Article

Overexpression of fucosyltransferase IV in A431 cell line increases cell proliferation.

Department of Biochemistry and Molecular Biology, Dalian Medical University, Liaoning Provincial Core Lab of Glycobiology and Glycoengineering, Dalian 116027, PR China.
The International Journal of Biochemistry & Cell Biology (impact factor: 4.63). 02/2007; 39(9):1722-30. DOI:10.1016/j.biocel.2007.04.024 pp.1722-30
Source: PubMed

ABSTRACT Fucosyltransferase IV is an essential enzyme that catalyzes the synthesis of fucosylated oligosaccharides by transferring GDP-fucose to the terminal N-acetylglucosamine with the alpha1,3-linkage. Lewis Y oligosaccharide has a terminal alpha1,3-linked fucose residue and elevation of Lewis Y level is seen in many epithelial cancers. The mechanism of Lewis Y elevation in neoplastic cells is still largely unknown. To study the impact of fucosyltransferase IV on Lewis Y expression and its role on neoplastic cell proliferation, a pEGFP-N1-FUT4 recombinant plasmid was developed and stably transfected into A431 cells. We found that fucosyltransferase IV overexpression promoted cell proliferation and increased the expression of proliferating cell nuclear antigen that correlated with Lewis Y augmentation. Cell cycle analysis demonstrated that fucosyltransferase IV overexpression facilitated cell cycle progression. In conclusion, fucosyltransferase IV overexpression augments Lewis Y expression to trigger neoplastic cell proliferation. These studies suggest that fucosyltransferase IV may serve as a potential therapeutic target for the treatment of Lewis Y-positive epithelial cancers.

0 0
 · 
0 Bookmarks
 · 
33 Views
  • Source
    Article: Functional analysis of α1,3/4-fucosyltransferase VI in human hepatocellular carcinoma cells.
    Qiya Guo, Bin Guo, Yingming Wang, Jun Wu, Wenjun Jiang, Shenan Zhao, Shouyi Qiao, Yanhua Wu
    [show abstract] [hide abstract]
    ABSTRACT: The α1,3/4-fucosyltransferases (FUT) subfamily are key enzymes in cell surface antigen synthesis during various biological processes. A novel role of FUTs in tumorigenesis has been discovered recently, however, the underlying mechanism remains largely unknown. Here, we characterized FUT6, a member of α1,3/4-FUT subfamily, in human hepatocellular carcinoma (HCC). In HCC tissues, the expression levels of FUT6 and its catalytic product SLe(x) were significantly up-regulated. Overexpression of FUT6 in HCC cells enhanced S-phase cell population, promoted cell growth and colony formation ability. Moreover, subcutaneously injection of FUT6-overexpressing cells in nude mice promoted cell growth in vivo. In addition, elevating FUT6 expression markedly induced intracellular Akt phosphorylation, and suppressed the expression of the cyclin-dependent kinases inhibitor p21. Bath application of the PI3K inhibitor blocked FUT6-induced Akt phosphorylation, p21 suppression and cell proliferation. Our results suggest that FUT6 plays an important role in HCC growth by regulating the PI3K/Akt signaling pathway.
    Biochemical and Biophysical Research Communications 12/2011; 417(1):311-7. · 2.48 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.

Keywords

Cell cycle analysis
 
epithelial cancers
 
essential enzyme
 
fucosylated oligosaccharides
 
fucosyltransferase IV overexpression
 
fucosyltransferase IV overexpression augments Lewis Y expression
 
fucosyltransferase IV overexpression facilitated cell cycle progression
 
Lewis Y augmentation
 
Lewis Y elevation
 
Lewis Y expression
 
Lewis Y level
 
Lewis Y oligosaccharide
 
Lewis Y-positive epithelial cancers
 
neoplastic cell proliferation
 
pEGFP-N1-FUT4 recombinant plasmid
 
potential therapeutic target
 
proliferating cell nuclear antigen
 
stably transfected
 
terminal alpha1,3-linked fucose residue
 
terminal N-acetylglucosamine