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2
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α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.α-突触核蛋白和亨廷顿蛋白外显子1淀粉样原纤维横向结合到细胞膜上。
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本文引用的文献

1
Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death.外源性α-突触核蛋白纤维诱导路易体病理，导致突触功能障碍和神经元死亡。
Neuron. 2011 Oct 6;72(1):57-71. doi: 10.1016/j.neuron.2011.08.033.
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Hsc70 protein interaction with soluble and fibrillar alpha-synuclein.热休克蛋白 70 与可溶性和纤维状α-突触核蛋白的相互作用。
J Biol Chem. 2011 Oct 7;286(40):34690-9. doi: 10.1074/jbc.M111.261321. Epub 2011 Aug 10.
3
α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells.α-突触核蛋白从老鼠大脑传播到移植的多巴胺能神经元，并在培养的人类细胞中引发聚集。
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Prion-like transmission of protein aggregates in neurodegenerative diseases.蛋白聚集物在神经退行性疾病中的朊病毒样传播。
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Heat shock proteins as suppressors of accumulation of toxic prefibrillar intermediates and misfolded proteins in neurodegenerative diseases.热休克蛋白作为抑制神经退行性疾病中有毒前纤维中间产物和错误折叠蛋白积累的抑制剂。
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Pathogenesis of Parkinson's disease: emerging role of molecular chaperones.帕金森病的发病机制：分子伴侣的作用日益凸显。
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The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states.E46K突变对α-突触核蛋白单体和寡聚体状态下性质的影响。
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Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels.热休克蛋白70（Hsc70）和热休克蛋白70（Hsp70）对上皮钠通道细胞内运输和功能表达的不同影响。
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Stages in the development of Parkinson's disease-related pathology.帕金森病相关病理学的发展阶段。
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热休克蛋白70（Hsc70）蛋白与纤维状α-突触核蛋白的相互作用及其在帕金森病中的治疗潜力。

The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson's disease.

作者信息

Pemberton Samantha, Melki Ronald

机构信息

Laboratoire d'Enzymologie et Biochimie Structurales; CNRS; Gif-sur-Yvette, France.

出版信息

Commun Integr Biol. 2012 Jan 1;5(1):94-5. doi: 10.4161/cib.18483.

DOI:10.4161/cib.18483
PMID:22482021
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3291325/
Abstract

We recently described the effect of the constitutively expressed chaperone, Hsc70 protein, on α‑Synuclein aggregation, a phenomenon associated with Parkinson disease. In vitro, Hsc70 binds to soluble α‑Syn and slows down its assembly into fibrils. Hsc70 also binds fibrillar α‑Syn, 5-fold tighter than soluble α‑Syn. This interaction reduces the cytotoxicity associated with naked α‑Syn fibrils. Herein, we discuss the feasibility of engineering a "minichaperone" which could be used against α‑Syn assembly propagation in Parkinson disease: taking what is necessary and sufficient within Hsc70 to protect against the damaging repercussions of high molecular weight α‑Syn species' passage from one neuron to another in the brain.

摘要

我们最近描述了组成型表达的伴侣蛋白Hsc70对α-突触核蛋白聚集的影响，这是一种与帕金森病相关的现象。在体外，Hsc70与可溶性α-突触核蛋白结合，并减缓其组装成纤维的过程。Hsc70还与纤维状α-突触核蛋白结合，其结合力比可溶性α-突触核蛋白强5倍。这种相互作用降低了与裸露的α-突触核蛋白纤维相关的细胞毒性。在此，我们讨论了设计一种“微型伴侣蛋白”的可行性，该蛋白可用于对抗帕金森病中α-突触核蛋白组装的传播：即利用Hsc70中必要且充分的部分来防止高分子量α-突触核蛋白在大脑中从一个神经元传递到另一个神经元所产生的有害影响。