Shan Frank Y, Fung Kar-Ming, Zieneldien Tarek, Kim Janice, Cao Chuanhai, Huang Jason H
Department of Anatomic Pathology, Baylor Scott & White Medical Center, College of Medicine, Texas A&M University, Temple, TX 76508, USA.
Department of Pathology, University of Oklahoma Medical Center, University of Oklahoma, Norman, OK 73019, USA.
Life (Basel). 2021 Oct 22;11(11):1126. doi: 10.3390/life11111126.
α-synuclein is considered the main pathological protein in a variety of neurodegenerative disorders, such as Parkinson's disease, multiple system atrophy, and dementia with Lewy bodies. As of now, numerous studies have been aimed at examining the post-translational modifications of α-synuclein to determine their effects on α-synuclein aggregation, propagation, and oligomerization, as well as the potential cellular pathway dysfunctions caused by α-synuclein, to determine the role of the protein in disease progression. Furthermore, α-synuclein also appears to contribute to the fibrilization of tau and amyloid beta, which are crucial proteins in Alzheimer's disease, advocating for α-synuclein's preeminent role in neurodegeneration. Due to this, investigating the mechanisms of toxicity of α-synuclein in neurodegeneration may lead to a more proficient understanding of the timeline progression in neurodegenerative synucleinopathies and could thereby lead to the development of potent targeted therapies.
α-突触核蛋白被认为是多种神经退行性疾病中的主要病理蛋白,如帕金森病、多系统萎缩和路易体痴呆。截至目前,众多研究旨在检测α-突触核蛋白的翻译后修饰,以确定它们对α-突触核蛋白聚集、传播和寡聚化的影响,以及由α-突触核蛋白引起的潜在细胞通路功能障碍,从而确定该蛋白在疾病进展中的作用。此外,α-突触核蛋白似乎也有助于tau蛋白和β-淀粉样蛋白的纤维化,而这两种蛋白是阿尔茨海默病中的关键蛋白,这表明α-突触核蛋白在神经退行性变中起着重要作用。因此,研究α-突触核蛋白在神经退行性变中的毒性机制可能会更深入地了解神经退行性突触核蛋白病的病程进展,从而可能开发出有效的靶向治疗方法。