Prion-like features of misfolded Aβ and tau aggregates
Prion-like features of misfolded Aβ and tau aggregates
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DOI：
10.1016/j.virusres.2014.12.031
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发表时间：
2015-09-02
期刊：
影响因子：
5
通讯作者：
Soto, Claudio
中科院分区：
文献类型：
--
作者：
Morales, Rodrigo;Callegari, Keri;Soto, Claudio
最近的研究表明，一些错误折叠的蛋白质可以通过将其构象特性转移到正常折叠的单位，以朊病毒样的方式传播疾病的发病机制。然而，这些分子到分子或细胞到细胞的传播过程反映整个朊病毒行为的程度现在是有争议的，特别是由于缺乏流行病学数据支持非朊病毒蛋白错误折叠疾病的个体间传播。然而，广泛的研究表明，当在动物模型中施用时，可以观察到AP和tau聚集体的朊病毒的几个典型特征。在这篇文章中，我们回顾了最近的研究，描述了朊病毒样的功能，这两种蛋白质，突出了真正的朊病毒的相似性，在个人间的传输，其应变样构象多样性，和传输的错误折叠的聚集体通过不同途径的管理。(C)2015爱思唯尔B.V.保留所有权利。
Recent findings have shown that several misfolded proteins can transmit disease pathogenesis in a prion-like manner by transferring their conformational properties to normally folded units. However, the extent by which these molecule-to-molecule or cell-to-cell spreading processes reflect the entire prion behavior is now subject of controversy, especially due to the lack of epidemiological data supporting inter-individual transmission of non-prion protein misfolding diseases. Nevertheless, extensive research has shown that several of the typical characteristics of prions can be observed for AP and tau aggregates when administered in animal models. In this article we review recent studies describing the prion-like features of both proteins, highlighting the similarities with bona fide prions in terms of inter-individual transmission, their strain-like conformational diversity, and the transmission of misfolded aggregates by different routes of administration. (C) 2015 Elsevier B.V. All rights reserved.