Fucosylation is one of the most common modifications involving oligosaccharides on glycoproteins or glycolipids. Fucosylation comprises the attachment of a fucose residue to N-glycans, O-glycans, and glycolipids. O-Fucosylation, a special type of fucosylation, is very important for Notch signaling. The regulatory mechanisms for fucosylation are complicated. Many kinds of fucosyltransferases, the GDP-fucose synthesis pathway, and GDP-fucose transporter are involved in the regulation of fucosylation. Increased levels of fucosylation have been reported in a number of pathological conditions, including inflammation and cancer. Therefore, certain types of fucosylated glycoproteins such as AFP-L3 and several kinds of antibodies, which recognize fucosylated oligosaccharides such as sialyl Lewis a/x, have been used as tumor markers. Furthermore, fucosylation of glycoproteins regulates the biological functions of adhesion molecules and growth factor receptors. Changes in fucosylation could provide a novel strategy for cancer therapy. To determine levels of cellular fucosylation, lectin blot analyses using AAL (Aleuria aurantia lectin) and LCA (Lens culinaris agglutinin) are powerful tools.


Pancreatic Cancer Chronic Liver Disease Sugar Chain Human Gastric Cancer Cell Line Porcine Brain 
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© Springer 2008

Authors and Affiliations

  • Eiji Miyoshi
    • 1
  1. 1.Department of Molecular Biochemistry & Clinical InvestigationOsaka University Graduate School of MedicineSuita, OsakaJapan

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