Regulation of TRAIL-induced Cancer Cell Death by Fucosylated Glycans

抄録

Fucosylation is one of the most important types of glycosylation in cancer. The expression levels of fucosylated glycans generally increase during cancer development. Consequently, fucosylated molecules have been used as tumor markers. The synthesis of fucosylated glycans occurs through the catalytic activity of fucosyltransferases, which are enzymatic entities that orchestrate the transfer of fucose from GDP-fucose to acceptor substrates. Previously, we reported, for the first time, a deficiency in GDP-mannose 4,6-dehydratase (GMDS), an enzyme crucial for the generation of cellular GDP-fucose, in human cancer cells. This finding was followed by the discovery that fucosylated glycans regulate the susceptibility of cancer cells to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced cell death and natural killer (NK) cell-mediated tumor immune surveillance. In this review, we summarize a series of our studies and discuss the role of fucosylation in the regulation of cancer cell death.