title: Functional roles of N-glycans in cell signaling and cell adhesion in cancer.
abstract: Glycosylation is one of the most common post-translational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structures are associated with many physiological and pathological events, including cell growth, migration, differentiation, tumor invasion, host-pathogen interactions, cell trafficking, and transmembrane signaling. Emerging roles of glycan functions have been highly attractive to scientists in various fields of life science as they open a field, "Functional Glycomics", that is a comprehensive study of the glycan structures in relation to functions. In particular, the N-glycans of signaling molecules including receptors or adhesion molecules are considered to be involved in cellular functions. This review will focus on the roles of glycosyltransferases involved in the biosynthesis of N-glycan branching and identification of cell surface receptors as their target proteins. We also suggest that the modulation of N-glycans of those receptors alters their important functions such as cell signaling and cell adhesion which are implicated in cancer invasion and metastasis.
authors.affiliation: Department of Disease Glycomics, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.
authors.forename: Yan-Yang
authors.initials: YY
authors.lastname: Zhao
authors.forename: Motoko
authors.initials: M
authors.lastname: Takahashi
authors.forename: Jian-Guo
authors.initials: JG
authors.lastname: Gu
authors.forename: Eiji
authors.initials: E
authors.lastname: Miyoshi
authors.forename: Akio
authors.initials: A
authors.lastname: Matsumoto
authors.forename: Shinobu
authors.initials: S
authors.lastname: Kitazume
authors.forename: Naoyuki
authors.initials: N
authors.lastname: Taniguchi
mesh_terms: D000818:Animals; D002448:Cell Adhesion; D066246:ErbB Receptors / Q000502:physiology; D005647:Fucosyltransferases / Q000502:physiology; D016695:Glycosyltransferases / Q000502:physiology*; D006801:Humans; D017351:N-Acetylglucosaminyltransferases / Q000502:physiology; D009361:Neoplasm Invasiveness; D009369:Neoplasms / Q000473:pathology*; D011134:Polysaccharides / Q000502:physiology*; D015398:Signal Transduction
chemical_list: D011134:Polysaccharides; D016695:Glycosyltransferases; D005647:Fucosyltransferases; D017351:N-Acetylglucosaminyltransferases; C054599:beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase; C052254:alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase; C020559:Glycoprotein 6-alpha-L-fucosyltransferase; D066246:ErbB Receptors