Department of Neurology, University of Kuopio, and Kuopio University Hospital, Kuopio, Finland.
Biochem Soc Trans. 2010 Feb;38(Pt 1):150-5. doi: 10.1042/BST0380150.
Abnormal protein aggregation and intracellular or extracellular accumulation of misfolded and aggregated proteins are key events in the pathogenesis of different neurodegenerative diseases. Furthermore, endoplasmic reticulum stress and impairment of the ubiquitin-proteasome system probably contribute to neurodegeneration in these diseases. A characteristic feature of AD (Alzheimer's disease) is the abnormal accumulation of Abeta (amyloid beta-peptide) in the brain. Evidence shows that the AD-associated PS (presenilin) also forms aggregates under certain conditions and that another AD-associated protein, ubiquilin-1, controls protein aggregation and deposition of aggregated proteins. Here, we review the current knowledge of ubiquilin-1 and PS in protein aggregation and related events that potentially influence neurodegeneration.
异常蛋白聚集以及错误折叠和聚集蛋白在细胞内或细胞外的积累，是多种神经退行性疾病发病机制中的关键事件。此外，内质网应激和泛素-蛋白酶体系统的损伤可能导致这些疾病中的神经退行性变。AD（阿尔茨海默病）的一个特征性特征是 Abeta（淀粉样β肽）在大脑中的异常积累。有证据表明，与 AD 相关的 PS（早老素）在某些条件下也会形成聚集体，另一种与 AD 相关的蛋白，泛素结合蛋白-1，控制着蛋白聚集和聚集蛋白的沉积。在这里，我们综述了泛素结合蛋白-1 和 PS 在蛋白聚集及相关事件中的最新知识，这些事件可能会影响神经退行性变。
