Barghorn S, Mandelkow E
Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, 22607 Hamburg, Germany.
Biochemistry. 2002 Dec 17;41(50):14885-96. doi: 10.1021/bi026469j.
Alzheimer's disease is characterized by aggregates of tau protein. Attempts to study the conditions for aggregation in vitro have led to different experimental systems, some of which appear mutually exclusive (e.g., oxidative vs reductive conditions, induction by polyanions vs fatty acids). We show here that different approaches and pathways can be viewed in a common framework, and that apparent differences can be explained by variations in the kinetics of subreactions. A unified view of PHF aggregation should help to analyze the causes of PHF aggregation and devise methods to prevent it.
阿尔茨海默病的特征是tau蛋白聚集。在体外研究聚集条件的尝试导致了不同的实验系统，其中一些似乎相互排斥（例如，氧化与还原条件、多阴离子诱导与脂肪酸诱导）。我们在此表明，不同的方法和途径可以在一个共同的框架中看待，并且明显的差异可以通过子反应动力学的变化来解释。对PHF聚集的统一观点应该有助于分析PHF聚集的原因并设计预防方法。
