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FUT7  -  fucosyltransferase 7 (alpha (1,3)...

Homo sapiens

Synonyms: Alpha-(1,3)-fucosyltransferase 7, Fuc-TVII, FucT-VII, Fucosyltransferase 7, Fucosyltransferase VII, ...
 
 
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High impact information on FUT7

  • Suppression of GATA-3 activity by dominant-negative GATA-3 or repressor of GATA (ROG) was necessary to attain a maximum expression of FUT7 and sialyl Lewis X in human T lymphoid cells [1].
  • We recently identified several individuals carrying a missense mutation (G329A; Arg(110)-Gln) in the FUT7 gene encoding fucosyltransferase VII [2].
  • It was found that PMN from both FUT7 homozygously and heterozygously mutated individuals exhibited an elevated expression of FUT4 mRNA compared with PMN from FUT7 nonmutated individuals [2].
  • No enzyme activity was measurable in expression studies in COS-7 cells using the mutated FUT7 construct [2].
  • Polymorphonuclear leukocytes from individuals carrying the G329A mutation in the alpha 1,3-fucosyltransferase VII gene (FUT7) roll on E- and P-selectins [2].
 

Biological context of FUT7

 

Anatomical context of FUT7

  • Enzymatic assays reveal that this cell line has normal alpha(2,3)sialyltransferase activity but is deficient in the alpha(1,3)fucosyltransferase responsible for biosynthesis of CD15s (FUT7) [6].
  • A cloned CD15s-negative variant of HL60 cells is deficient in expression of FUT7 and does not adhere to cytokine-stimulated endothelial cells [6].
  • 3. The last gene cloned (FUT7) encodes an alpha-3-fucosyltransferase expressed in leukocytes which synthesizes the sialyl Lĕ antigen, a selectin ligand [7].
  • The FUT7 mutation rate, which in tetrapod ancestors is about half that in amniote ancestors, may be related to the role of this gene in immune systems [8].
  • Characterization of EBV-transformed B-cells established from an individual homozygously mutated (G329A) in the FUT7 alpha1,3-fucosyltransferase gene [9].
 

Associations of FUT7 with chemical compounds

  • FUT7 could not transfer a fucose to an acceptor which is non-sialylated [10].
 

Other interactions of FUT7

  • The products of the monomorphic genes FUT4 and FUT7 seem implicated in cell-cell interactions during embryo-foetal development and in the leukocyte adhesion phenomena to endothelial cells in the adult [4].
  • These CHO-K1 cells have been previously transfected with the cDNA encoding Core2GlcNAc-T and/or FUT3 and/or FUT7 [11].

References

  1. Interaction of GATA-3/T-bet transcription factors regulates expression of sialyl Lewis X homing receptors on Th1/Th2 lymphocytes. Chen, G.Y., Osada, H., Santamaria-Babi, L.F., Kannagi, R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Polymorphonuclear leukocytes from individuals carrying the G329A mutation in the alpha 1,3-fucosyltransferase VII gene (FUT7) roll on E- and P-selectins. Bengtson, P., Lundblad, A., Larson, G., Påhlsson, P. J. Immunol. (2002) [Pubmed]
  3. Molecular genetics of H, Se, Lewis and other fucosyltransferase genes. Mollicone, R., Cailleau, A., Oriol, R. Transfusion clinique et biologique : journal de la Société française de transfusion sanguine. (1995) [Pubmed]
  4. Advances in molecular genetics of alpha-2- and alpha-3/4-fucosyltransferases. Costache, M., Cailleau, A., Fernandez-Mateos, P., Oriol, R., Mollicone, R. Transfusion clinique et biologique : journal de la Société française de transfusion sanguine. (1997) [Pubmed]
  5. Identification of a missense mutation (G329A;Arg(110)--> GLN) in the human FUT7 gene. Bengtson, P., Larson, C., Lundblad, A., Larson, G., Påhlsson, P. J. Biol. Chem. (2001) [Pubmed]
  6. A cloned CD15s-negative variant of HL60 cells is deficient in expression of FUT7 and does not adhere to cytokine-stimulated endothelial cells. Weston, B.W., Hiller, K.M., Mayben, J.P., Manousos, G., Nelson, C.M., Klein, M.B., Goodman, J.L. Eur. J. Haematol. (1999) [Pubmed]
  7. Fucosyltransferase genes are dispersed in the genome: FUT7 is located on 9q34.3 distal to D9S1830. Reguigne-Arnould, I., Wolfe, J., Hornigold, N., Fauré, S., Mollicone, R., Oriol, R., Coullin, P. C. R. Acad. Sci. III, Sci. Vie (1996) [Pubmed]
  8. En Bloc Duplications, Mutation Rates, and Densities of Amino Acid Changes Clarify the Evolution of Vertebrate alpha-1,3/4-Fucosyltransferases. Petit, D., Maftah, A., Julien, R., Petit, J.M. J. Mol. Evol. (2006) [Pubmed]
  9. Characterization of EBV-transformed B-cells established from an individual homozygously mutated (G329A) in the FUT7 alpha1,3-fucosyltransferase gene. Bengtson, P., Zetterberg, H., Mellberg, T., Påhlsson, P., Larson, G. Scand. J. Immunol. (2005) [Pubmed]
  10. Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue. Nishihara, S., Iwasaki, H., Kaneko, M., Tawada, A., Ito, M., Narimatsu, H. FEBS Lett. (1999) [Pubmed]
  11. The formation of the oncofetal J28 glycotope involves core-2 beta6-N-acetylglucosaminyltransferase and alpha3/4-fucosyltransferase activities. Panicot, L., Mas, E., Pasqualini, E., Zerfaoui, M., Lombardo, D., Sadoulet, M.O., El Battari, A. Glycobiology (1999) [Pubmed]
 
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