Division of Medicine, Department of Imaging, Centre for Advanced Biomedical Imaging, Faculty of Medical Sciences, University College London, Paul O'Gorman Building, 72 Huntley Street, London, WC1E 6DD, UK.
Transl Neurodegener. 2022 Mar 21;11(1):19. doi: 10.1186/s40035-022-00293-2.
Many neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, are characterised by the accumulation of misfolded protein deposits in the brain, leading to a progressive destabilisation of the neuronal network and neuronal death. Among the proteins that can abnormally accumulate are tau and α-synuclein, which can propagate in a prion-like manner and which upon aggregation, represent the most common intracellular proteinaceous lesions associated with neurodegeneration. For years it was thought that these intracellular proteins and their accumulation had no immediate relationship with extracellular homeostasis pathways such as the glymphatic clearance system; however, mounting evidence has now suggested that this is not the case. The involvement of the glymphatic system in neurodegenerative disease is yet to be fully defined; however, it is becoming increasingly clear that this pathway contributes to parenchymal solute clearance. Importantly, recent data show that proteins prone to intracellular accumulation are subject to glymphatic clearance, suggesting that this system plays a key role in many neurological disorders. In this review, we provide a background on the biology of tau and α-synuclein and discuss the latest findings on the cell-to-cell propagation mechanisms of these proteins. Importantly, we discuss recent data demonstrating that manipulation of the glymphatic system may have the potential to alleviate and reduce pathogenic accumulation of propagation-prone intracellular cytotoxic proteins. Furthermore, we will allude to the latest potential therapeutic opportunities targeting the glymphatic system that might have an impact as disease modifiers in neurodegenerative diseases.
许多神经退行性疾病,包括阿尔茨海默病和帕金森病,其特征是大脑中错误折叠的蛋白质沉积物的积累,导致神经元网络的渐进性不稳定和神经元死亡。在可能异常积累的蛋白质中,有 tau 和 α-突触核蛋白,它们可以以类朊病毒的方式传播,并且在聚集时,代表与神经退行性变最常见的细胞内蛋白病变。多年来,人们一直认为这些细胞内蛋白质及其积累与细胞外稳态途径(如神经胶清除系统)没有直接关系;然而,越来越多的证据表明情况并非如此。神经胶清除系统在神经退行性疾病中的参与尚未完全定义;然而,越来越明显的是,该途径有助于实质溶质清除。重要的是,最近的数据表明,易于在细胞内积累的蛋白质易受神经胶清除作用,这表明该系统在许多神经疾病中发挥着关键作用。在这篇综述中,我们提供了 tau 和 α-突触核蛋白的生物学背景,并讨论了这些蛋白质的细胞间传播机制的最新发现。重要的是,我们讨论了最近的数据表明,对神经胶清除系统的操作可能具有减轻和减少传播倾向的细胞内细胞毒性蛋白质的致病性积累的潜力。此外,我们将提及针对神经胶清除系统的最新潜在治疗机会,这些机会可能作为神经退行性疾病的疾病修饰剂产生影响。