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Enzymes for N-Glycan Branching and Their Genetic and Nongenetic Regulation in Cancer

Disease Glycomics Team, Systems Glycobiology Research Group, Global Research Cluster, RIKEN, Wako, 351-0198, Japan
Author to whom correspondence should be addressed.
Academic Editor: Franz-Georg Hanisch
Biomolecules 2016, 6(2), 25;
Received: 23 March 2016 / Revised: 15 April 2016 / Accepted: 21 April 2016 / Published: 28 April 2016
(This article belongs to the Special Issue Cancer and Glycosylation)
PDF [1541 KB, uploaded 28 April 2016]


N-glycan, a fundamental and versatile protein modification in mammals, plays critical roles in various physiological and pathological events including cancer progression. The formation of N-glycan branches catalyzed by specific N-acetylglucosaminyltransferases [GnT-III, GnT-IVs, GnT-V, GnT-IX (Vb)] and a fucosyltransferase, Fut8, provides functionally diverse N-glycosylated proteins. Aberrations of these branches are often found in cancer cells and are profoundly involved in cancer growth, invasion and metastasis. In this review, we focus on the GlcNAc and fucose branches of N-glycans and describe how their expression is dysregulated in cancer by genetic and nongenetic mechanisms including epigenetics and nucleotide sugar metabolisms. We also survey the roles that these N-glycans play in cancer progression and therapeutics. Finally, we discuss possible applications of our knowledge on basic glycobiology to the development of medicine and biomarkers for cancer therapy. View Full-Text
Keywords: cancer; fucose; GlcNAc; N-Glycan; glycosylation; glycosyltransferase cancer; fucose; GlcNAc; N-Glycan; glycosylation; glycosyltransferase

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Kizuka, Y.; Taniguchi, N. Enzymes for N-Glycan Branching and Their Genetic and Nongenetic Regulation in Cancer. Biomolecules 2016, 6, 25.

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