α-突触核蛋白原纤维对免疫细胞的细胞毒性研究。

IF 2.5 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Mikhail Matveyenka , Abid Ali , Charles L. Mitchell , Mikhail Sholukh , Dmitry Kurouski
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引用次数: 0

摘要

α-突触核蛋白(α-Syn)是一种参与细胞囊泡运输的小细胞质蛋白,在中脑、下丘脑和丘脑中逐渐聚集与帕金森病(PD)有关。淀粉样蛋白低聚物和原纤维是这种聚集的结果,对神经元具有高度毒性。然而,淀粉样蛋白诱导的神经元毒性是否是PD患者进行性神经变性的主要机制尚不清楚。在目前的研究中,我们研究了在无脂环境中以及两种磷脂存在下形成的α-Syn原纤维对巨噬细胞、树突状细胞和小胶质细胞的细胞毒性。我们发现α-Syn原纤维对树突细胞和小胶质细胞的毒性比神经元大得多。我们还观察到这种淀粉样蛋白对巨噬细胞的毒性很低。实时聚合酶链反应(RT-PCR)结果表明,淀粉样蛋白聚集体的毒性与细胞自噬水平有关。这些结果表明,大脑免疫系统的严重损伤可能是PD发病时发生的神经退行性过程的第一站。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Elucidation of cytotoxicity of α-Synuclein fibrils on immune cells
Progressive aggregation of α-synuclein (α-Syn), a small cytosolic protein involved in cell vesicle trafficking, in the midbrain, hypothalamus, and thalamus is linked to Parkinson's disease (PD). Amyloid oligomers and fibrils formed as a result of such aggregation are highly toxic to neurons. However, it remains unclear whether amyloid-induced toxicity of neurons is the primary mechanism of the progressive neurodegeneration observed upon PD. In the current study, we investigated cytotoxicity exerted by α-Syn fibrils formed in the lipid-free environment, as well as in the presence of two phospholipids, on macrophages, dendritic cells, and microglia. We found that α-Syn fibrils are far more toxic to dendritic cells and microglia compared to neurons. We also observe low toxicity levels of such amyloids to macrophages. Real-time polymerase chain reaction (RT-PCR) results suggest that toxicity of amyloids aggregates is linked to the levels of autophagy in cells. These results suggest that a strong impairment of the immune system in the brain may be the first stop of neurodegenerative processes that are taking place upon the onset of PD.
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来源期刊
CiteScore
8.00
自引率
0.00%
发文量
55
审稿时长
33 days
期刊介绍: BBA Proteins and Proteomics covers protein structure conformation and dynamics; protein folding; protein-ligand interactions; enzyme mechanisms, models and kinetics; protein physical properties and spectroscopy; and proteomics and bioinformatics analyses of protein structure, protein function, or protein regulation.
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