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Glycobiology Advance Access published online on December 8, 2005
Glycobiology, doi:10.1093/glycob/cwj067
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received May 6, 2005
Revised December 5, 2005
Accepted December 6, 2005

Article

Mass spectrometric approach for screening modifications of Total Serum N-Glycome in human diseases: application to cirrhosis

Willy Morelle 1, Christophe Flahaut 2, Jean-Claude Michalski 1, Alexandre Louvet 3, Philippe Mathurin 3, and André Klein 4 *

1 Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, IFR 118, Université des Sciences et Technologies de Lille 1, 59655 Villeneuve d’Ascq, France
2 Laboratoire de physiopathologie de la barrière hémato-encéphalique, E.A. 2465, IMPRT-IFR 114 Université d’Artois, rue Souvraz, SP18, 62307 Lens Cedex
3 Services d’Hépato-Gastroentérologie, Hôpital Huriez, CHRU Lille, France
4 Laboratoire de Biochimie et de Biologie Moléculaire, UAM de glycopathologies, Hôpital Calmette, CHRU Lille, Bld du Professeur Jules Leclerc, Lille 59037 Cedex, France; Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, IFR 118, Université des Sciences et Technologies de Lille 1, 59655 Villeneuve d’Ascq, France

* To whom correspondence should be addressed.
André Klein, E-mail: a-klein{at}chru-lille.fr


  Abstract

Congenital and acquired modifications of glycosylation in diseases are a rapidly growing field that demonstrates the importance of glycosylation in human biology. Unfortunately, in clinical biochemistry, very few tests are available to explore oligosaccharide metabolism on a large scale. Such an assay needs to be of high throughput, rapid, and preferentially non-invasive. In the present study, we describe a method to analyze qualitative variations of N-glycosylation of human serum proteins. The method is based on direct release of N-linked oligosaccharides from patient serum samples, a single step purification and a matrix assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometric analysis. A complementary structural study of the released oligosaccharides was achieved by enzymatic digestions, linkage analysis and electrospray ionization ion trap mass spectrometry (ESI-IT-MS) of the permethylated N-glycome. 26 oligosaccharides structures were individualised, their presence in human serum being the result of the combination of the biosynthesis and catabolic pathways. Application of the protocol to the serum of patients with cirrhosis demonstrates the ability of this assay to identify acquired modifications of glycosylation. Furthermore, we have analyzed the N-glycans and showed the increase in bisecting N-acetylglucosamine residue, core fucosylation and the presence of an important population of neutral oligosaccharides. The study of total serum N-glycome modifications is a preliminary for the discovery of new non-invasive diagnostic or prognostic biomarkers resulting of the variations of the N-glycans metabolism during diseases.

Keywords: Cirrhosis/Glycosylation disorders/mass spectrometry/N-glycan/N-glycome.
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