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Complementarity of electrophoretic, mass spectrometric, and gene sequencing techniques for the diagnosis and characterization of congenital disorders of glycosylation
Author(s) -
Bruneel Arnaud,
Cholet Sophie,
DrouinGarraud Valérie,
Jacquemont MarieLine,
Cano Aline,
Mégarbané André,
Ruel Coralie,
Cheillan David,
Dupré Thierry,
VuillaumierBarrot Sandrine,
Seta Nathalie,
Fenaille François
Publication year - 2018
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201800021
Subject(s) - glycosylation , glycan , gene , glycoprotein , transferrin , biology , proteomics , dna sequencing , mass spectrometry , mucin , genetics , biochemistry , microbiology and biotechnology , chemistry , chromatography
Congenital disorders of glycosylation (CDG) are rare autosomal genetic diseases affecting the glycosylation of proteins and lipids. Since CDG‐related clinical symptoms are classically extremely variable and nonspecific, a combination of electrophoretic, mass spectrometric, and gene sequencing techniques is often mandatory for obtaining a definitive CDG diagnosis, as well as identifying causative gene mutations and deciphering the underlying biochemical mechanisms. Here, we illustrate the potential of integrating data from capillary electrophoresis of transferrin, two‐dimensional electrophoresis of N‐ and O‐ glycoproteins, mass spectrometry analyses of total serum N‐ linked glycans and mucin core1 O‐ glycosylated apolipoprotein C‐III for the determination of various culprit CDG gene mutations. “Step‐by‐step” diagnosis pathways of four particular and new CDG cases, including MGAT2‐CDG, ATP6V0A2‐CDG, SLC35A2‐CDG, and SLC35A3‐CDG, are described as illustrative examples.