O-linked-N-acetylglucosamine(O-GlcNAc)glycosylation is an abundant and unique post-translational modification by adding N-acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins,which is closely related to various diseases such as cancer,neurodegeneration and diabetes.Identification of the O-GlcNAc modification sites is a prerequisite for exploring their potential regulatory mechanisms in related diseases,as well as a key to clinical diagnosis and targeted intervention.In this paper,we summarize the progresses of diseases associated with aberrant O-GlcNAc modification in recent years,as well as the methods for identifying the relevant modification sites,including antibodies,lectins,chemoenzymatic assays,hydrophilic interaction liquid chromatography,and unnatural carbohydrate metabolism labeling,etc.Furthermore,the strategies of"bump and hole theory"and"spatial activation"have been attracted much attentions recently to targeted label proteins in expected tissues.In addition,multifunctional enzymes theory of"one stone,many birds"and the methods of simultaneous analysis of multiple glycan structures in"one pot"will greatly promote the development of glycoproteomics identification.In conclusion,the development of more effective and specific enrichment approaches for O-GlcNAcylated proteins will be of great significance to elucidate the regulatory mechanism of aberrant glycosylation modifications in related diseases.
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