Biological function of fucosylation in cancer biology.
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.
Miyoshi
Eiji
E
Department 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
Moriwaki
Kenta
K
Nakagawa
Tsutomu
T
D000818:Animals; D005643:Fucose / Q000378:metabolism*; D005647:Fucosyltransferases / Q000502:physiology*; D006801:Humans; D009369:Neoplasms / Q000378:metabolism*
D005643:Fucose; D005647:Fucosyltransferases