The unfolded protein response is involved in the pathology of Alzheimer's disease
The unfolded protein response is involved in the pathology of Alzheimer's disease
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DOI：
10.1111/j.1749-6632.2002.tb04837.x
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发表时间：
2002-01-01
期刊：
影响因子：
--
通讯作者：
Takeda, M
中科院分区：
文献类型：
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作者：
Kudo, T;Katayama, T;Takeda, M
内质网（ER）完成蛋白质的合成、翻译后修饰和正确折叠。多种条件可以是ER应激，导致ER中未折叠或错误折叠蛋白质的积累。真核细胞有三种不同的机制来处理ER中未折叠蛋白的积累，称为未折叠蛋白反应（UPR）：转录诱导，翻译衰减和降解。本文就UPR与AD发病的关系作一综述。我们的研究结果表明一种新的机制，PS1突变可能会影响ER应力的传感。IRE1、PERK或eIF2 α磷酸化或GRP78表达的实验操作可能允许开发FAD的治疗策略。
The endoplasmic reticulum (ER) performs the synthesis, posttranslational modification, and proper folding of proteins. A variety of conditions can be ER stress, causing the accumulation of unfolding or misfolding proteins in the ER. Eukaryotic cells have three different mechanisms for dealing with an accumulation of unfolded proteins in the ER known as the unfolded protein response (UPR): transcriptional induction, translational attenuation, and degradation. This paper focuses on the relationship between UPR and the pathogenesis of AD. Our results indicate a new mechanism by which PS1 mutations may affect the sensing of ER stress. Experimental manipulation of IRE1, PERK, or eIF2alpha phosphorylation or GRP78 expression might allow the development of therapeutic strategies for FAD.