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  • Fuc-TIII  (2)
  • Springer  (2)
  • American Association for the Advancement of Science
  • 1995-1999  (2)
  • 1960-1964
  • 1935-1939
  • 1920-1924
Collection
Keywords
Publisher
  • Springer  (2)
  • American Association for the Advancement of Science
Years
  • 1995-1999  (2)
  • 1960-1964
  • 1935-1939
  • 1920-1924
Year
  • 1
    Electronic Resource
    Electronic Resource
    Murine monoclonal antibody recognizing human α(1,3/1,4)fucosyltransferase (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 802-812 
    Details
    ISSN: 1573-4986
    Keywords: monoclonal antibody ; α(1,3/1,4)fucosyltransferase ; Fuc-TIII ; Lewis type enzyme ; sialyl Lewis a ; sLea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We prepared a mouse monoclonal antibody, FTA1-16, that specifically recognizes human α(1,3/1,4)fucosyltransferase without crossreactivity to any other members of the α(1,3)fucosyltransferase family. The specificity was confirmed by both immunofluorescense staining of native antigens in the Golgi apparatus and Western blotting analysis, using stable transformant cells transfected with each gene of the α(1,3)fucosyltransferase family. Western blotting analysis on a series of human tumour cell lines from various tissues revealed that some epithelial cancer cell lines from digestive organs expressed an amount of α(1,3/1,4)fucosyltransferase in good correlation with expression of sialyl Lewis a antigen. Immunohistochemical staining by FTA1-16 on colon cancer tissues revealed enhanced expression of the enzyme in cancer cells in comparison to normal cells. Finally, the antigenic epitope recognized by FTA1-16 was determined using truncated recombinant peptides which were expressed inE. coli. A minimal length determined was a fragment, amino acid positions 132–153, of the α(1,3/1,4)fucosyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731242
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  • 2
    Electronic Resource
    Electronic Resource
    Significance of each of three missense mutations, G484A, G667A, and G808A, present in an inactive allele of the human Lewis gene (FUT3) for α(1,3/1,4)fucosyltransferase inactivation (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 961-967 
    Details
    ISSN: 1573-4986
    Keywords: α(1,3/1,4)fucosyltransferase ; Fuc-TIII ; Lewis-negative allele ; Chimera ; Mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Recently, we found three novel missense mutations, G484A (Asp162Asn), G667A (Gly223Arg), and G808A (Val270Met), present in a Lewis-negative allele (le484,667,808) from an African (Xhosa) population. To define the relative contribution of each of the three mutations in the le484,667,808 allele for inactivation of the FUT3-encoded enzyme, we made chimeric FUT3 containing each of the three mutations. A transient expression study indicated that COS7 cells transfected with the FUT3 construct containing the G484A mutation expressed the Lewis antigen and had about 20% enzyme activity as compared with COS7 cells transfected with the wild type FUT3 allele, whereas COS7 cells transfected with the FUT3 construct containing either the G667A mutation or the G808A mutation did not express the Lewis antigen and showed no detectable α(1,3/1,4)fucosyltransferase activity. These results suggest that the G667A and/or the G808A missense mutations of FUT3 alleles are responsible for the inactivation of the FUT3-encoded enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006981724233
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