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Methionine oxidation within the prion protein.
Prion ( IF 1.9 ) Pub Date : 2020-08-02 , DOI: 10.1080/19336896.2020.1796898
John Bettinger 1 , Sina Ghaemmaghami 1
Affiliation  

ABSTRACT

Prion diseases are characterized by the self-templated misfolding of the cellular prion protein (PrPC) into infectious aggregates (PrPSc). The detailed molecular basis of the misfolding and aggregation of PrPC remains incompletely understood. It is believed that the transient misfolding of PrPC into partially structured intermediates precedes the formation of insoluble protein aggregates and is a critical component of the prion misfolding pathway. A number of environmental factors have been shown to induce the destabilization of PrPC and promote its initial misfolding. Recently, oxidative stress and reactive oxygen species (ROS) have emerged as one possible mechanism by which the destabilization of PrPC can be induced under physiological conditions. Methionine residues are uniquely vulnerable to oxidation by ROS and the formation of methionine sulfoxides leads to the misfolding and subsequent aggregation of PrPC. Here, we provide a review of the evidence for the oxidation of methionine residues in PrPC and its potential role in the formation of pathogenic prion aggregates.



中文翻译:


朊病毒蛋白内的甲硫氨酸氧化。


 抽象的


朊病毒疾病的特征是细胞朊病毒蛋白(PrP C )自我模板错误折叠成感染性聚集体(PrP Sc )。 PrP C错误折叠和聚集的详细分子基础仍不完全清楚。据信,PrP C短暂错误折叠成部分结构化中间体先于不溶性蛋白质聚集体的形成,并且是朊病毒错误折叠途径的关键组成部分。许多环境因素已被证明会导致 PrP C不稳定并促进其最初的错误折叠。最近,氧化应激和活性氧(ROS)已成为在生理条件下诱导 PrP C不稳定的一种可能机制。蛋氨酸残基特别容易被 ROS 氧化,蛋氨酸亚砜的形成会导致 PrP C的错误折叠和随后的聚集。在这里,我们回顾了 PrP C中蛋氨酸残基的氧化及其在致病性朊病毒聚集体形成中的潜在作用的证据。

更新日期:2020-08-02
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