Premedical Department Division, Weill Cornell Medicine, Qatar Foundation, Education City, P.O. Box 24144, Doha, Qatar.
Int J Biol Macromol. 2019 Jun 15;131:396-411. doi: 10.1016/j.ijbiomac.2019.02.148. Epub 2019 Mar 7.
Many neurodegenerative diseases including Parkinson's disease, Alzheimer's disease, Prion's disease, polyQ and Huntington's disease share abnormal folding of potentially cytotoxic protein species associated with degeneration and death of specific neuronal populations. In order to maintain cellular protein homeostasis, neurons have developed an intrinsic protein quality control system as a strategy to counteract protein aggregation and their toxicity. Heat shock proteins are an essential component for regulating protein quality control and contribute potentially in the process of protein folding, prevent protein aggregation and in disaggregation in several neurodegenerative diseases. Therefore, molecular chaperones are considered an exciting therapeutic target. In this book chapter, we will focus on the potential importance of different heat shock proteins in neurodegenerative diseases and understand their mechanisms to protect neurons form aggregates and their toxicity.
许多神经退行性疾病，包括帕金森病、阿尔茨海默病、朊病毒病、polyQ 和亨廷顿病，都与潜在的细胞毒性蛋白物种的异常折叠有关，这些蛋白物种与特定神经元群体的退化和死亡有关。为了维持细胞内蛋白质的平衡，神经元已经发展出一种内在的蛋白质质量控制系统，作为对抗蛋白质聚集及其毒性的策略。热休克蛋白是调节蛋白质质量控制的重要组成部分，在几种神经退行性疾病的蛋白质折叠、防止蛋白质聚集和去聚集过程中可能发挥作用。因此，分子伴侣被认为是一个令人兴奋的治疗靶点。在这一章中，我们将重点讨论不同热休克蛋白在神经退行性疾病中的潜在重要性，并了解它们保护神经元免受聚集物和毒性的机制。
