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  • Title: The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand.
    Author: Koszdin KL, Bowen BR.
    Journal: Biochem Biophys Res Commun; 1992 Aug 31; 187(1):152-7. PubMed ID: 1520296.
    Abstract:
    The polymerase chain reaction was used to amplify a novel fucosyltransferase cDNA (FucT-VI) from A431 and from HL60 cells. The amplified cDNA has a high degree of sequence identity to FucT-V and to FucT-III, and a much lower level of similarity to FucT-IV. Transfection of the FucT-VI gene into mammalian cells confers alpha-1,3 fucosyltransferase activity to the cells, resulting in cell surface expression of Lewis x and sialyl-Lewis x carbohydrates. In contrast to FucT-IV activity, FucT-VI catalyzes the transfer of fucose from GDP-beta-fucose to alpha-2,3 sialylated substrates. The substrate specificity of the FucT-VI gene product suggests that FucT-VI may be an enzyme involved in the biosynthesis of the E-Selectin ligand, sialyl-Lewis x, in myeloid cells.
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