Gamblin T Chris, Berry Robert W, Binder Lester I
Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA.
Biochemistry. 2003 Dec 30;42(51):15009-17. doi: 10.1021/bi035722s.
The major antigenic component of neurofibrillary pathology in a large number of neurodegenerative diseases consists of the microtubule-associated protein tau. It is currently unclear how tau protein makes the transition from an important component of the microtubule-based cytoskeleton to an insoluble polymerized state. In vitro techniques have been employed to study the polymerization of tau in an effort to understand the underlying molecular mechanisms responsible for this process. These efforts have resulted in the elucidation of roles played by the different parts of the molecule in the polymerization process. Here we discuss the advantages and disadvantages of the various techniques used to model tau polymerization and the discoveries arising from these techniques that have led to a better structural understanding of tau polymerization in relation to Alzheimer's disease and other tauopathies.
在许多神经退行性疾病中，神经原纤维病理的主要抗原成分是微管相关蛋白tau。目前尚不清楚tau蛋白是如何从基于微管的细胞骨架的重要组成部分转变为不溶性聚合状态的。为了理解导致这一过程的潜在分子机制，人们采用了体外技术来研究tau的聚合。这些努力已阐明了该分子不同部分在聚合过程中所起的作用。在此，我们讨论用于模拟tau聚合的各种技术的优缺点，以及由这些技术所带来的发现，这些发现使我们对与阿尔茨海默病及其他tau蛋白病相关的tau聚合有了更好的结构理解。
