Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT6gene.[1][2][3]
The alpha-1,3-fucosyltransferases constitute a large family of glycosyltransferases with a high degree of homology. The enzymes of this family comprise 3 main activity patterns called myeloid, plasma, and Lewis, based on their capacity to transfer alpha-L-fucose to distinct oligosaccharide acceptors, their sensitivity to N-ethylmaleimide inhibition, their cation requirements, and their tissue-specific expression patterns. The different categories of alpha-1,3-fucosyltransferases are sequentially expressed during embryo-fetal development.[supplied by OMIM][3]
References
↑Koszdin KL, Bowen BR (Oct 1992). "The cloning and expression of a human alpha-1,3 fucosyltransferase capable of forming the E-selectin ligand". Biochem Biophys Res Commun. 187 (1): 152–7. doi:10.1016/S0006-291X(05)81472-X. PMID1520296.
↑McCurley RS, Recinos A III, Olsen AS, Gingrich JC, Szczepaniak D, Cameron HS, Krauss R, Weston BW (Jul 1995). "Physical maps of human alpha (1,3)fucosyltransferase genes FUT3-FUT6 on chromosomes 19p13.3 and 11q21". Genomics. 26 (1): 142–6. doi:10.1016/0888-7543(95)80094-3. PMID7782074.
Weston BW, Smith PL, Kelly RJ, Lowe JB (1992). "Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes". J. Biol. Chem. 267 (34): 24575–84. PMID1339443.
Cameron HS, Szczepaniak D, Weston BW (1995). "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms". J. Biol. Chem. 270 (34): 20112–22. doi:10.1074/jbc.270.34.20112. PMID7650030.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Mollicone R, Reguigne I, Fletcher A, et al. (1994). "Molecular basis for plasma alpha(1,3)-fucosyltransferase gene deficiency (FUT6)". J. Biol. Chem. 269 (17): 12662–71. PMID8175676.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Borsig L, Imbach T, Höchli M, Berger EG (2000). "alpha1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with beta1,4galactosyltransferase I in the golgi apparatus and monensin-induced swollen vesicles". Glycobiology. 9 (11): 1273–80. doi:10.1093/glycob/9.11.1273. PMID10536043.
Kamińska J, Musielak M, Nowicka A, et al. (2001). "Neutrophils promote the release of alpha-6-fucosyltransferase from blood platelets through the action of cathepsin G and elastase". Biochimie. 83 (8): 739–42. doi:10.1016/S0300-9084(01)01306-2. PMID11530205.
Roos C, Kolmer M, Mattila P, Renkonen R (2002). "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". J. Biol. Chem. 277 (5): 3168–75. doi:10.1074/jbc.M107927200. PMID11698403.
Kanoh A, Ota M, Narimatsu H, Irimura T (2003). "Expression levels of FUT6 gene transfected into human colon carcinoma cells switch two sialyl-Lewis X-related carbohydrate antigens with distinct properties in cell adhesion". Biochem. Biophys. Res. Commun. 303 (3): 896–901. doi:10.1016/S0006-291X(03)00420-0. PMID12670495.
Martinez-Duncker I, Michalski JC, Bauvy C, et al. (2004). "Activity and tissue distribution of splice variants of alpha6-fucosyltransferase in human embryogenesis". Glycobiology. 14 (1): 13–25. doi:10.1093/glycob/cwh006. PMID14514715.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Higai K, Miyazaki N, Azuma Y, Matsumoto K (2007). "Interleukin-1beta induces sialyl Lewis X on hepatocellular carcinoma HuH-7 cells via enhanced expression of ST3Gal IV and FUT VI gene". FEBS Lett. 580 (26): 6069–75. doi:10.1016/j.febslet.2006.09.073. PMID17054948.