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Fucosylation is the process of transferring fucose from GDP-fucose to their substrates, which includes certain proteins, N- and O-linked glycans in glycoprotein or glycolipids, by fucosyltransferases in all mammalian cells. Fucosylated glycans play vital role in selectin-mediated leukocyte extravasation, lymphocyte homing, and pathogen-host interactions, whereas fucosylated proteins are essential for signaling transduction in numerous ontogenic events. Aberrant fucosylation due to the availability of high energy donor GDP-fucose, abnormal expression of FUTs and/or α-fucosidase, and the availability of their substrates leads to different fucosylated glycan or protein structures. Accumulating evidence demonstrates that aberrant fucosylation plays important role in all aspects of cancer biology. In this review, we will summarize the current knowledge about fucosylation in different physiological and pathological processes with a focus on their roles not only in cancer cell proliferation, invasion, and metastasis but also in tumor immune surveillance. Furthermore, the clinical potential and applications of fucosylation in cancer diagnosis and treatment will also be discussed.
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| http://dx.doi.org/10.1016/bs.pmbts.2019.01.002 | DOI Listing |
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Article Synopsis
- Aberrant glycosylation is a key feature of cancer, but the specific glycogenes involved in esophageal squamous cell carcinoma (ESCC) remain largely unidentified, prompting this research.
- The study utilized various methods, including genomic analysis and experiments on cell proliferation and metastasis, to evaluate the impact of the glycogenes POFUT1 and RPN1 in ESCC.
- Results showed that increased expression of POFUT1 and RPN1 correlates with worse patient outcomes and enhanced cancer progression, with POFUT1 influencing migration through the Notch signaling pathway, suggesting both glycogenes as potential targets for cancer treatment in ESCC.
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