Analyzing Tau Aggregation with Electron Microscopy
Analyzing Tau Aggregation with Electron Microscopy
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DOI：
10.1007/978-1-4939-2978-8_7
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发表时间：
2016-01-01
期刊：
影响因子：
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通讯作者：
Kuret, Jeff
中科院分区：
文献类型：
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作者：
Huseby, Carol J.;Kuret, Jeff
单体tau蛋白转化为丝状聚集体是阿尔茨海默病发病机制中的决定性事件。为了深入了解疾病的发病机制，触发和介导tau蛋白聚集的机制正在进行深入研究。表征工作主要依赖于重组tau蛋白制剂和基于高通量溶液的检测方法，如thiofl avindye荧光和激光散射光谱。透射电子显微镜（TEM）是一种静态成像工具，通过以纳米分辨率检测单个tau细丝来补充这些方法。在这样做的过程中，它可以提供对合成tau细丝群体的质量，数量和组成的独特见解。在这里，我们描述了用于通过TEM分析tau细丝群体以剖析聚集机制的方案。
Conversion of monomeric tau protein into filamentous aggregates is a defining event in the pathogenesis of Alzheimer's disease. To gain insight into disease pathogenesis, the mechanisms that trigger and mediate tau aggregation are under intense investigation. Characterization efforts have relied primarily on recombinant tau protein preparations and high-throughput solution-based detection methods such as thiofl avindye fluorescence and laser-light-scattering spectroscopies. Transmission electron microscopy (TEM) is a static imaging tool that complements these approaches by detecting individual tau filaments at nanometer resolution. In doing so, it can provide unique insight into the quality, quantity, and composition of synthetic tau filament populations. Here we describe protocols for analysis of tau filament populations by TEM for purposes of dissecting aggregation mechanism.