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.
Subject(s)
Glycomics/methods , Immune System/physiology , Polysaccharides/chemistry , Animals , Carbohydrate Conformation , Carbohydrate Sequence , Cell Line , Epitopes/chemistry , Glycogen Storage Disease/immunology , Glycosylation , Humans , Molecular Sequence Data , Neutropenia/congenital , Neutropenia/immunology , Neutrophils/chemistry , Neutrophils/immunology , Sensitivity and Specificity , Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationABSTRACT
Antisera against Lafora bodies were made in rabbits by subcutaneous injection of the myocardium from a patient died of Lafora disease. Using this antisera, immunohistochemistry revealed that corpora amylacea, the basophilic degeneration of myocardium and deposits of type IV glycogenosis contained the materials which were antigenically common to Lafora bodies.
