Alpha synuclein aggregation: is it the toxic gain of function responsible for neurodegeneration in Parkinson's disease?
Alpha synuclein aggregation: is it the toxic gain of function responsible for neurodegeneration in Parkinson's disease?
复制标题
DOI：
10.1016/s0047-6374(01)00283-4
复制
发表时间：
2001-09-30
影响因子：
5.3
通讯作者：
Andersen, JK
中科院分区：
文献类型：
--
作者：
Rajagopalan, S;Andersen, JK
蛋白质聚集似乎是一系列不同的神经退行性疾病的共同点，但它在这些不同条件下相关神经元病理中的作用仍然难以捉摸。在帕金森病中，α-突触核蛋白聚集体在细胞内路易体闭塞中的定位是这种疾病的一个主要标志，并表明这种聚集可能在由此导致的多巴胺能细胞损失中发挥作用。在这篇观点文章中。最近的数据被回顾有关如何发生α突触核蛋白聚集，什么细胞事件可能负责，以及这可能如何干扰正常的细胞功能(S)。看来，虽然α突触核蛋白的聚集可能会干扰其在细胞中的正常功能，但这并不是相关神经变性的主要原因。(C)2001爱思唯尔爱尔兰科学有限公司。保留所有权利。
Protein aggregation appears to be the common denominator in a series of distinct neurodegenerative diseases yet its role in the associated neuronal pathology in these various conditions remains elusive. In Parkinson's disease, localization of alpha synuclein aggregates within intracellular Lewy body occlusions represent a major hallmark of this disorder and suggest that such aggregation may play a causative role in the resulting dopaminergic cell loss. In this Viewpoint article. recent data is reviewed related to how alpha synuclein aggregation may occur, what cellular events might be responsible, and how this may interfere with normal cellular function(s). It appears likely that while aggregation of alpha synuclein may interfere with its normal function in the cell, this is not the primary cause of the related neurodegeneration. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.