淀粉样前体蛋白与线粒体。
Amyloid precursor protein and mitochondria.
机构信息
University of Kansas Alzheimer's Disease Center, Kansas City, KS, USA; Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA. Electronic address: https://twitter.com/OneDayDrTay.
University of Kansas Alzheimer's Disease Center, Kansas City, KS, USA; Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA; Department of Neurology University of Kansas Medical Center, Kansas City, KS, USA.
出版信息
Curr Opin Neurobiol. 2023 Feb;78:102651. doi: 10.1016/j.conb.2022.102651. Epub 2022 Nov 30.
Amyloid Precursor Protein (APP) processing to amyloid beta (Aβ) is a major hallmark of Alzheimer's disease (AD). The amyloid cascade hypothesis postulates that Aβ accumulation and aggregation causes AD, however many therapeutics targeting Aβ have failed recently. Decades of research describe metabolic deficits in AD. Mitochondrial dysfunction is observed in AD subjects within the brain and systemically. APP and γ-secretase are localized to mitochondria. APP can be processed within mitochondria and its localization to mitochondria affects function. Here we discuss the evidence showing APP and γ-secretase localize to mitochondria. We also discuss the implications for the function of APP and its cleavage products in regulating mitochondrial function.
淀粉样前体蛋白 (APP) 加工为淀粉样 β (Aβ) 是阿尔茨海默病 (AD) 的主要标志。淀粉样蛋白级联假说假定 Aβ 的积累和聚集导致 AD，然而最近许多针对 Aβ 的治疗方法都失败了。几十年来的研究描述了 AD 中的代谢缺陷。在 AD 患者的大脑和全身中观察到线粒体功能障碍。APP 和 γ-分泌酶位于线粒体中。APP 可以在线粒体中被加工，其在线粒体中的定位会影响功能。在这里，我们讨论了表明 APP 和 γ-分泌酶定位于线粒体的证据。我们还讨论了 APP 及其裂解产物在调节线粒体功能中的作用的意义。
Zotero 插件