文献类型：期刊文献

中文题名：α-突触核蛋白的生物学功能及其在帕金森病中的作用

英文题名：Biological functions of α-synuclein and its role in Parkinson’s disease

作者：熊中奎[1,2];胡雅儿[2]

机构：[1]绍兴文理学院医学院临床医学部;[2]上海交通大学医学院细胞调控实验室

年份：2010

卷号：26

期号：9

起止页码：1855

中文期刊名：中国病理生理杂志

外文期刊名：Chinese Journal of Pathophysiology

收录：CSTPCD、、CSCD2011_2012、北大核心2008、北大核心、CSCD

基金：绍兴文理学院重点科研资助项目(No09LG1013)

语种：中文

中文关键词：α-突触核蛋白;帕金森病

外文关键词：α-synuclein; Parkinson disease

中文摘要：α-突触核蛋白（α-synuclein）是一种脑内含量丰富的神经蛋白,既参与正常突触功能的维持,又与各种神经退行性疾病有关。在帕金森病（Parkinson’Sdisease，PD）患者脑内，α-突触核蛋白是多巴胺神经元中嗜伊红染色Lewy小体主要成分。α-突触核蛋白基因位于染色体4q21．3-q22，均由5个外显子构成。

外文摘要：α-Synuclein is identified as a constant component of dopaminergic neuronal pale eosinophilic inclusions＂the Lewy bodies＂in Parkinson’s disease. In fact,normal α-synuclein has lots of biological functions,which regulates synaptic plasticity,integrates presynaptic signaling,regulates dopamine level in the synapse,modulates microglial activation and lipid metabolism,and exerts heat shock protein-like function. However,abnormal α-synuclein leads to pathological lesion. Many studies show that pathological α-synuclein levels are elevated under the condition of its gene mutation,certain posttranslational modifications,dysfunction of molecular chaperones or ubiquitin proteasome system. The pathological α-synuclein plays an important role in neurodegeneration,in particular,Parkinson’s disease because it interrupts integrity of synaptic vesicles,ER-Golgi traffic and axonal transport,inhibits histone acetylation and chaperone-mediated autophagy,stabilizes itself against proteasomal degradation,and leads to neuroinflammation and abnormal phosphorylation of tau.