Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses. (21st September 2011)

• Record Type: Journal Article
• Authors: Antonopoulos, Aristotelis; North, Simon J.; Haslam, Stuart M.; Dell, Anne
• Is Part Of: Biochemical Society transactions. Volume 39:Number 5(2011)
• Page Start: 1334
• Page End: 1340
• Publication Date: 2011-09-21
• Subjects: congenital disorder of glycosylation -- congenital neutropenia -- glycogen storage disease 1b (GSD 1b) -- mass spectrometry -- matrix-assisted laser-desorption ionization–time-of-flight (MALDI–TOF) -- N-glycan; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0391334
• Languages: English
• ISSNs: 0300-5127

Abstract

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.