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A rapid mass spectrometric strategy for the characterization of N‐ and O‐glycan chains in the diagnosis of defects in glycan biosynthesis

A rapid mass spectrometric strategy for the characterization of N‐ and O‐glycan chains in the... Glycosylation of proteins is a very complex process which involves numerous factors such as enzymes or transporters. A defect in one of these factors in glycan biosynthetic pathways leads to dramatic disorders named congenital disorders of glycosylation (CDG). CDG can affect the biosynthesis of not only protein N‐glycans but also O‐glycans. The structural analysis of glycans on serum glycoproteins is essential to solving the defect. For this reason, we propose in this paper a strategy for the simultaneous characterization of both N‐ and O‐glycan chains isolated from the serum glycoproteins. The serum (20 μL) is used for the characterization of N‐glycans which are released by enzymatic digestion with PNGase F. O‐glycans are chemically released by reductive elimination from whole serum glycoproteins using 10 μL of the serum. Using strategies based on mass spectrometric analysis, the structures of N‐ and O‐glycan chains are defined. These strategies were applied on the sera from one patient with CDG type IIa, and one patient with a mild form of congenital disorder of glycosylation type II (CDG‐II) that is caused by a deficiency in the Cog1 subunit of the complex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteomics Wiley

A rapid mass spectrometric strategy for the characterization of N‐ and O‐glycan chains in the diagnosis of defects in glycan biosynthesis

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References (42)

Publisher
Wiley
Copyright
"Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company"
ISSN
1615-9853
eISSN
1615-9861
DOI
10.1002/pmic.200600977
pmid
17520685
Publisher site
See Article on Publisher Site

Abstract

Glycosylation of proteins is a very complex process which involves numerous factors such as enzymes or transporters. A defect in one of these factors in glycan biosynthetic pathways leads to dramatic disorders named congenital disorders of glycosylation (CDG). CDG can affect the biosynthesis of not only protein N‐glycans but also O‐glycans. The structural analysis of glycans on serum glycoproteins is essential to solving the defect. For this reason, we propose in this paper a strategy for the simultaneous characterization of both N‐ and O‐glycan chains isolated from the serum glycoproteins. The serum (20 μL) is used for the characterization of N‐glycans which are released by enzymatic digestion with PNGase F. O‐glycans are chemically released by reductive elimination from whole serum glycoproteins using 10 μL of the serum. Using strategies based on mass spectrometric analysis, the structures of N‐ and O‐glycan chains are defined. These strategies were applied on the sera from one patient with CDG type IIa, and one patient with a mild form of congenital disorder of glycosylation type II (CDG‐II) that is caused by a deficiency in the Cog1 subunit of the complex.

Journal

ProteomicsWiley

Published: Jun 1, 2007

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