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Fucosyltransferase 5

FUT5, Fuc-TV, fucosyltransferase V
Top mentioned proteins: fucosyltransferase, FUT6, Alpha-1, ACID, CAN
Papers on FUT5
Inflammatory cytokines regulate the expression of glycosyltransferases involved in the biosynthesis of tumor-associated sialylated glycans in pancreatic cancer cell lines.
Peracaula et al., Girona, Spain. In Cytokine, Sep 2015
In addition, variation in the mRNA expression of sialyltransferase (ST) and fucosyltransferase (FUT) genes, which codify for the ST and FucT enzymes involved in the carbohydrate antigens' biosynthesis, was determined.
Variation at ABO histo-blood group and FUT loci and diffuse and intestinal gastric cancer risk in a European population.
González et al., Barcelona, Spain. In Int J Cancer, Mar 2015
were associated with diffuse-type GC; however, conditional models with other ABO variants indicated that the associations were largely due to allelic blood group A. One variant in FUT5 was also associated with diffuse-type GC, and four variants (and haplotypes) in FUT2 (Se), FUT3 (Le) and FUT6 with intestinal-type GC.
Virus-induced appearance of the selectin ligand sLeX in herpes simplex virus type 1-infected T-cells: involvement of host and viral factors.
Olofsson et al., Göteborg, Sweden. In Glycobiology, 2013
In CD3+ cells, derived from peripheral blood mononuclear cells, HSV1 infection induced expression of FUT3, FUT5 and FUT6, whereas FUT7 was not altered.
[Distribution specificity of human fucosyltransferase 5 and its expression and localization in spermatids].
Pang et al., Shenyang, China. In Fa Yi Xue Za Zhi, 2012
OBJECTIVE: To investigate distribution specificity of human fucosyltransferase 5 (FUT5) as well as its expression and localization in spermatids.
Down-regulation of FUT3 and FUT5 by shRNA alters Lewis antigens expression and reduces the adhesion capacities of gastric cancer cells.
de Bolós et al., Barcelona, Spain. In Biochim Biophys Acta, 2011
down-regulation of FUT3 and FUT5 reduces the expression of sialyl-Lewis antigens and the adhesion capacities of gastric cancer cells and allows to identify the specific alpha1-3,4 fucosyltransferases implicated in the Lewis antigens synthesis
Regulation of glycosyltransferases and Lewis antigens expression by IL-1β and IL-6 in human gastric cancer cells.
de Bolós et al., Barcelona, Spain. In Glycoconj J, 2011
IL-1β induced significant increases in the mRNA levels of FUT1, FUT2 and FUT4, and decreases of FUT3 and FUT5.
The biosynthesis of the selectin-ligand sialyl Lewis x in colorectal cancer tissues is regulated by fucosyltransferase VI and can be inhibited by an RNA interference-based approach.
Dall'olio et al., Varese, Italy. In Int J Biochem Cell Biol, 2011
We found that: (i) in colon cancer, but not in normal mucosa where the antigen was poorly expressed, sLex correlated with a Fuc-T which, like Fuc-TVI, was active on 3'sialyllactosamine at a low concentration (Fuc-T(SLN)); (ii) competitive RT-PCR analysis revealed that the level of Fuc-T mRNA expression in both normal and cancer colon was Fuc-TVI>Fuc-TIII>Fuc-TIV; Fuc-TV and Fuc-TVII expression was negligible; (iii) sLex was expressed only by the gastrointestinal cell lines displaying both Fuc-TVI mRNA and Fuc-T(SLN) activity, but not by those expressing only Fuc-TIII mRNA; (iv) transfection with Fuc-TVI cDNA, but not with Fuc-TIII cDNA, induced sLex expression in gastrointestinal cell lines; (v) Fuc-TVI knock-down with specific siRNA induced down-regulation of Fuc-TVI mRNA and Fuc-T(SLN) activity and a dramatic inhibition of sLex expression.
An efficient approach to the discovery of potent inhibitors against glycosyltransferases.
Nishimura et al., Sapporo, Japan. In J Med Chem, 2010
Versatility of this strategy was demonstrated by identification of two selective inhibitors for human recombinant alpha1,3-fucosyltransferase V (alpha1,3-FucT, K(i) = 293 nM) and alpha1,6-fucosyltransferase VIII (alpha1,6-FucT, K(i) = 13.8 microM).
[The genetic diversity in the full coding region of human FUT5 gene in a Chinese Han population].
Pang et al., Shenyang, China. In Zhonghua Yi Xue Yi Chuan Xue Za Zhi, 2010
OBJECTIVE: To reveal the sequence variations of the full coding region of the human alpha (1,beta/1,4) fucosyltransferase 5 gene (FUT5) in a Chinese Han population.
Inhibition of protein deacetylation augments herpes simplex virus type 1-activated transcription of host fucosyltransferase genes associated with virus-induced sLex expression.
Olofsson et al., Göteborg, Sweden. In Arch Virol, 2010
Herpes simplex virus type 1 induces expression of the selectin ligand sialyl Lewis X in infected cells by activating transcription of three normally silent host glycosyltransferase genes, FUT3, FUT5, and FUT6, a process that is initiated by binding of viral RNA to cellular protein kinase R. We investigated the involvement of protein deacetylation and promoter methylation in viral activation of host FUT genes by analysing the effects of appropriate inhibitors on the transcription rates of the FUT genes in virus-infected cells.
Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells.
Reis et al., Porto, Portugal. In Int J Biochem Cell Biol, 2010
The final glycosylation step in sialyl Lewis x and sialyl Lewis a biosynthesis in MKN45 cell line was shown to be associated to FUT5, which efficiently fucosylated sialyl Lewis precursors on glycoproteins.
Induction of sialyl-Lex expression by herpes simplex virus type 1 is dependent on viral immediate early RNA-activated transcription of host fucosyltransferase genes.
Olofsson et al., Göteborg, Sweden. In Glycobiology, 2009
We have previously shown that varicella-zoster virus (VZV) and cytomegalovirus (CMV) infection of diploid human fibroblasts (HEL) results in neo-expression of Lewis antigens sialyl Lewis x (sLe(x)) and Lewis y (Le(y)), respectively, after transcriptional activation of different combinations of dormant human fucosyltransferase genes (FUT1, FUT3, FUT5, and FUT6), whose gene products are responsible for the synthesis of Le antigens.
Activation of host antiviral RNA-sensing factors necessary for herpes simplex virus type 1-activated transcription of host cell fucosyltransferase genes FUT3, FUT5, and FUT6 and subsequent expression of sLe(x) in virus-infected cells.
Olofsson et al., Göteborg, Sweden. In Glycobiology, 2009
results suggested that PKR is the primary target for HSV-1 early RNA during induction of FUT3, FUT5, and FUT6
Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding.
Yeung et al., Hong Kong, Hong Kong. In J Cell Sci, 2007
FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and glycodelin-A inhibits spermatozoa-zona binding by blocking the binding of sperm FUT5 to the zona pellucida
Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells.
Fukuda et al., Sendai, Japan. In Int J Cancer, 2004
Prostatic cancer cell transfected with this enzyme adhered to prostatic stromal cells in vitro with higher affinity than mock-transfected cancer cells.
Advances in molecular genetics of alpha-2- and alpha-3/4-fucosyltransferases.
Mollicone et al., Villejuif, France. In Transfus Clin Biol, 1997
Polymorphic genes FUT1-FUT2 and FUT3-FUT5-FUT6 are organized in two clusters and each gene is partially or totally inactivated by different types of point mutations (nonsense, missense and frame shift), complete gene deletion or a fusion gene.
Molecular genetics of H, Se, Lewis and other fucosyltransferase genes.
Oriol et al., Villejuif, France. In Transfus Clin Biol, 1994
The alpha-3-fucosyltransferases: FUT3 (Lewis) of exocrine secretions; FUT4 (myeloid) of white cells and brain; FUT5 whose tissue distribution has not been defined as yet; FUT6 (plasma) present in plasma, renal proximal tubules and hepatocytes; FUT7 (leukocyte) found in neutrophils.
Molecular genetics of alpha-L-fucosyltransferase genes (H, Se, Le, FUT4, FUT5 and FUT6).
Oriol et al., Villejuif, France. In Transfus Clin Biol, 1993
FUT3, FUT4, FUT5 and FUT6 encode different alpha(1,3)fucosyltransferases which share between 60 and 90% homology with each other, but none with FUT1.
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