通过质谱分析蛋白质O-连接的N-乙酰葡糖胺糖基化
Analysis of Protein O-GlcNAcylation by Mass Spectrometry.
作者信息
Ma Junfeng, Hart Gerald W
机构信息
Department of Biological Chemistry, The Johns Hopkins University, School of Medicine, Baltimore, Maryland.
出版信息
Curr Protoc Protein Sci. 2017 Feb 2;87:24.10.1-24.10.16. doi: 10.1002/cpps.24.
Abstract
O-linked β-D-N-acetyl glucosamine (O-GlcNAc) addition (O-GlcNAcylation), a post-translational modification of serine/threonine residues of proteins, is involved in diverse cellular metabolic and signaling pathways. Aberrant O-GlcNAcylation underlies the initiation and progression of multiple chronic diseases including diabetes, cancer, and neurodegenerative diseases. Numerous methods have been developed for the analysis of protein O-GlcNAcylation, but instead of discussing the classical biochemical techniques, this unit covers O-GlcNAc characterization by combining several enrichment methods and mass spectrometry detection techniques [including collision-induced dissociation (CID), higher energy collision dissociation (HCD), and electron transfer dissociation (ETD) mass spectrometry]. © 2017 by John Wiley & Sons, Inc.
摘要
O-连接的β-D-N-乙酰葡糖胺（O-GlcNAc）添加（O-GlcNAc化）是蛋白质丝氨酸/苏氨酸残基的一种翻译后修饰，参与多种细胞代谢和信号通路。异常的O-GlcNAc化是包括糖尿病、癌症和神经退行性疾病在内的多种慢性疾病发生和发展的基础。已经开发出许多用于分析蛋白质O-GlcNAc化的方法，但本单元不讨论经典的生化技术，而是介绍通过结合几种富集方法和质谱检测技术（包括碰撞诱导解离（CID）、高能碰撞解离（HCD）和电子转移解离（ETD）质谱）来进行O-GlcNAc表征。© 2017约翰威立父子公司版权所有。
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