The George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, Department of Neurology, University of Texas Medical Branch, Galveston, Texas 77555-1045, United States.
Biochemistry. 2010 Nov 30;49(47):10039-41. doi: 10.1021/bi1016233. Epub 2010 Nov 8.
Tau aggregation is a pathological hallmark of Alzheimer's disease, Parkinson's disease, and many other neurodegenerative disorders known as tauopathies. Tau aggregates take on many forms, and their formation is a multistage process with intermediate stages. Recently, tau oligomers have emerged as the pathogenic species in tauopathies and a possible mediator of amyloid-β toxicity in Alzheimer's disease. Here, we use a novel, physiologically relevant method (oligomer cross-seeding) to prepare homogeneous populations of tau oligomers and characterize these oligomers in vitro. We show that both Aβ and α-synuclein oligomers induce tau aggregation and the formation of β-sheet-rich neurotoxic tau oligomers.
tau 聚集是阿尔茨海默病、帕金森病和许多其他神经退行性疾病（称为 tau 病）的病理标志。tau 聚集有多种形式，其形成是一个多阶段的过程，存在中间阶段。最近，tau 低聚物已成为 tau 病中的致病物质，也是阿尔茨海默病中淀粉样 β 毒性的可能介导物。在这里，我们使用一种新颖的、与生理相关的方法（低聚物交叉引发）来制备同质的 tau 低聚物群体，并在体外对这些低聚物进行表征。我们表明，Aβ 和 α-突触核蛋白低聚物均可诱导 tau 聚集，并形成富含 β-折叠的神经毒性 tau 低聚物。
