Roles of Fucosylation in Tumor Immunology

Kenta Moriwaki, Eiji Miyoshi
2010 Trends in glycoscience and glycotechnology  
The explosive progress of glycobiology in the past few decades has revealed that fucose is indispensable in various organisms and is involved in many biological events. Many researchers have spent a lot of time in order to unveil the mysterious functions of fucosylation. However, the findings which have ever been clarified are not sufficient to explain all fucosylation-related biological events. In the field of oncology, although several fucosylated molecules have been reported to be increased
more » ... n cancer and have been used as cancer biomarkers, it remains unknown how dynamic changes of fucosylation are associated with cancer biology. Recently, we found that fucosylation is involved in NK cell-mediated tumor immune surveillance through regulation of the susceptibility to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL), which is an apoptosis-inducing molecule. In this review, we describe the relationship between cancer biology and fucosylation, according to our recent findings. A. Introduction Glycosylation comprises the enzymatic attachment of sugars to biological macromolecules, such as proteins and lipids, and is one of the most important post-translational modifications. Fucose is a kind of monosaccharide that forms oligosaccharides through binding via glycosidic linkages. L-fucose is equivalent to 6-deoxy-L-galactose and exhibits two structural differences from other hexoses in mammals. One is the lack of a hydroxyl group on the carbon at the 6-position and the other is the L-configuration. Fucosylation is a reaction by which an L-fucose residue is attached to oligosaccharides on glycoproteins and glycolipids or proteins. Fucosylation can confer unique functional properties to oligosaccharides or proteins and is closely associated with various physiological events, including development, incompatible blood transfusion reaction, and leukocyte trafficking (1). In addition,
doi:10.4052/tigg.22.239 fatcat:xwyupl7jrreljocx6t7clyx53m