Disease relevance of FUT5

• By applying these procedures, it was shown that the transcription of FUT5 was increased by 50-fold 5-24h after HSV-1 infection and 200-fold by the inhibition of viral DNA replication in HSV-infected cells [1].
• We detected transcripts of the fucosyltransferases Fuc-TIII and Fuc-TV in 4 melanoma cell lines despite the absence of cell surface sialyl-Le(x) [2].
• Interestingly, all of the 12 glycosyltransferase genes examined, except the Fuc-TV, Fuc-TVI, Fuc-TVII, and ST3Gal III genes, were markedly up-regulated in all of the poorly differentiated carcinomas [3].

High impact information on FUT5

• Transfection of the fucosyltransferases Fuc-TIII, Fuc-TIV, and Fuc-TV mediates cell surface expression of sialyl-Le(x) in many cell lines [2].
• The Fuc-TV reactivity of free LNB resembled that of LNBbeta1-3'R of a polylactosamine, contrasting strongly with the dissimilarity of the reactivities of the analogous pair of LN and LNbeta1-3'R [4].
• Coding region sequence analysis and alpha(1,3)Fuc-T acceptor specificity comparisons with recombinant human Fuc-TV and Fuc-TVI showed that the cloned FUT gene is orthologous to the human FUT6 gene [5].
• At the equivalent position, a tryptophan was found in FUT3-encoded Lewis alpha1,3/1,4-fucosyltransferase (Fuc-TIII) and FUT5-encoded alpha1,3/1,4-fucosyltransferase, the only fucosyltransferases that can also transfer fucose in alpha1, 4-linkage [6].
• In Northern blot analyses, no transcripts of Fuc-TIII, Fuc-TV, or Fuc-TVI were detected in total RNA from mature granulocytes or mRNA from HL-60 cells before or after differentiation [7].

Biological context of FUT5

• Two polyadenylation sites were shown for FUT5, but absence of consensus sequences suggests reduced efficiency for cleavage and polyadenylation [8].
• Polymorphic markers of FUT3, FUT5, and FUT6 were used for linkage analysis with 14 Généthon microsatellites in Indonesian families [9].
• The enzyme shares 85% amino acid sequence identity with Fuc-TIII and 89% identity with Fuc-TV but differs substantially in its acceptor substrate requirements [10].
• Polymerase chain reaction analyses demonstrate that the gene is syntenic to Fuc-TIII and Fuc-TV on chromosome 19 [10].
• Fuc-TIII and Fuc-TV showed very similar patterns of sLe(x) positive bands, which indicated that the enzymes have similar acceptor substrate specificities [11].

Anatomical context of FUT5

• The enzyme in COS cell extracts acting on unsialylated Type 2 structures is closely similar in its properties to the alpha1,3-fucosyltransferase encoded by human FUT4 gene and does not resemble the product of the FUT5 gene [12].
• The equilibrium dissociation constant of sperm FUT5 binding to solubilized zona pellucida was 42.82 pmol/ml [13].
• Biologically active FUT5 was purified from spermatozoa [13].
• Flow cytometric analysis of HeLa cells and Namalwa cells again demonstrated the similar specificities of Fuc-TIII and Fuc-TV [11].
• In HT-29 cells as well as in normal or malignant colonic tissues Fuc-TIII, Fuc-TIV, Fuc-TVI but not Fuc-TV nor Fuc-TVII were detectable after RT-PCR [14].

Associations of FUT5 with chemical compounds

• Thin layer chromatography immunostaining revealed that FucT-IV preferred the distal GlcNAc residue in nLc6Cer, whereas Fuc-TV preferred the proximal Gl-cNAc residue [15].
• Fuc-TIII and Fuc-TV catalyzed fucose transfer exclusively to OH-3 of glucose in lacto-N-neotetraose and lacto-N-tetraose, respectively, as was demonstrated by 1H NMR spectroscopy [15].
• Unexpectedly, chimeric Fuc-TV exhibited a GDP-fucose hydrolyzing activity [15].
• Compound 1 (stachybotrydial) exhibits potent inhibitory activity against alpha1,3-fucosyltransferase (Fuc-TV) during screening, while compounds 2 and 3 show no such inhibitory activity [16].
• We have synthesized the sialyl-Lewisx tetrasaccharide by total enzymatic synthesis from N-acetyllactosamine using a placental alpha 2-->3-sialyltransferase specific for type-2 chain acceptors, followed by a cloned human alpha 1-->3-fucosyltransferase (FucTV, the 'plasma-type' enzyme) [17].

Other interactions of FUT5

• FUT3 and FUT6 were expressed at high levels, while FUT5 expression was lower and restricted to fewer cell types [8].
• The levels of RNA encoded by beta-actin or GAPDH were found to vary by several orders of magnitude during HSV-1 infection, introducing large errors in the estimation of the gB-1 and FUT5 RNA levels [1].

Analytical, diagnostic and therapeutic context of FUT5

• Co-immunoprecipitation confirmed the interaction between glycodelin-A and sperm FUT5 [13].
• Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated [18].

References