Glycobiology Advance Access originally published online on January 22, 2003
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Glycobiology, 2003, Vol. 13, No. 5 367-375
© 2003 Oxford University Press
Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I
2 Department of Molecular Biomedical Research, Ghent University and Flanders Interuniversity Institute for Biotechnology, K.l.-ledeganckstraat 35, B-9000 Ghent, Belgium
3 Center for Human Genetics, Campus Gasthuisberg, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium
4 Center for Metabolic Disease, Campus Gasthuisberg, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium
Received on October 31, 2002; revised on December 5, 2002; accepted on December 5, 2002
The N-glycans present on the total mixture of serum glycoproteins (serum N-glycome) were analyzed in 24 subjects with congenital disorder of glycosylation type I (CDG-I) and 7 healthy, age-matched individuals. No new N-glycan structures were observed in the sera of CDG-I patients as compared with normal sera. However, we observed in all subtypes a significantly increased degree of core 
-1,6-fucosylation of the biantennary glycans as compared to normal, as well as a significant decrease in the amount of triantennary glycans. These serum N-glycome changes appear to be a milder manifestation of some of the changes observed in adult liver cirrhosis patients, which is compatible with the reported steatosis and fibrosis in CDG-I patients. In the CDG-Ia subgroup, the extent of the serum N-glycome changes correlates with the aberration of the serum transferrin isoelectric focusing pattern, which measures the severity of the lack of entire N-glycan chains (primary consequence of CDG-I) in the liver and is the standard diagnostic test for this category of inherited diseases.
1 To whom correspondence should be addressed; e-mail: roland.contreras{at}dmb.rug.ac.be
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