《生命科学》 2018, 30(4): 480-490
摘 要：摘 要：蛋白质糖基化修饰结构多样、分布广泛，以N- 糖基化、O-GalNAc 糖基化和O-GlcNAc 糖基化等不同修饰形式存在。糖修饰以各种方式广泛参与基本生物学过程，包括基因转录、蛋白质翻译、信号转导、细胞-细胞间以及宿主-病原体相互作用等。糖基化修饰的异常变化与多种重要疾病的发生发展相关，包括免疫性疾病、肿瘤、先天性糖缺陷等。该文系统展示几种常见糖修饰的结构、参与的生理病理过程，以及最新的研究方法，尤其是糖修饰蛋白质或肽段的特异性富集方法和基于质谱的序列分析方法进展，以期丰富糖修饰蛋白质的研究手段，为糖蛋白质功能机制研究、疾病治疗靶标或候选标志物的发现提供新视角。
Abstract: Abstract: Glycosylation of proteins is diverse in structure， widely distributed and exists in various forms such as N-glycosylation， O-GalNAcylation and O-GlcNAcylation. Different glycosylations are involved in a variety of biological processes， including gene transcription， protein translation， cell signaling， cell-cell and host-pathogen interactions. Abnormal changes in glycosylation are related to the occurrence and development of various important diseases， such as immune diseases， cancer， and congenital disorders of glycosylation. This article introduces several common types of glycosylation， the physiological and pathological processes they involved， and the advances in research methods， specifically the enrichment methods， as well as advances in mass spectrometry. The review is expected to broaden the knowledge on glycoproteomics and to provide novel perspectives for the function of glycoproteins， and drug targets or candidate biomarkers discovery.
