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Updated: Jul 8, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Biological function of fucosylation in cancer biology
Eiji Miyoshi1, Kenta Moriwaki, Tsutomu Nakagawa
1Department of Molecular Biochemistry & Clinical Investigation, Osaka University Graduate School of Medicine, 1-7, Yamada-oka, Suita, 565-0871, Japan. emiyoshi@sahs.med.osaka-u.ac.jp
Abstract:
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, which is a special type of fucosylation, is very important for Notch signalling. 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 or several kinds of antibodies, which recognize fucosylated oligosaccharides such as sialyl Lewis a/x, have been used as tumour 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. In this review, the biological significance of and regulatory pathway for fucosylation have been described.
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