帕金森病相关蛋白α-Synuclein翻译后修饰的研究  

Post-translational modification of α-Synuclein in Parkinson Disease

作　　者：陈连连[1] 曾照芳[1] 

机构地区：[1]重庆医科大学检验系临床检验诊断学教育部重点实验室重庆市重点实验室

出　　处：《激光杂志》2010年第4期82-84,共3页Laser Journal

摘　　要：帕金森病是中老年常见的神经退行性疾病,以黑质多巴胺能神经元变性缺失和路易小体形成为特征。α-Synuclein是路易小体的主要组成成分,由于它在介导帕金森病的神经毒性方面发挥很大的作用,而越来越引起人们的关注。帕金森病相关蛋白α-Synuclein存在多种翻译后修饰,可能促使路易小体形成,从而参与帕金森病的发生和发展。本文在研究α-Synuclein蛋白的磷酸化、硝基化和泛素化与帕金森病的关系的基础上进行了总结。Parkinson＇s disease is one of the most common neurodegenerative diseases among middle-aged people,characterized by progressive degeneration of dopaminergic neurons in the substantia nigra and accumulation of cytoplasmic inclusions termed Lewy bodies in surviving neurons.α-Synuclein,which is the main component of Lewy bodies,has raised more and more concerns about its function of mediating neurotoxicity in PD.Posttranslational modification（PTM） has been identified on α-Synuclein,which may promote Lewy body（LD） formation and play an important role in the initiation and progression of PD neuropathophysiology.We mainly discussed phosphorylation,nitrition and ubiquitination of α-Synuclein in this review.

关 键 词：帕金森病 蛋白质翻译后修饰 Α-共核蛋白 路易小体 磷酸化 硝基化 泛素化 

分 类 号：R477[医药卫生—护理学]