Skip to main content

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 6 (ST3GAL6)

  • Reference work entry
  • First Online:
Handbook of Glycosyltransferases and Related Genes

Abstract

ST3Gal6 (Uniprot ID: Q11203) is a member of the sialyltransferase family that transfers sialic acid from the activated cytidine 5′-monophospho-N-acetylneuraminic acid to terminal galactose on glycolipids (gangliosides) or the N- or O-linked sugar chains of glycoproteins in α2,3 linkage. ST3Gal6 has high specificity for neolactotetraosylceramide (paragloboside) and neolactohexaosylceramide as glycosphingolipid substrates and contributes to the formation of sialyl type II lactosamine and thereby Sialyl-Lewis X, a tetrasaccharide carbohydrate important for selectin-mediated cell adhesion and a blood group antigen.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 799.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 549.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Chachadi VB, Cheng H, Klinkebiel D, Christman JK, Cheng PW (2011) 5-Aza-2′-deoxycytidine increases Sialyl Lewis X on MUC1 by stimulating β-galactoside α2,3-sialyltransferase 6 Gene. Int J Biochem Cell Biol 43:586–593

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  • Okajima T, Fukumoto S, Miyazaki H, Ishida H, Kiso M, Furukawa K, Urano T, Furukawa K (1999) Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J Biol Chem 274:11479–11486

    Article  CAS  PubMed  Google Scholar 

  • Souady J, Hülsewig M, Distler U, Haier J, Denz A, Pilarsky C, Senninger N, Dreisewerd K, Peter-Katalinic J, Müthing J (2011) Differences in CD75s- and iso-CD75s-ganglioside content and altered mRNA expression of sialyltransferases ST6GAL1 and ST3GAL6 in human hepatocellular carcinomas and nontumoral liver tissues. Glycobiology 21:584–594

    Article  CAS  PubMed  Google Scholar 

  • Taniguchi A, Kaneta R, Morishita K, Matsumoto K (2001) Gene structure and transcriptional regulation of human Gal β1,4(3) GlcNAc α2,3-sialyltransferase VI (hST3Gal VI) gene in prostate cancer cell line. Biochem Biophys Res Commun 287:1148–1156

    Article  CAS  PubMed  Google Scholar 

  • Yang WH, Nussbaum C, Grewal PK, Marth JD, Sperandio M (2012) Coordinated roles of ST3Gal-VI and ST3Gal-IV sialyltransferases in the synthesis of selectin ligands. Blood 120:1015–1026

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Tetsuya Okajima .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2014 Springer Japan

About this entry

Cite this entry

Okajima, T., Furukawa, K. (2014). ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 6 (ST3GAL6). In: Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (eds) Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54240-7_35

Download citation

Publish with us

Policies and ethics