Linking alpha-synuclein properties with oxidation: a hypothesis on a mechanism underling cellular aggregation.
Linking alpha-synuclein properties with oxidation: a hypothesis on a mechanism underling cellular aggregation.
复制标题
将 α-突触核蛋白特性与氧化联系起来：细胞聚集机制的假设。
DOI：
10.1007/s10863-014-9540-5
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发表时间：
2014
影响因子：
3
通讯作者：
Golebiewska,Urszula
中科院分区：
文献类型：
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作者：
Scarlata,Suzanne;Golebiewska,Urszula
α-突触核蛋白是一种小的、天然的非结构蛋白，具有聚集的倾向。α-突触核蛋白纤维是路易小体的主要成分，是许多神经退行性疾病的特征。α-突触核蛋白的溶液性质和聚集行为已经被很好地描述，但是尽管许多研究解决了α-突触核蛋白在细胞中的作用，但该蛋白的明确的生理功能仍然是一个谜。在过去的十年里，已经写了一百多篇关于α-突触核蛋白的综述文章，这使得很难列出所有的重要研究，这些研究增加了我们对α-突触核蛋白生理学的认识。相反，我们简要回顾了α-突触核蛋白的研究现状，并提出了一个基于以下想法的模型：α-突触核蛋白可能不具有细胞内的固有活性，而是修改一组蛋白质伙伴的功能，进而影响细胞过程。我们认为，正是氧化条件下细胞伙伴的丧失促进了α-突触核蛋白的聚集，加速了神经元的死亡。
α-Synuclein is a small, natively unstructured protein with propensity to aggregate. α-Synuclein fibrils are major components of Lewy bodies that are hallmarks of many neurodegenerative diseases. The solution properties and aggregation behavior of α-synuclein has been well characterized, but despite numerous studies that address the role of α-synuclein in cells, a clear physiological function of this protein remains a mystery. Over a hundred review articles of α-synuclein have been written in the last decade, making it difficult to list all of the important studies that have added to our insight of α-synuclein physiology. Instead, we briefly review the status of α-synuclein research and propose a model based on the idea that α-synuclein may not have an intrinsic activity in cells but rather, it modifies the function of a group of protein partners that in turn affect cell processes. We propose that it is the loss of its cellular partners under oxidative conditions that promotes α-synuclein aggregation accelerating neuronal death.