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ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 4 (ST6GALNAC4)

  • Shou Takashima
  • Shuichi Tsuji
Reference work entry

Abstract

ST6GalNAc-III, ST6GalNAc-IV, ST6GalNAc-V, and ST6GalNAc-VI are members of NeuAcα2-3Galβ1-3GalNAc α2,6-sialyltransferases. These members except ST6GalNAc-IV can efficiently synthesize the ganglioside GD1α from GM1b (Sjoberg et al. 1996; Lee et al. 1999; Okajima et al. 1999, 2000; Ikehara et al. 1999; Harduin-Lepers et al. 2000; Tsuchida et al. 2005; Ko et al. 2010). Compared with other members, ST6GalNAc-IV prefers O-linked glycans of glycoproteins to glycolipids as substrates. Therefore, ST6GalNAc-IV may be the main candidate for synthesizing the NeuAcα2-3Galβ1-3(NeuAcα2-6)GalNAc residue, which is usually found in the O-glycans. ST6GalNAc-IV is also considered to be involved in the early alteration of the sialylation pattern of cell surface molecules in activated lymphocytes (Kaufmann et al. 1999). Like ST6GalNAc-III, ST6GalNAc-IV is a relatively small sialyltransferase (302 amino acids in length for human, mouse, and pig enzymes) compared with other animal sialyltransferases because of the short stem region. However, isoforms of ST6GalNAc-IV with different amino acid length are also reported (350 and 360 amino acids in length for mouse isoforms). The overall amino acid sequence identity of mouse ST6GalNAc-IV is 88.4 % to human ST6GalNAc-IV, 86.1 % to pig ST6GalNAc-IV, 43.0 % to mouse ST6GalNAc-III, 44.8 % to mouse ST6GalNAc-V, and 41.2 % to mouse ST6GalNAc-VI, respectively, but ST6GalNAc-IV shows no significant similarity to other sialyltransferases except in sialylmotifs.

Keywords

Acceptor Substrate mRNA Differential Display Amino Acid Length GalNAc Residue Differential Display Polymerase Chain Reaction 
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.

References

  1. Harduin-Lepers A, Stokes DC, Steelant WFA, Samyn-Petit B, Krzewinski-Recchi MA, Vallejo-Ruiz V, Zanetta JP, Augé C, Delannoy P (2000) Cloning, expression and gene organization of a human Neu5Acα2-3Galβ1-3GalNAc α2,6-sialyltransferase: hST6GalNAc IV. Biochem J 352:37–48PubMedCrossRefGoogle Scholar
  2. Higai K, Ishihara S, Matsumoto K (2006) NFκB-p65 dependent transcriptional regulation of glycosyltransferases in human colon adenocarcinoma HT-29 by stimulation with tumor necrosis factor α. Biol Pharm Bull 29:2372–2377. doi:10.1248/bpb.29.2372PubMedCrossRefGoogle Scholar
  3. 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
  4. Kang NY, Park YD, Choi HJ, Kim KS, Lee YC, Kim CH (2004) Regulatory elements involved in transcription of the human NeuAcα2,3Galβ1,3GalNAcα2,6-sialyltransferase (hST6GalNAc IV) gene. Mol Cells 18:157–162PubMedGoogle Scholar
  5. Kaufmann M, Blaser C, Takashima S, Schwartz-Albiez R, Tsuji S, Pircher H (1999) Identification of an α2,6-sialyltransferase induced early after lymphocyte activation. Int Immunol 11:731–738. doi:10.1093/intimm/11.5.731PubMedCrossRefGoogle Scholar
  6. Kim SW, Kang NY, Lee SH, Kim KW, Kim KS, Lee JH, Kim CH, Lee YC (2003) Genomic structure and promoter analysis of human NeuAc α2,3Galβ1,3GalNAc α2,6-sialyltransferase (hST6GalNAc IV) gene. Gene 305:113–120. doi:10.1016/S0378-1119(02)01234-9PubMedCrossRefGoogle Scholar
  7. Kitazume-Kawaguchi S, Kabata S, Arita M (2001) Differential biosynthesis of polysialic or disialic acid structure by ST8Sia II and ST8Sia IV. J Biol Chem 276:15696–15703. doi:10.1074/jbc.M010371200PubMedCrossRefGoogle Scholar
  8. Ko HK, Song KH, Jin UH, Seong HH, Chang YC, Kim NH, Kim DS, Lee YC, Kim CH (2010) Molecular characterization of pig α2,3-Gal-β1,3-GalNAc-α2,6-sialyltransferase (pST6GalNAc IV) gene specific for Neu5Acα2-3Galβ1-3GalNAc trisaccharide structure. Glycoconj J 27:367–374. doi:10.1007/s10719-010-9284-3PubMedCrossRefGoogle Scholar
  9. 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 274:11958–11967. doi:10.1074/jbc.274.17.11958PubMedCrossRefGoogle Scholar
  10. 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 274:30557–30562. doi:10.1074/jbc.274.43.30557PubMedCrossRefGoogle Scholar
  11. 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 275:6717–6723. doi:10.1074/jbc.275.10.6717PubMedCrossRefGoogle Scholar
  12. 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 271:7450–7459. doi:10.1074/jbc.271.13.7450PubMedCrossRefGoogle Scholar
  13. Takashima S, Tsuji S (2011) Functional diversity of mammalian sialyltransferases. Trends Glycosci Glycotech 23:178–193. doi:10.4052/tigg.23.178CrossRefGoogle Scholar
  14. 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
  15. Tsuchida A, Ogiso M, Nakamura Y, Kiso M, Furukawa K, Furukawa K (2005) Molecular cloning and expression of human ST6GalNAc III: restricted tissue distribution and substrate specificity. J Biochem 138:237–243. doi:10.1093/jb/mvi124PubMedCrossRefGoogle Scholar
  16. Tsuji S, Datta AK, Paulson JC (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6(7):v–viiPubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.Laboratory of GlycobiologyThe Noguchi InstituteItabashiJapan
  2. 2.Institute of GlycoscienceTokai UniversityHiratsukaJapan

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