Advertisement

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 3 (ST3GAL3)

  • Ronald L. Schnaar
Reference work entry

Abstract

ST3Gal-III is a member of the N-acetyllactosaminide α-2,3-sialyltransferase family, transferring sialic acid from CMP-NeuAc in α-2,3 linkage preferentially to Galβ1-3GlcNAc, but also to Galβ1-4GlcNAc and Galβ1-3GalNAc termini on glycoproteins and glycolipids. It was among the first sialyltransferases purified and cloned (Wen et al. 1992), leading to the discovery of sialyltransferase sialyl motifs.

Keywords

Sialic Acid Intellectual Disability Brain Ganglioside Sialic Acid Analog Disaccharide Acceptor 
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. Audry M, Jeanneau C, Imberty A, Harduin-Lepers A, Delannoy P, Breton C (2011) Current trends in the structure-activity relationships of sialyltransferases. Glycobiology 21:716–726PubMedCrossRefGoogle Scholar
  2. Blixt O, Allin K, Bohorov O, Liu X, Andersson-Sand H, Hoffmann J, Razi N (2008) Glycan microarrays for screening sialyltransferase specificities. Glycoconj J 25:59–68PubMedCrossRefGoogle Scholar
  3. Crocker PR, Paulson JC, Varki A (2007) Siglecs and their roles in the immune system. Nat Rev Immunol 7:255–266PubMedCrossRefGoogle Scholar
  4. Ellies LG, Sperandio M, Underhill GH, Yousif J, Smith M, Priatel JJ, Kansas GS, Ley K, Marth JD (2002) Sialyltransferase specificity in selectin ligand formation. Blood 100:3618–3625PubMedCrossRefGoogle Scholar
  5. Grahn A, Barkhordar GS, Larson G (2002) Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues. Glycoconj J 19:197–210PubMedCrossRefGoogle Scholar
  6. Guo JP, Brummet ME, Myers AC, Na HJ, Rowland E, Schnaar RL, Zheng T, Zhu Z, Bochner BS (2011) Characterization of expression of glycan ligands for Siglec-F in normal mouse lungs. Am J Respir Cell Mol Biol 44:238–243PubMedCrossRefGoogle Scholar
  7. Harduin-Lepers A (2010) Comprehensive analysis of sialyltransferases in vertebrate genomes. Glycobiology Insights 2:29–61CrossRefGoogle Scholar
  8. Harduin-Lepers A, Krzewinski-Recchi MA, Colomb F, Foulquier F, Groux-Degroote S, Delannoy P (2012) Sialyltransferases functions in cancers. Front Biosci (Elite Ed) 4:499–515CrossRefGoogle Scholar
  9. Hu H, Eggers K, Chen W, Garshasbi M, Motazacker MM, Wrogemann K, Kahrizi K, Tzschach A, Hosseini M, Bahman I, Hucho T, Muhlenhoff M, Gerardy-Schahn R, Najmabadi H, Ropers HH, Kuss AW (2011) ST3GAL3 mutations impair the development of higher cognitive functions. Am J Hum Genet 89:407–414PubMedCentralPubMedCrossRefGoogle Scholar
  10. Ivannikova T, Bintein F, Malleron A, Juliant S, Cerutti M, Harduin-Lepers A, Delannoy P, Auge C, Lubineau A (2003) Recombinant (2-->3)-alpha-sialyltransferase immobilized on nickel-agarose for preparative synthesis of sialyl Lewis(x) and Lewis(a) precursor oligosaccharides. Carbohydr Res 338:1153–1161PubMedCrossRefGoogle Scholar
  11. Kitagawa H, Paulson JC (1994) Differential expression of five sialyltransferase genes in human tissues. J Biol Chem 269:17872–17878PubMedGoogle Scholar
  12. Kono M, Ohyama Y, Lee YC, Hamamoto T, Kojima N, Tsuji S (1997) Mouse beta-galactoside alpha 2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue specific expression. Glycobiology 7:469–479PubMedCrossRefGoogle Scholar
  13. Perez-Garay M, Arteta B, Pages L, de L R, de B C, Vidal-Vanaclocha F, Peracaula R (2010) Alpha2,3-sialyltransferase ST3Gal III modulates pancreatic cancer cell motility and adhesion in vitro and enhances its metastatic potential in vivo. PLoS One 5:e12524PubMedCentralPubMedCrossRefGoogle Scholar
  14. Rao FV, Rich JR, Rakic B, Buddai S, Schwartz MF, Johnson K, Bowe C, Wakarchuk WW, Defrees S, Withers SG, Strynadka NC (2009) Structural insight into mammalian sialyltransferases. Nat Struct Mol Biol 16:1186–1188PubMedCrossRefGoogle Scholar
  15. Ropers HH (2008) Genetics of intellectual disability. Curr Opin Genet Dev 18:241–250PubMedCrossRefGoogle Scholar
  16. Schnaar RL (2004) Glycolipid-mediated cell-cell recognition in inflammation and nerve regeneration. Arch Biochem Biophys 426:163–172PubMedCrossRefGoogle Scholar
  17. Sturgill ER, Aoki K, Lopez PH, Colacurcio D, Vajn K, Lorenzini I, Majiæ S, Yang WH, Heffer M, Tiemeyer M, Marth JD, Schnaar RL (2012) Biosynthesis of the major brain gangliosides GD1a and GT1b. Glycobiology 22:1289–1301PubMedCrossRefGoogle Scholar
  18. Tsuji S, Datta AK, Paulson JC (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6(7):v–viiPubMedCrossRefGoogle Scholar
  19. Weinstein J, de Souza-e-Silva, Paulson JC (1982a) Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver. J Biol Chem 257:13845–13853PubMedGoogle Scholar
  20. Weinstein J, de Souza-e-Silva U, Paulson JC (1982b) Purification of a Galb1-4GlcNAc a2-6sialyltransferase and a Galb1-3(4)GlcNAc a2-3 sialyltransferase to homogeneity from rat liver. J Biol Chem 257:13835–13844PubMedGoogle Scholar
  21. Wen DX, Livingston BD, Medzihradszky KF, Kelm S, Burlingame AL, Paulson JC (1992) Primary structure of Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family. J Biol Chem 267:21011–21019PubMedGoogle Scholar
  22. Zhang M, Angata T, Cho JY, Miller M, Broide DH, Varki A (2007) Defining the in vivo function of Siglec-F, a CD33-related Siglec expressed on mouse eosinophils. Blood 109:4280–4287PubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.Departments of Pharmacology and NeuroscienceJohns Hopkins University School of MedicineBaltimoreUSA

Personalised recommendations