MALDI‐TOF MS applied to apoC‐III glycoforms of patients with congenital disorders affecting O‐glycosylation. Comparison with two‐dimensional electrophoresis. Issue 7 (24th March 2015)

• Record Type: Journal Article
• Authors: Yen‐Nicolaÿ, Stéphanie; Boursier, Céline; Rio, Marlène; Lefeber, Dirk J.; Pilon, Antoine; Seta, Nathalie; Bruneel, Arnaud; Cutler, Paul; Voshol, Hans
• Is Part Of: Proteomics. Volume 9:Issue 7/8(2015)
• Page Start: 787
• Page End: 793
• Publication Date: 2015-03-24
• Subjects: Proteomics -- Periodicals; 572.605
• DOI: 10.1002/prca.201400187
• Languages: English
• ISSNs: 1862-8346

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="prca1624-sec-0010" sec-type="section"> <title>Purpose</title> <p>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.</p> </sec> <sec id="prca1624-sec-0020" sec-type="section"> <title>Experimental design</title> <p>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.</p> </sec> <sec id="prca1624-sec-0030" sec-type="section"> <title>Results</title> <p>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.</p> </sec> <sec id="prca1624-sec-0040" sec-type="section"> <title>Conclusions and clinical relevance</title> <p>MALDI‐TOF MS appears as a powerful technique for the analysis of apoC‐III glycoforms for potential routine screening of COG‐ and ATP6V0A2‐CDGs.</p> </sec> </abstract>