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神经毒性多巴胺醌促进tau蛋白组装成纤维状聚合物。

Neurotoxic dopamine quinone facilitates the assembly of tau into fibrillar polymers.

作者信息

Santa-María Ismael, Hernández Félix, Smith Mark A, Perry George, Avila Jesús, Moreno Francisco J

机构信息

Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain.

出版信息

Mol Cell Biochem. 2005 Oct;278(1-2):203-12. doi: 10.1007/s11010-005-7499-6.

DOI:10.1007/s11010-005-7499-6
PMID:16180106
Abstract

Aberrant aggregation of microtubule associated protein tau is the main characteristic of different disorders known as tauopathies. Different compounds have been described to facilitate tau aberrant aggregation. In this work, we demonstrate that oxidized products of dopamine (neurotoxic dopamine quinone), a neurotransmitter involved in Parkinson's disease, promote tau polymerization. Curiously, neurons expressing dopamine (substantia nigra) show a low content of tau protein and seldom have tau aggregation in tauopathies. In non-dopaminergic neurons, quinone oxidation products may be involved in tau polymerization. These results support a link between oxidative damage and the onset of tauopathies.

摘要

微管相关蛋白tau的异常聚集是被称为tau蛋白病的不同疾病的主要特征。已有不同化合物被描述可促进tau异常聚集。在这项研究中,我们证明了多巴胺的氧化产物(神经毒性多巴胺醌),一种与帕金森病相关的神经递质,可促进tau聚合。奇怪的是,表达多巴胺的神经元(黑质)在tau蛋白病中显示tau蛋白含量低且很少有tau聚集。在非多巴胺能神经元中,醌氧化产物可能参与tau聚合。这些结果支持氧化损伤与tau蛋白病发病之间的联系。

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Quinones facilitate the self-assembly of the phosphorylated tubulin binding region of tau into fibrillar polymers.醌类物质促进tau蛋白磷酸化微管结合区域自组装成纤维状聚合物。
阿尔茨海默病中线粒体功能障碍与神经传递失败之间的关系
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