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Journal of Biochemistry Advance Access first published online on January 24, 2008
This version published online on January 30, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn011
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© 2008 The Japanese Biochemical Society

JB Minireview

Biological Function of Fucosylation in Cancer Biology

Eiji Miyoshi, Kenta Moriwaki and Tsutomu Nakagawa

Department of Molecular Biochemistry & Clinical Investigation, Osaka University Graduate School of Medicine, 1-7, Yamada-oka, Suita, 565-0871

Correspondence : Dr. Eiji Miyoshi: Department of Molecular Biochemistry & Clinical Investigation, Osaka University Graduate School of Medicine, 1-7, Yamada-oka, Suita, 565-0871 Tel: +81-6-6879-2590, Fax: +81-6-6879-2590, E-mail: emiyoshi{at}sahs.med.osaka-u.ac.jp

Received November 15, 2007; Accepted November 22, 2007


  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 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 or 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. In this review, the biological significance of and regulatory pathway for fucosylation have been described.

Key Words: fucosylation, HCC, AFP-L3, fucosyltransferase, GDP-fucose


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