Department of Bio-Analytical Chemistry, Research Institute of Pharmaceutical Sciences, Faculty of Pharmacy, Musashino University, Tokyo 202-8585, Japan.
Int J Mol Sci. 2021 Jan 28;22(3):1267. doi: 10.3390/ijms22031267.
Prion diseases are progressive and transmissive neurodegenerative diseases. The conformational conversion of normal cellular prion protein (PrP) into abnormal pathogenic prion protein (PrP) is critical for its infection and pathogenesis. PrP possesses the ability to bind to various neurometals, including copper, zinc, iron, and manganese. Moreover, increasing evidence suggests that PrP plays essential roles in the maintenance of homeostasis of these neurometals in the synapse. In addition, trace metals are critical determinants of the conformational change and toxicity of PrP. Here, we review our studies and other new findings that inform the current understanding of the links between trace elements and physiological functions of PrP and the neurotoxicity of PrP.
朊病毒病是进行性和传染性神经退行性疾病。正常细胞朊蛋白（PrP）构象转换为异常致病性朊蛋白（PrP）对于其感染和发病机制至关重要。PrP 具有结合各种神经金属的能力，包括铜、锌、铁和锰。此外，越来越多的证据表明，PrP 在突触中维持这些神经金属的内环境平衡中发挥重要作用。此外，痕量金属是 PrP 构象变化和毒性的关键决定因素。在这里，我们回顾了我们的研究和其他新发现，这些发现为目前对痕量元素与 PrP 的生理功能之间的联系以及 PrP 的神经毒性的理解提供了信息。
