Protein Glysosylation and Congenital Disorders of Glycosylation

  • Eva Morava
  • Dirk J. Lefeber
  • Ron A. Wevers
Part of the Protein Reviews book series (PRON, volume 13)


Congenital Disorders of Glycosylation (CDG) form a group of inborn errors of metabolism, first described by Jaeken in 1987. Since then the molecular basis has been delineated in 23 different CDG subtypes. All underlying molecular defects in CDG interfere with the process of glycosylation, thus having functional consequences for many proteins. In the majority of the CDG subtypes the molecular defect has been found in genes coding for proteins related to the endoplasmic reticulum. Part of the glycosylation process takes place in the Golgi-apparatus. In most of the patients with Golgi-related glycosylation disorders the molecular etiology remains unsolved. The current review focusses on the biochemical background and clinical presentation of the disorders of N-linked, O-linked and combined N-and O-linked glycosylation.


Nucleotide Sugar Congenital Muscular Dystrophy Cutis Laxa Conserve Oligomeric Golgi Conserve Oligomeric Golgi Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Congenital disorders of glycosylation


Conserved oligomeric Golgi


Uridine 5′-diphosphate


Endoplasmatic reticulum


Isoelectric point


Transferrin isoelectric focusing


Isoelectric focusing


Lipid linked oligosaccharides


Apolipoprotein C-III


Autosomal recessive cutis laxa


(For Abbreviations of enzymes see Table 5.1)



This work was supported by a grant from the European Commission (FP6 – Euroglycanet – contract no. 512131).


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© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Department of PaediatricsRadboud University Nijmegen Medical CentreNijmegenThe Netherlands

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