α-突触核蛋白乙酰化修饰在帕金森病中作用的研究进展  

Research advances in acetylation modification of α-synuclein in Parkinson's disease

作　　者：杨笑 杜芸兰[1] 管阳太[1] YANG Xiao;DU Yun-lan;GUAN Yang-tai(Department of Neurology,Renji Hospital,Shanghai Jiao Tong University School of Medicine,Shanghai 200127,China)

机构地区：[1]上海交通大学医学院附属仁济医院神经内科,上海200127

出　　处：《上海交通大学学报（医学版）》2018年第11期1381-1385,共5页Journal of Shanghai Jiao tong University:Medical Science

基　　金：国家自然科学基金(81671247);上海市自然科学基金(16ZR1420100)~~

摘　　要：帕金森病(Parkinson's disease,PD)是目前尚无法治愈的神经系统退行性疾病,严重影响患者的生活质量。多年来,研究发现α-突触核蛋白的过量产生或者结构异常会导致形成具有毒性作用的聚集体,这是PD发病的关键环节。α-突触核蛋白的异常修饰与其聚集状态密切相关,如蛋白磷酸化修饰、泛素化修饰、硝基化修饰等,但这些修饰的确切作用尚不确定。近年来的研究显示乙酰化修饰在α-突触核蛋白的异常聚集中发挥不可忽视的作用。该文就其研究进展进行综述。Parkinson＇s disease （PD） is an incurable neurodegenerative disease, which seriously affects the life quality of patients. Researches in recent years found that excessive production or abnormal structure of α-synuclein and forming toxic aggregates are the key factors in the pathogenesis of PD. In a variety of mechanisms, abnormal modifcation of α-synuclein is closely related to its aggregation state, such as phosphorylation, ubiquitination and nitration modifcation, but the exact effects are still uncertain. Recent studies have shown that acetylation modifcation of α-synuclein plays an important role in the abnormal aggregation of α-synuclein. This article reviewed the progress of acetylation modifcation of α-synuclein.

关 键 词：Α-突触核蛋白 帕金森病 聚集体 乙酰化修饰 

分 类 号：R742.5[医药卫生—神经病学与精神病学]