蛋白质O-GlcNAc修饰的检测技术

O-连接的N-乙酰葡糖胺（O-GlcNAc）修饰是位于细胞浆和细胞核蛋白质的丝氨酸或苏氨酸上的一种翻译后修饰，在高等真核生物细胞中广泛存在.越来越多的研究表明,O-GlcNAc修饰在代谢调控、压力应激、细胞周期、凋亡、糖尿病、心血管疾病和癌症等多种生理和病理过程中发挥重要作用，因此, O-GlcNAc修饰已受到众多生命科学领域研究人员的关注.然而,由于O-GlcNAc修饰与传统的N聚糖和O聚糖修饰有所不同，常规糖基化修饰的检测方法并不适用于O-GlcNAc.本文对O-GlcNAc修饰的检测及其修饰位点的确定方法进行了综述，并分析了各种方法的优缺点.

Methods for Detecting and Site-mapping O-GlcNAc Modification of Proteins

O-linked attachment of N-acetyl-glucosamine (O-GlcNAc) on serine and threonine residues of nuclear and cytoplasmic proteins is a ubiquitous post-translational modification present in higher eukaryotes. There is accumulating evidence that O-GlcNAcylation plays an important role in multiple physiological and pathological processes, such as regulation of metabolism, stress response, cell cycle, apoptosis, diabetes, cardiovascular disease and cancer. However, conventional detection methods developed for N-glycans and O-glycans are not suitable for this special modification. Many efforts have therefore been made to address this problem. This paper summarizes the detection and site mapping methods of O-GlcNAc, and analyzes the advantage and disadvantage of each method to facilitate future studies.