Abstract
Mouse α1,3-fucosyltransferase-IX (Fuc-TIX, Fut9) has been cloned as the sixth member of the α1,3-fucosyltransferase family by an expression cloning method for a mouse brain cDNA library (Kudo et al. 1998). The nucleotide and amino acid sequences of human α1,3-fucosyltransferase-IX (FUT9) are highly conserved in comparison with those of mouse Fut9, indicating that α1,3-fucosyltransferase-IX had been under a strong selective pressure during its evolution (Kaneko et al. 1999). The other five α1,3FUTs (FUT3, 4, 5, 6, and 7) share a highly homologous sequence, whereas the FUT9 amino acid sequence shows the lowest homology with other α1,3FUTs. FUT9 exhibited very strong activity for the Lewis x (Lex: Galβ1-4(Fucα1-3)GlcNAc) and Lewis y (Ley: Fucα1-2Galβ1-4(Fucα1-3)GlcNAc) synthesis, but not for the synthesis of sialyl Lewis x epitope (sLex: Siaα2-3Galβ1-4(Fucα1-3)GlcNAc). Moreover, FUT9 has more efficient activity for synthesis of the Lex carbohydrate epitope than other α1,3FUTs (Nishihara et al. 1999).
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Buffone A Jr, Mondal N, Gupta R, McHugh KP, Lau JT, Neelamegham S (2013) Silencing α1,3-fucosyltransferases in human leukocytes reveals a role for FUT9 enzyme during E-selectin-mediated cell adhesion. J Biol Chem 288:1620–1633
Comelli EM, Head SR, Gilmartin T, Whisenant T, Haslam SM, North SJ, Wong NK, Kudo T, Narimatsu H, Esko JD, Drickamer K, Dell A, Paulson JC (2006) A focused microarray approach to functional glycomics: transcriptional regulation of the glycome. Glycobiology 16:117–131
Ge Z, Chan NW, Palcic MM, Taylor DE (1997) Cloning and heterologous expression of an α1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori. J Biol Chem 272:21357–21363
Gouveia R, Schaffer L, Papp S, Grammel N, Kandzia S, Head SR, Kleene R, Schachner M, Conradt HS, Costa J (2012) Expression of glycogenes in differentiating human NT2N neurons. Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels and impaired neurite outgrowth. Biochim Biophys Acta 1820:2007–2019
Hennen E, Safina D, Haussmann U, Worsdorfer P, Edenhofer F, Poetsch A, Faissner A (2013) A LewisX-glycoprotein screen identifies the low density lipoprotein receptor-related protein 1 (LRP1) as a modulator of oligodendrogenesis in mice. J Biol Chem 288(23):16538–16545
Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H (1999) α1,3-Fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. FEBS Lett 452:237–242
Kudo T, Ikehara Y, Togayachi A, Kaneko M, Hiraga T, Sasaki K, Narimatsu H (1998) Expression cloning and characterization of a novel murine α1, 3-fucosyltransferase, mFuc-TIX, that synthesizes the Lewis x (CD15) epitope in brain and kidney. J Biol Chem 273:26729–26738
Kudo T, Kaneko M, Iwasaki H, Togayachi A, Nishihara S, Abe K, Narimatsu H (2004) Normal embryonic and germ cell development in mice lacking α1,3-fucosyltransferase IX (Fut9) which show disappearance of stage-specific embryonic antigen 1. Mol Cell Biol 24:4221–4228
Kudo T, Fujii T, Ikegami S, Inokuchi K, Takayama Y, Ikehara Y, Nishihara S, Togayachi A, Takahashi S, Tachibana K, Yuasa S, Narimatsu H (2007) Mice lacking α1,3-fucosyltransferase IX demonstrate disappearance of Lewis x structure in brain and increased anxiety-like behaviors. Glycobiology 17:1–9
Mollicone R, Gibaud A, Francois A, Ratcliffe M, Oriol R (1990) Acceptor specificity and tissue distribution of three human α-3-fucosyltransferases. Eur J Biochem 191:169–176
Nishihara S, Iwasaki H, Kaneko M, Tawada A, Ito M, Narimatsu H (1999) α1,3-Fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four α1,3FUT members preferentially fucosylate the inner GlcNAc residue. FEBS Lett 462:289–294
Nishihara S, Iwasaki H, Nakajima K, Togayachi A, Ikehara Y, Kudo T, Kushi Y, Furuya A, Shitara K, Narimatsu H (2003) α1,3-Fucosyltransferase IX (Fut9) determines Lewis X expression in brain. Glycobiology 13:445–455
Osanai T, Chai W, Tajima Y, Shimoda Y, Sanai Y, Yuen CT (2001) Expression of glycoconjugates bearing the Lewis X epitope during neural differentiation of P19 EC cells. FEBS Lett 488:23–28
Seelhorst K, Stacke C, Ziegelmuller P, Hahn U (2013) N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity. Glycobiology 23:559–567
Sikora M, Ferrer-Admetlla A, Laayouni H, Menendez C, Mayor A, Bardaji A, Sigauque B, Mandomando I, Alonso PL, Bertranpetit J, Casals F (2009) A variant in the gene FUT9 is associated with susceptibility to placental malaria infection. Hum Mol Genet 18:3136–3144
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Japan
About this entry
Cite this entry
Kudo, T., Narimatsu, H. (2014). Fucosyltransferase 9. GDP-Fucose Lactosamine α1,3-Fucosyltransferase. Lex Specific (FUT9). 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_97
Download citation
DOI: https://doi.org/10.1007/978-4-431-54240-7_97
Published:
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-54239-1
Online ISBN: 978-4-431-54240-7
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences