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Current Methods for the Characterization of O-Glycans.

Authors
  • Wilkinson, Hayden1, 2, 3
  • Saldova, Radka1, 2, 3
  • 1 NIBRT GlycoScience Group, National Institute for Bioprocessing, Research and Training, Blackrock, Dublin, Ireland. , (Ireland)
  • 2 CÚRAM, SFI Research Centre for Medical Devices, National University of Ireland, Galway, Ireland. , (Ireland)
  • 3 UCD School of Medicine, College of Health and Agricultural Science, University College Dublin, Dublin, Ireland. , (Ireland)
Type
Published Article
Journal
Journal of Proteome Research
Publisher
American Chemical Society
Publication Date
Oct 02, 2020
Volume
19
Issue
10
Pages
3890–3905
Identifiers
DOI: 10.1021/acs.jproteome.0c00435
PMID: 32893643
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Glycosylation is crucial in cellular metabolism and survival. Of interest is the role of N-linked and O-linked glycans in disease states. Robust analytical methods must be defined to identify suitable glycan biomarkers and glyco-therapeutics. Fortunately, in N-glycan analysis, a universal enzyme exists to deglycosylate a variety of common-core structures from proteins for analysis using mass spectrometric and fluorescence techniques. Unfortunately, for their O-linked counterparts, no such enzyme exists. Furthermore, O-glycan heterogeneity is vast due to the lack of a common glycan core, making analysis challenging. As such, chemical methods are used to liberate O-glycans, however, often to the detriment of the glycan's structure due to "peeling" reactions. This review outlines approaches for O-glycan release and downstream glycomic and glycoproteomic analysis.

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