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MALDI‐TOF MS applied to apoC‐III glycoforms of patients with congenital disorders affecting O‐glycosylation. Comparison with two‐dimensional electrophoresis
Author(s) -
YenNicolaÿ Stéphanie,
Boursier Céline,
Rio Marlène,
Lefeber Dirk J.,
Pilon Antoine,
Seta Nathalie,
Bruneel Arnaud
Publication year - 2015
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.201400187
Subject(s) - glycan , glycosylation , mass spectrometry , chemistry , gel electrophoresis , cog , apolipoprotein b , microbiology and biotechnology , glycoprotein , biochemistry , biology , chromatography , artificial intelligence , cholesterol , computer science
Purpose The O‐glycan abnormalities accompanying some congenital disorders of glycosylation, namely conserved oligomeric Golgi‐congenital disorders of glycosylation (COG‐CDGs) and ATP6V0A2‐CDGs, are mainly detected using electrophoresis methods applied to circulating apolipoprotein C‐III. The objective of this study was to evaluate the reliability of MALDI‐TOF MS of apoC‐III for the detection and characterization of CDG‐associated O‐glycan defects. Experimental design plasmas from CDG‐negative, COG‐CDG, and ATP6V0A2‐CDG patients were analyzed and results were compared to those obtained using 2DE followed by Western blot. Results MALDI‐TOF of apoC‐III allowed to detect various significant O‐glycan abnormalities in CDG‐patients with emphasis to COG‐CDG. Furthermore, in CDG samples, comparison study between 2DE and MALDI‐TOF showed a particular behavior of monosialylated apoC‐III in the mass spectrometer that could be related to an abnormal O‐glycan structure. Conclusions and clinical relevance MALDI‐TOF MS appears as a powerful technique for the analysis of apoC‐III glycoforms for potential routine screening of COG‐ and ATP6V0A2‐CDGs.