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Gene Review

Fut1  -  fucosyltransferase 1

Mus musculus

Synonyms: Alpha(1,2)FT 1, Fucosyltransferase 1, GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1, Galactoside 2-alpha-L-fucosyltransferase 1, H transferase
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Disease relevance of Fut1


High impact information on Fut1


Biological context of Fut1


Anatomical context of Fut1

  • The alpha1,2-FT and alpha1, 3-FT mRNAs were located in both the inner cell mass and the trophoblast cells [9].
  • COS-7 cells transfected with MFUT-I and -II exhibited alpha1,2-fucosyltransferase activity and the best acceptor substrate for both gene products was GA1 to yield a fucosyl GA1 structure, but no activity was detected in COS-7 cells with MFUT-III [10].
  • GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase, MFUT-II, and not MFUT-I or -III, is induced in a restricted region of the digestive tract of germ-free mice by host-microbe interactions and cycloheximide [13].
  • In mice, selectin ligand activity regulating leukocyte recruitment and lymphocyte homing into lymph nodes results from the sum of unequal contributions of fucosyltransferase (FucT)-IV and FucT-VII, with FucT-VII playing a predominant role [14].
  • To find direct evidence for fucosylation and sorting signal into bile ducts, we used alpha1-6 fucosyltransferase (Fut8)-deficient mice because fucosylation of glycoproteins produced in mouse liver was mainly an alpha1-6 linkage [15].

Associations of Fut1 with chemical compounds

  • alpha1,6-Fucosyltransferase (Fut8) catalyzes the transfer of a fucose residue to N-linked oligosaccharides on glycoproteins by means of an alpha1,6-linkage to form core fucosylation in mammals [16].
  • In order to understand the enzymatic basis for the expression of Le(x) bearing glycolipids, we measured glycolipid, glycoprotein and oligosaccharide fucosyltransferase (Fuc-T) activities using appropriate substrates in P19 EC cells with or without RA treatment [17].
  • Consistent with the sequence similarity, the transfection of a 1,544 bp fragment under the control of the cytomegarovirus enhancer and beta actin promoter into COS-1 cells confers alpha-1,3 fucosyltransferase activity on the cells, resulting in cell surface expression of SSEA-1 [18].
  • Phenotype Changes of Fut8 Knockout Mouse: Core Fucosylation Is Crucial for the Function of Growth Factor Receptor(s) [16].
  • Moreover integrin-mediated cell signaling was reduced in Fut8(-/-) cells [11].

Regulatory relationships of Fut1

  • In addition, the expression of alpha1, 2-FT was differentially regulated and the uterine factor was not prerequisite of the expression of Ley [9].

Other interactions of Fut1

  • Northern blot analysis on total RNA showed a transient expression at day 4-6 of the Fut2 gene encoding a Fucalpha1-2 fucosyltransferase, probably responsible for the detected blood group H-type epitopes [19].
  • We therefore determined the activities of this fucosyltransferase and several other glycosyltransferases, which included UDP-GlcNAc:beta-D-Gal-beta 1,3-N-acetylglucosaminyltransferase, UDP-Gal:beta-D-GlcNAc-beta 1,4-galactosyltransferase, and GDP-Fuc:beta-D-GlcNAc-alpha 1,6-fucosyltransferase [20].
  • AIM: To study the influence of the expression of human alpha galactosidase and alpha1,2 fucosyltransferase on Gal alpha 1,3 Gal and consequent xenoreactivity in NIH3T3 cells [21].
  • Western blot studies of extracts from stably transfected CHO cells showed a band corresponding to the schistosome fucosyltransferase at 50 kDa, suggesting that the enzyme is indeed glycosylated [22].
  • RESULTS: Western blot showed that glycoproteins with molecular weight of 107 kDa, 98 kDa, 88 kDa, 56 kDa, 40 kDa, and 37 kDa were inhibited and even abrogated totally in alpha galactosidase transfectants and alpha 1,2 fucosyltransferase transfectants [21].

Analytical, diagnostic and therapeutic context of Fut1

  • We then investigated the two possible Fuc-T genes that might be responsible for these changes using RT-PCR analysis [17].
  • Southern blot analysis of genomic DNA indicated that this S. mansoni fucosyltransferase is the product of a single gene [22].
  • Here we present the molecular cloning and characterization of a fucosyltransferase of Schistosoma mansoni with a DNA sequence similarity of 84.6 and 63.7% to mouse and human fucosyltransferase type VII [22].
  • We further demonstrated the expression and enzymatic activity of the fucosyltransferase in the transfected cells by immunofluorescence studies and flow microfluorimetric analysis, which indicated that the enzyme is capable of synthesizing the SLeX blood group determinant but not the LeX determinant in CHO cells [22].
  • CONCLUSION: Although alpha galactosidase and alpha 1,2 fucosyltransferase had different biochemical properties, they could inhibit the expression of Gal alpha 1,3 Gal synergistically, leading to stronger resistance of xenograft against cytolysis [21].


  1. Coordinate expression of X and Y haptens during murine embryogenesis. Fenderson, B.A., Holmes, E.H., Fukushi, Y., Hakomori, S. Dev. Biol. (1986) [Pubmed]
  2. Down-regulation of trypsinogen expression is associated with growth retardation in {alpha}1,6-fucosyltransferase-deficient mice: attenuation of proteinase-activated receptor 2 activity. Li, W., Nakagawa, T., Koyama, N., Wang, X., Jin, J., Mizuno-Horikawa, Y., Gu, J., Miyoshi, E., Kato, I., Honke, K., Taniguchi, N., Kondo, A. Glycobiology (2006) [Pubmed]
  3. Redirection of tumor metastasis by expression of E-selectin in vivo. Biancone, L., Araki, M., Araki, K., Vassalli, P., Stamenkovic, I. J. Exp. Med. (1996) [Pubmed]
  4. The alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking through an essential role in L-, E-, and P-selectin ligand biosynthesis. Malý, P., Thall, A., Petryniak, B., Rogers, C.E., Smith, P.L., Marks, R.M., Kelly, R.J., Gersten, K.M., Cheng, G., Saunders, T.L., Camper, S.A., Camphausen, R.T., Sullivan, F.X., Isogai, Y., Hindsgaul, O., von Andrian, U.H., Lowe, J.B. Cell (1996) [Pubmed]
  5. A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase. Kukowska-Latallo, J.F., Larsen, R.D., Nair, R.P., Lowe, J.B. Genes Dev. (1990) [Pubmed]
  6. Specialized contributions by alpha(1,3)-fucosyltransferase-IV and FucT-VII during leukocyte rolling in dermal microvessels. Weninger, W., Ulfman, L.H., Cheng, G., Souchkova, N., Quackenbush, E.J., Lowe, J.B., von Andrian, U.H. Immunity (2000) [Pubmed]
  7. Enzymatic basis for a lectin-resistant phenotype: increase in a fucosyltransferase in mouse melanoma cells. Finne, J., Burger, M.M., Prieels, J.P. J. Cell Biol. (1982) [Pubmed]
  8. Normal embryonic and germ cell development in mice lacking alpha 1,3-fucosyltransferase IX (Fut9) which show disappearance of stage-specific embryonic antigen 1. Kudo, T., Kaneko, M., Iwasaki, H., Togayachi, A., Nishihara, S., Abe, K., Narimatsu, H. Mol. Cell. Biol. (2004) [Pubmed]
  9. Stage-specific expression of alpha1,2-fucosyltransferase and alpha1, 3-fucosyltransferase (FT) during mouse embryogenesis. Liu, N., Jin, C., Zhu, Z.M., Zhang, J., Tao, H., Ge, C., Yang, S., Zhang, S. Eur. J. Biochem. (1999) [Pubmed]
  10. Characterization of three members of murine alpha1,2-fucosyltransferases: change in the expression of the Se gene in the intestine of mice after administration of microbes. Lin, B., Saito, M., Sakakibara, Y., Hayashi, Y., Yanagisawa, M., Iwamori, M. Arch. Biochem. Biophys. (2001) [Pubmed]
  11. Deletion of Core Fucosylation on {alpha}3beta1 Integrin Down-regulates Its Functions. Zhao, Y., Itoh, S., Wang, X., Isaji, T., Miyoshi, E., Kariya, Y., Miyazaki, K., Kawasaki, N., Taniguchi, N., Gu, J. J. Biol. Chem. (2006) [Pubmed]
  12. Changes in cell surface glycosylation in alpha1,3-galactosyltransferase knockout and alpha1,2-fucosyltransferase transgenic mice. Shinkel, T.A., Chen, C.G., Salvaris, E., Henion, T.R., Barlow, H., Galili, U., Pearse, M.J., d'Apice, A.J. Transplantation (1997) [Pubmed]
  13. GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase, MFUT-II, and not MFUT-I or -III, is induced in a restricted region of the digestive tract of germ-free mice by host-microbe interactions and cycloheximide. Lin, B., Hayashi, Y., Saito, M., Sakakibara, Y., Yanagisawa, M., Iwamori, M. Biochim. Biophys. Acta (2000) [Pubmed]
  14. Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: role of human fucosyltransferase-IV and -VII. Martinez, M., Joffraud, M., Giraud, S., Baïsse, B., Bernimoulin, M.P., Schapira, M., Spertini, O. J. Biol. Chem. (2005) [Pubmed]
  15. Fucosylation of N-glycans regulates the secretion of hepatic glycoproteins into bile ducts. Nakagawa, T., Uozumi, N., Nakano, M., Mizuno-Horikawa, Y., Okuyama, N., Taguchi, T., Gu, J., Kondo, A., Taniguchi, N., Miyoshi, E. J. Biol. Chem. (2006) [Pubmed]
  16. Phenotype Changes of Fut8 Knockout Mouse: Core Fucosylation Is Crucial for the Function of Growth Factor Receptor(s). Wang, X., Gu, J., Miyoshi, E., Honke, K., Taniguchi, N. Meth. Enzymol. (2006) [Pubmed]
  17. Expression of glycoconjugates bearing the Lewis X epitope during neural differentiation of P19 EC cells. Osanai, T., Chai, W., Tajima, Y., Shimoda, Y., Sanai, Y., Yuen, C.T. FEBS Lett. (2001) [Pubmed]
  18. Molecular cloning and expression of a mouse alpha-1,3 fucosyltransferase gene that shows homology with the human alpha-1,3 fucosyltransferase IV gene. Ozawa, M., Muramatsu, T. J. Biochem. (1996) [Pubmed]
  19. Two glycosylation alterations of mouse intestinal mucins due to infection caused by the parasite Nippostrongylus brasiliensis. Holmén, J.M., Olson, F.J., Karlsson, H., Hansson, G.C. Glycoconj. J. (2002) [Pubmed]
  20. Retinoic acid-induced differentiation of the mouse teratocarcinoma cell line F9 is accompanied by an increase in the activity of UDP-galactose: beta-D-galactosyl-alpha 1,3-galactosyltransferase. Cummings, R.D., Mattox, S.A. J. Biol. Chem. (1988) [Pubmed]
  21. Human alpha galactosidase and alpha 1,2 fucosyltransferase concordantly inhibit xenoreactivity of NIH 3T3 cells with human serum. Yan, J.L., Yu, L.Y., Guo, L.H. Acta Pharmacol. Sin. (2003) [Pubmed]
  22. Molecular characterization of a fucosyltransferase encoded by Schistosoma mansoni. Marques, E.T., Weiss, J.B., Strand, M. Mol. Biochem. Parasitol. (1998) [Pubmed]
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