry, Faculty of ScienceOchanomizu University, Otsuka, Bunkyo-kuTokyoJapan

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