Biology:Fucosyltransferase 3

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Short description: Protein and coding gene in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Galactoside 3(4)-L-fucosyltransferase is an enzyme that in humans is encoded by the FUT3 gene.[1][2][3]

Function

The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.[3]

See also

References

  1. ↑ "A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase". Genes & Development 4 (8): 1288–303. Aug 1990. doi:10.1101/gad.4.8.1288. PMID 1977660. 
  2. ↑ "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities". The Journal of Biological Chemistry 267 (6): 4152–60. Feb 1992. doi:10.1016/S0021-9258(19)50641-X. PMID 1740457. 
  3. ↑ 3.0 3.1 "Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525. 

Further reading

  • "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms". The Journal of Biological Chemistry 270 (34): 20112–22. Aug 1995. doi:10.1074/jbc.270.34.20112. PMID 7650030. 
  • "Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19". Cytogenetics and Cell Genetics 71 (2): 158–62. 1995. doi:10.1159/000134098. PMID 7656588. 
  • "Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19". Biochemical and Biophysical Research Communications 190 (1): 42–6. Jan 1993. doi:10.1006/bbrc.1993.1008. PMID 7916594. 
  • "Molecular genetic analysis of the human Lewis histo-blood group system". The Journal of Biological Chemistry 269 (46): 29271–8. Nov 1994. doi:10.1016/S0021-9258(19)62041-7. PMID 7961897. 
  • "Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees". The Journal of Biological Chemistry 269 (33): 20987–94. Aug 1994. doi:10.1016/S0021-9258(17)31919-1. PMID 8063716. 
  • "Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals". Blood 82 (9): 2915–9. Nov 1993. doi:10.1182/blood.V82.9.2915.2915. PMID 8219240. 
  • "Genotypic heterogeneity among Lewis negative individuals". Biochemical and Biophysical Research Communications 196 (2): 515–20. Oct 1993. doi:10.1006/bbrc.1993.2280. PMID 8240322. 
  • "Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals". Biochemical and Biophysical Research Communications 196 (2): 624–31. Oct 1993. doi:10.1006/bbrc.1993.2295. PMID 8240337. 
  • "DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system". Vox Sanguinis 70 (2): 97–103. 1996. doi:10.1111/j.1423-0410.1996.tb01300.x. PMID 8801770. 
  • "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. Sep 1996. doi:10.1101/gr.6.9.791. PMID 8889548. 
  • "Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels". The Journal of Biological Chemistry 271 (50): 32260–8. Dec 1996. doi:10.1074/jbc.271.50.32260. PMID 8943285. 
  • "Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII". The Journal of Biological Chemistry 272 (35): 21994–8. Aug 1997. doi:10.1074/jbc.272.35.21994. PMID 9268337. 
  • "Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa". Human Genetics 102 (6): 675–80. Jun 1998. doi:10.1007/s004390050760. PMID 9703429. 
  • "Molecular behavior of mutant Lewis enzymes in vivo". Glycobiology 9 (4): 373–82. Apr 1999. doi:10.1093/glycob/9.4.373. PMID 10089211. 
  • "Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia". Experimental and Clinical Immunogenetics 16 (3): 125–30. 1999. doi:10.1159/000019104. PMID 10394050. 
  • "Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites". The Journal of Biological Chemistry 275 (32): 24237–45. Aug 2000. doi:10.1074/jbc.M000888200. PMID 10816554. 
  • "Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples". Human Mutation 18 (4): 358–9. Oct 2001. doi:10.1002/humu.1204. PMID 11668626. 
  • "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". The Journal of Biological Chemistry 277 (5): 3168–75. Feb 2002. doi:10.1074/jbc.M107927200. PMID 11698403. 

External links



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