The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand.
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.
Koszdin
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CIBA-GEIGY Corp., Summit, NJ 07901.
Bowen
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D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry / Q000235:genetics; D005647:Fucosyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D014162:Transfection
D007527:Isoenzymes; D004247:DNA; D005647:Fucosyltransferases; C031692:galactoside 3-fucosyltransferase