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.
Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses
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Aristotelis Antonopoulos, Simon J. North, Stuart M. Haslam, Anne Dell; Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses. Biochem Soc Trans 1 October 2011; 39 (5): 1334–1340. doi: https://doi.org/10.1042/BST0391334
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