The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Biological Function of Fucosylation in Cancer Biology
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 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.
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Cites
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
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Malý, P., Thall, A. D., Petryniak, B., Rogers, C. E., Smith, P. L., Marks, R. M., Kelly, R. J., Gersten, K. M., Cheng, G., Saunders, T. L., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80137-3 · Cited by 714
Wang, X., Inoue, S., Gu, J., Miyoshi, E., Noda, K., Li, W., Mizuno-Horikawa, Y., Nakano, M., Asahi, M., Takahashi, M., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507375102 · Cited by 476
Self-citationCore Fucosylation Regulates Epidermal Growth Factor Receptor-mediated Intracellular Signaling
Wang, X., Gu, J., Ihara, H., Miyoshi, E., Honke, K., & Taniguchi, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510893200 · Cited by 323
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Cited by
Cell surface protein glycosylation in cancer
Christiansen, M. N., Chik, J., Lee, L., Anugraham, M., Abrahams, J. L., & Packer, N. H. (2014) · PROTEOMICS · doi:10.1002/pmic.201300387 · Cited by 518
High-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
Alley, W. R., Mann, B. F., & Novotny, M. V. (2013) · Chemical Reviews · doi:10.1021/cr3003714 · Cited by 310
Unmasking Fucosylation: from Cell Adhesion to Immune System Regulation and Diseases
Li, J., Hsu, H.-C., Mountz, J. D., & Allen, J. G. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.02.005 · Cited by 256
Milledge, J. J., Nielsen, B. V., & Bailey, D. (2016) · Reviews in Environmental Science and Bio/Technology · doi:10.1007/s11157-015-9381-7 · Cited by 193
Capillary Electrophoresis Separations of Glycans
Lu, G., Crihfield, C. L., Gattu, S., Veltri, L. M., & Holland, L. A. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00669 · Cited by 174
Metadata
- Authors
- Miyoshi, E., Moriwaki, K., & Nakagawa, T.
- Venue
- Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-11-16
- Volume
- 143
- Issue
- 6
- Pages
- 725-729
- ISSN
- 0021-924X (ISSN-L)
- OpenAlex
- W2132240438
- Cited by
- 395
- References
- 5
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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