Alzheimer's disease (AD) is characterized neuropathologically by progressive neurodegeneration and by the presence of amyloid plaques and neurofibrillary tangles. These plaques and tangles are composed, respectively, of amyloid-beta (Aβ) and tau proteins. While long recognized as hallmarks of AD, it remains unclear what causes the formation of these insoluble deposits. One theory holds that prion-like templated misfolding of Aβ and tau induces these proteins to form pathological aggregates, and propagation of this misfolding causes the stereotyped progression of pathology commonly seen in AD. Supporting this theory, numerous studies have been conducted in which aggregated Aβ, tau, or α-synuclein is injected intracerebrally into pathology-free host animals, resulting in robust formation of pathology. Here, we review this literature, focusing on in vivo intracerebral seeding of Aβ and tau in mice. We compare the results of these experiments to what is known about the seeding and spread of α-synuclein pathology, and we discuss how this research informs our understanding of the factors underlying the onset, progression, and outcomes of proteinaceous pathologies.

中文翻译：

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淀粉样蛋白β的脑内播种和小鼠tau病理：病毒样扩散的基础因素以及与α-突触核蛋白的比较。

在神经病理学上，阿尔茨海默氏病（AD）的特征是进行性神经退行性变以及淀粉样斑块和神经原纤维缠结的存在。这些斑块和缠结分别由淀粉样蛋白（Aβ）和tau蛋白组成。尽管长期以来被公认为是AD的标志，但仍不清楚是什么原因导致了这些不溶性沉积物的形成。一种理论认为，Aβ和tau的病毒样模板错误折叠会诱导这些蛋白质形成病理性聚集体，这种错误折叠的传播会导致AD中常见的病理定型发展。支持该理论的许多研究已经进行，其中将聚集的Aβ，tau或α-突触核蛋白脑内注射到无病理的宿主动物中，从而导致病理的稳固形成。在这里，我们回顾一下这些文献，专注于小鼠体内脑内Aβ和tau的接种。我们将这些实验的结果与已知的α-突触核蛋白病理学播种和传播进行比较，并讨论该研究如何帮助我们理解蛋白质病理学起因，进展和结果的因素。