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首页> 外文期刊>The FEBS journal >TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
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TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

机译：TDP-43：肌萎缩性侧索硬化症中蛋白质聚集与神经变性和额颞叶变性的关系

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摘要

Accumulations of aggregated proteins are a key feature of the pathology of all of the major neurodegenerative diseases. Amyotrophic lateral sclerosis (ALS) was brought into this fold quite recently with the discovery of TDP-43 (TAR DNA binding protein, 43 kDa) inclusions in nearly all ALS cases. In part this discovery was fueled by the recognition of the clinical overlap between ALS and frontotemporal lobar degeneration, where ubiquitinated TDP-43 inclusions were first identified. Later the identification of TDP-43 mutations in rare familial forms of ALS confirmed that altered TDP-43 function can be a primary cause of the disease. However, the simple concept that TDP-43 is an aggregation-prone protein that forms toxic inclusions capable of promoting neurodegeneration has not been upheld by initial investigations. This review discusses observations from human pathology, cell culture and animal model systems, to highlight our somewhat murky understanding of the relationship between TDP-43 aggregation and neurodegeneration.
机译：聚集蛋白的积累是所有主要神经退行性疾病病理学的关键特征。由于几乎在所有ALS病例中都发现了TDP-43（TAR DNA结合蛋白，43 kDa）夹杂物，肌萎缩性侧索硬化症（ALS）引起了人们的关注。在某种程度上，这一发现是由于认识到ALS与额颞叶变性之间的临床重叠而加剧的，在此处首先发现了泛素化的TDP-43内含物。后来鉴定出罕见的ALS家族形式的TDP-43突变，证实了TDP-43功能的改变可能是导致该疾病的主要原因。但是，TDP-43是易于聚集的蛋白质，会形成能够促进神经退行性变的有毒内含物，这一简单概念尚未得到初步研究的证实。这篇综述讨论了来自人类病理学，细胞培养和动物模型系统的观察结果，以突出我们对TDP-43聚集与神经变性之间关系的模糊理解。

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