基于生物质谱的蛋白质O-GalNAc糖基化修饰研究进展

Advances in O-GalNAc glycosylation research based on biological mass spectrometry

糖基化是生物体内蛋白质最常见、最重要的翻译后修饰之一,普遍存在于细胞膜蛋白及分泌蛋白,执行重要的生物学功能.常见的蛋白糖基化修饰有N-糖基化及O-糖基化两种类型,而O-GalNAc是O-糖基化中重要的存在形式,在特定生物学进程、癌症发生发展中起着重要作用,近年来受到广泛重视.得益于代谢标记、化学衍生化、高分辨和多种碎裂模式质谱技术以及基因编辑技术的高速发展,O-GalNAc的糖基化位点、糖型鉴定和生理功能研究取得一系列重大进展.本文综述了基于生物质谱技术的蛋白质O-GalNAc糖基化修饰研究进展.

Glycosylation is one of the most common and important post-translational modifications of proteins in eukaryotic cells. It is prevalent in cell membrane proteins and secreted proteins, performing important biological functions. Major types of protein glycosylation include N-glycosylation and O-glycosylation. O-GalNAc glycosylation is an important form of O-glycosylation and plays vital roles in regulating many key biological processes. It has close correlation with the occurrence and development of cancer. Thanks to powerful metabolic labeling methods, chemical derivatization approaches, mass spectrometry techniques and gene editing technology, the identification and elucidation of O-GalNAc glycosylation sites and sugar chains are developing rapidly. This paper reviews the advances in research of O-GalNAc glycosylation in recent years.