Issue 1, 2023

Recent development of analytical methods for disease-specific protein O-GlcNAcylation

Abstract

The enzymatic modification of protein serine or threonine residues by N-acetylglucosamine, namely O-GlcNAcylation, is a ubiquitous post-translational modification that frequently occurs in the nucleus and cytoplasm. O-GlcNAcylation is dynamically regulated by two enzymes, O-GlcNAc transferase and O-GlcNAcase, and regulates nearly all cellular processes in epigenetics, transcription, translation, cell division, metabolism, signal transduction and stress. Aberrant O-GlcNAcylation has been shown in a variety of diseases, including diabetes, neurodegenerative diseases and cancers. Deciphering O-GlcNAcylation remains a challenge due to its low abundance, low stoichiometry and extreme lability in most tandem mass spectrometry. Separation or enrichment of O-GlcNAc proteins or peptides from complex mixtures has been of great interest because quantitative analysis of protein O-GlcNAcylation can elucidate their functions and regulatory mechanisms in disease. However, valid and specific analytical methods are still lacking, and efforts are needed to further advance this direction. Here, we provide an overview of recent advances in various analytical methods, focusing on chemical oxidation, affinity of antibodies and lectins, hydrophilic interaction, and enzymatic addition of monosaccharides in conjugation with these methods. O-GlcNAcylation quantification has been described in detail using mass-spectrometric or non-mass-spectrometric techniques. We briefly summarized dysregulated changes in O-GlcNAcylation in disease.

Graphical abstract: Recent development of analytical methods for disease-specific protein O-GlcNAcylation

Article information

Article type
Review Article
Submitted
12 nov 2022
Accepted
13 des 2022
First published
21 des 2022
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2023,13, 264-280

Recent development of analytical methods for disease-specific protein O-GlcNAcylation

W. Hu, G. Zhang, Y. Zhou, J. Xia, P. Zhang, W. Xiao, M. Xue, Z. Lu and S. Yang, RSC Adv., 2023, 13, 264 DOI: 10.1039/D2RA07184C

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