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).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Basu M, De T, Das KK, Kyte JW, Chon H, Schaeper RJ, Basu S (1987) Glycolipids. Methods Enzymol 138:575–607
Basu S (1991) The serendipity of ganglioside biosynthesis: pathway to CARS and HY-CARS glycosyltransferases. Glycobiology 1:469–475
Kitagawa H, Paulson JC (1994a) Cloning of a novel α2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J Biol Chem 269:1394–1401
Kitagawa H, Paulson JC (1994b) Differential expression of five sialyltransferase genes in human tissues. J Biol Chem 269:17872–17878
Kitagawa H, Mattei M-G, Paulson JC (1996) Genomic organization and chromosomal mapping of the Galβ1,3GlcNAc/Galβ1,4GlcNAc α2,3-sialyltransferase. J Biol Chem 271:931–938
Kono M, Ohyama Y, Lee YC, Hamamoto T, Kojima N, Tsuji S (1997) Mouse β-galactoside α2,3-sialyltransferases: comparison of in vitro substrate specificities and tissue-specific expression. Glycobiology 7:469–479
Priatel JJ, Chui D, Hiraoka N, Simmons CJ, Richardson KB, Page DM, Fukuda M, Varki NM, Marth JD (2000) The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte home-ostasis by modulating O-glycan biosynthesis. Immunity 12:273–283
Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M (1993) Expression cloning of a novel Galβ(1-3/1-4)GlcNAc-α2,3-sialyltransferase using lectin resistance selection. J Biol Chem 268:22782–22787
Takashima S, Tsuji S (2000) Comparison of genomic structures of four members of mouse β-galactoside α2,3-sialyltransferase genes. Cytogenet Cell Genet 89:101–106
Takashima S, Tachida Y, Nakagawa T, Hamamoto T, Tsuji S (1999) Quantitative analysis of expression of mouse sialyltransferase genes by competitive PCR. Biochem Biophys Res Commun 260:23–27
Tsuji S (1999) Molecular cloning and characterization of sialyltransferases. In: Inoue Y, Lee YC, Troy FA (eds) Sialobiology and other novel forms of glycosylation. Gakushin, Osaka, pp 145–154
Tsuji S, Datta AK, Paulson JC (1996) Systematic nomenclature for sialyltransferases. Glycobiology 6(7):v–vii
Weinstein J, de Souza-s-Silva U, Paulson JC (1982) Sialylation of glycoprotein oligosaccha-rides N-linked to asparagine. J Biol Chem 257:13845–13853
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Japan
About this chapter
Cite this chapter
Kitazume-Kawaguchi, S., Tsuji, S. (2002). ST3Gal-IV. In: Taniguchi, N., et al. Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-67877-9_38
Download citation
DOI: https://doi.org/10.1007/978-4-431-67877-9_38
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-67996-7
Online ISBN: 978-4-431-67877-9
eBook Packages: Springer Book Archive