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Glycobiology Advance Access originally published online on May 28, 2003
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Glycobiology, 2003, Vol. 13, No. 9 601-622
© 2003 Oxford University Press

Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis

Michael Butler2, D. Quelhas3, Alison J. Critchley2, Hubert Carchon4, Holger F. Hebestreit2, Richard G. Hibbert2, Laura Vilarinho3, E. Teles5, Gert Matthijs6, Els Schollen6, Pablo Argibay2, David J. Harvey2, Raymond A. Dwek2, Jaak Jaeken4 and Pauline M. Rudd1,2

2 The Glycobiology Institute, Department of Biochemistry, Oxford University, South Parks Road, Oxford, OX1 3QU, U.K.
3 Medical Genetics Institute, Clinical Biology Department, Praça Pedro Nunes, 88, 4050 Porto, Portugal
4 Centre for Metabolic Disease, University of Leuven, Leuven, Belgium
5 Hospital S. João, Pediatrics Department, Porto, Portugal
6 Center for Human Genetics, University Hospital Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium

Received on January 15, 2003; revised on April 2, 2003; accepted on May 1, 2003

The fundamental importance of correct protein glycosylation is abundantly clear in a group of diseases known as congenital disorders of glycosylation (CDGs). In these diseases, many biological functions are compromised, giving rise to a wide range of severe clinical conditions. By performing detailed analyses of the total serum glycoproteins as well as isolated transferrin and IgG, we have directly correlated aberrant glycosylation with a faulty glycosylation processing step. In one patient the complete absence of complex type sugars was consistent with ablation of GlcNAcTase II activity. In another CDG type II patient, the identification of specific hybrid sugars suggested that the defective processing step was cell type–specific and involved the mannosidase III pathway. In each case, complementary serum proteome analyses revealed significant changes in some 31 glycoproteins, including components of the complement system. This biochemical approach to charting diseases that involve alterations in glycan processing provides a rapid indicator of the nature, severity, and cell type specificity of the suboptimal glycan processing steps; allows links to genetic mutations; indicates the expression levels of proteins; and gives insight into the pathways affected in the disease process.

1 To whom correspondence should be addressed; e-mail: pmr{at}glycob.ox.ac.uk


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