Analysis of N- and O-linked protein glycosylation in children with Prader-Willi syndrome

Munce, T., Heussler, H. S. and Bowling, F. G. (2010) Analysis of N- and O-linked protein glycosylation in children with Prader-Willi syndrome. Journal of Intellectual Disability Research, 54 10: 929-937. doi:10.1111/j.1365-2788.2010.01323.x

Author Munce, T.
Heussler, H. S.
Bowling, F. G.
Title Analysis of N- and O-linked protein glycosylation in children with Prader-Willi syndrome
Journal name Journal of Intellectual Disability Research   Check publisher's open access policy
ISSN 0964-2633
Publication date 2010-10
Sub-type Article (original research)
DOI 10.1111/j.1365-2788.2010.01323.x
Volume 54
Issue 10
Start page 929
End page 937
Total pages 9
Place of publication Oxford, United Kingdom
Publisher Wiley-Blackwell Publishing
Collection year 2011
Language eng
Formatted abstract
Current genotype-phenotype correlations in Prader-Willi syndrome (PWS) are struggling to give an explanation of the diversity in phenotype and there is a need to move towards a molecular understanding of PWS. A range of functions related to glycoproteins are involved in the pathophysiology of PWS and it may be that abnormal glycosylation is contributing to the biological phenotype. The objective of this study was to investigate the state of N- and O-linked glycosylation in children with Prader-Willi syndrome.


Twenty-three children with PWS and 20 non-PWS controls were included in the study. Protein N-linked glycosylation was assessed by analysing serum transferrin through mass spectrometry and protein O-linked through isoelectric focusing (IEF) of serum apolipoprotein C-III (apoC-III), confirmed by mass spectrometry.


The results of this analysis indicated that the N-linked glycosylation pathway in PWS is normal. A subgroup of PWS individuals was found to have a hyposialylated pattern of apoC-III isoforms. This was independent of the underlying genetic mechanism and is the first report of an apoC-III IEF abnormality in PWS.

This is the first report of apoC-III hyposialylation in PWS. As this field is in its infancy, additional study is required before these findings may be used in clinical settings.
Copyright © 1999-2010 John Wiley & Sons, Inc. All Rights Reserved.
Keyword Mass spectrometry
Prader-Willi syndrome
Protein glycosylation
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Chemistry and Molecular Biosciences
School of Medicine Publications
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Citation counts: TR Web of Science Citation Count  Cited 2 times in Thomson Reuters Web of Science Article | Citations
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Created: Sun, 24 Oct 2010, 00:10:45 EST