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首页> 外文期刊>Trends in Neurosciences >More than just two peas in a pod: common amyloidogenic properties of tau and alpha-synuclein in neurodegenerative diseases.
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More than just two peas in a pod: common amyloidogenic properties of tau and alpha-synuclein in neurodegenerative diseases.

机译：豆荚中不止两个豌豆：tau和α-突触核蛋白在神经变性疾病中的常见淀粉样变性特性。

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摘要

Intracytoplasmic filamentous aggregates, such as neurofibrillary tangles in Alzheimer's disease and Lewy bodies in Parkinson's disease, are composed of the proteins tau and alpha-synuclein, respectively. These pathological inclusions are linked directly to the etiology and mechanisms of disease in a wide spectrum of neurodegenerative disorders, termed 'tauopathies' and 'synucleinopathies'. Emerging evidence indicates that there is frequent overlap of the pathological and clinical features of patients with tauopathies and synucleinopathies, thereby re-enforcing the notion that these disorders might be linked mechanistically. Indeed, several lines of investigation suggest that tau and alpha-synuclein might constitute a unique class of unstructured proteins that assemble predominantly into homopolymeric (rather than heteropolymeric) fibrils, which deposit mainly in separate amyloid inclusions, but occasionally deposit together. Thus, the ability of tau and alpha-synuclein to affect each other directly or indirectly might contribute to the overlap in the clinical and pathological features of tauopathies and synucleinopathies.
机译：胞质内的丝状聚集物，例如阿尔茨海默氏病中的神经原纤维缠结和帕金森氏病中的路易体，分别由蛋白质tau和α-突触核蛋白组成。这些病理性内含物直接与广泛的神经退行性疾病（称为“ tauopathies”和“ synucleinopathies”）的病因和发病机制有关。越来越多的证据表明，患有tauopathies和sucleinoinopathies的患者的病理学和临床特征经常重叠，从而再次证明了这些疾病可能是机械性联系的观念。确实，一些研究表明tau和α-突触核蛋白可能构成一类独特的非结构化蛋白质，主要组装成均聚（而非杂聚）原纤维，该原纤维主要沉积在单独的淀粉样蛋白内含物中，但偶尔沉积在一起。因此，tau和α-突触核蛋白直接或间接相互影响的能力可能会导致陶氏病和突触核蛋白病的临床和病理特征重叠。

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