Post-translational modification of α-synuclein in Parkinson's disease
Post-translational modification of α-synuclein in Parkinson's disease
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DOI：
10.1016/j.brainres.2015.06.002
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发表时间：
2015-12-02
期刊：
影响因子：
2.9
通讯作者：
Greenamyre, J. Timothy
中科院分区：
文献类型：
--
作者：
Barrett, Paul J.;Greenamyre, J. Timothy
帕金森病（PD）是第二常见的神经退行性疾病，也是最常见的退行性运动障碍。据估计，这种与年龄有关的神经退行性疾病的患病率将在未来25年内翻一番。虽然帕金森氏病的病因尚不完全清楚，但遗传和散发性疾病之间的共同联系是a-突触核蛋白。在PD脑中，α -突触核蛋白通常存在于称为路易小体和路易神经突的大的不溶性蛋白质聚集体中。a-synuclein的确切作用尚不清楚，但已经证明它经历了各种翻译后修饰，这些修饰以不同的方式影响a-synuclein的聚集和低聚物的形成。这篇综述强调了关键的翻译后修饰及其对α -突触核蛋白聚集和毒性的影响，阐明了PD的潜在发病机制和未来治疗的靶点。这篇文章是《SI：神经保护》特刊的一部分。(C) 2015 Elsevier B.V.版权所有
Parkinson's disease (PD) is the second most common neurodegenerative disease, and the most prevalent degenerative movement disorder. It is estimated that the prevalence of such age-related neurodegenerative diseases will double in the next 25 years. While the etiology of Parkinson's disease is not entirely clear, a common link between both inherited and sporadic forms of disease is the protein a-synuclein. In PD brains, alpha-synuclein is typically found in large, insoluble protein aggregates referred to as Lewy bodies and Lewy neurites. The exact role of a-synuclein is still unknown, but it has been shown to undergo a variety of post-translational modifications, which impact a-synuclein aggregation and oligomer formation in different ways. This review highlights key post-translational modifications and the impact they have on alpha-synuclein aggregation and toxicity, elucidating potential mechanisms for PD pathogenesis and targets for future therapeutics. This article is part of a Special Issue entitled SI: Neuroprotection. (C) 2015 Elsevier B.V. All rights reserved.