α-突触核蛋白和亮氨酸丰富重复激酶2在tau蛋白磷酸化中的作用

Kawakami Fumitaka, Ichikawa Takafumi

Department of Regulation Biochemistry, Graduate School of Medical Sciences, Kitasato University, Sagamihara 2520373, Japan.

Parkinsons Dis. 2015;2015:734746. doi: 10.1155/2015/734746. Epub 2015 Apr 21.

There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to ameliorate neurodegenerative diseases associated with tau pathology, we also discuss therapeutic strategies for PD focusing on inhibition of α-synuclein- and LRRK2-associated tau phosphorylation by HSPs.

现在有大量实验证据表明，帕金森病是由致病分子的生理相互作用导致tau病理而引发的。在本综述中，我们讨论了α-突触核蛋白和富含亮氨酸重复激酶2（LRRK2）在tau异常磷酸化中的生理作用。此外，由于最近的报告表明，诱导热休克蛋白（HSPs）的药物有助于改善与tau病理相关的神经退行性疾病，我们还讨论了以通过热休克蛋白抑制与α-突触核蛋白和LRRK2相关的tau磷酸化为重点的帕金森病治疗策略。