Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China; University of Chinese Academy of Sciences, Beijing 100049, China.
Biochem Pharmacol. 2019 Sep;167:58-63. doi: 10.1016/j.bcp.2019.04.028. Epub 2019 Apr 26.
Abnormal protein aggregation is a common pathological feature of neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD) and amyotrophic lateral sclerosis (ALS). Protein posttranslational modifications (PTMs) play a crucial regulatory role in the formation of pathologic aggregation. Among the known PTMs involved in neurodegeneration, poly(ADP-ribosylation) (PARylation) has emerged with promising therapeutic potentials of the use of poly(ADP-ribose) (PAR) polymerase (PARP) inhibitors. In this review, we describe the mounting evidence that abnormal PARP activation is involved in various neurodegenerative diseases, and discuss the underpinning mechanisms with a focus on the recent findings that PARylation affects liquid-liquid phase separation and aggregation of amyloid proteins. We hope this review will stimulate further investigation of the unknown functions of PARylation and promote the development of more effective therapeutic agents in treating neurodegeneration.
异常蛋白质聚集是阿尔茨海默病(AD)、帕金森病(PD)、亨廷顿病(HD)和肌萎缩侧索硬化症(ALS)等神经退行性疾病的共同病理特征。蛋白质翻译后修饰(PTMs)在病理性聚集的形成中起着关键的调节作用。在已知的与神经退行性变有关的 PTMs 中,多聚(ADP-核糖)(PARylation)的出现具有使用多聚(ADP-核糖)(PAR)聚合酶(PARP)抑制剂的有前途的治疗潜力。在这篇综述中,我们描述了越来越多的证据表明异常 PARP 激活参与了各种神经退行性疾病,并讨论了潜在的机制,重点是最近发现 PARylation 影响淀粉样蛋白的液-液相分离和聚集。我们希望这篇综述将激发对 PARylation 未知功能的进一步研究,并促进开发更有效的治疗神经退行性变的治疗剂。