title: Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses.
abstract: N-glycans are key players mediating cell-cell communication in the immune system, interacting with glycan-binding proteins. In the present article, we discuss key themes that are emerging from the structural analysis of complex-type N-linked glycans from human and murine immune cell lines, employing high-sensitivity MALDI (matrix-assisted laser desorption ionization)-TOF (time-of-flight) MS technology. Particular focus is given to terminal epitopes, the abundance of multiply branched N-glycans and how glycosylation can affect human health in diseases such as congenital neutropenia and glycogen storage disease.
authors.affiliation: Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK. a.dell@imperial.ac.uk
authors.forename: Aristotelis
authors.initials: A
authors.lastname: Antonopoulos
authors.forename: Simon J
authors.initials: SJ
authors.lastname: North
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Haslam
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
mesh_terms: D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D000939:Epitopes / Q000737:chemistry; D006008:Glycogen Storage Disease / Q000276:immunology; D054794:Glycomics / Q000379:methods*; D006031:Glycosylation; D006801:Humans; D007107:Immune System / Q000502:physiology*; D008969:Molecular Sequence Data; D009503:Neutropenia / Q000151:congenital / Q000276:immunology; D009504:Neutrophils / Q000737:chemistry / Q000276:immunology; D011134:Polysaccharides / Q000737:chemistry*; D012680:Sensitivity and Specificity; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000939:Epitopes; D011134:Polysaccharides