文献类型：期刊文献

英文题名：Accumulated amyloid-β peptide and hyperphosphorylated tau protein: Relationship and links in Alzheimer's disease

作者：Huang H.-C.[1,2,3];Jiang Z.-F.[1,2,3]

第一作者：Huang H.-C.

通讯作者：Huang, H.-C.[1,2,3]

机构：[1]Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing Union University, Beijing, China;[2]College of Arts and Sciences, Beijing Union University, Beijing, China;[3]Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing United University, Beijing 100083, China

第一机构：北京联合大学应用文理学院|北京联合大学生物化学工程学院

年份：2009

卷号：16

期号：1

起止页码：15-27

外文期刊名：Journal of Alzheimer's Disease

收录：Scopus(收录号：2-s2.0-58849143335)

语种：英文

外文关键词：Amyloid-β peptide (Aβ); Oxidative stress; PI3K/Akt; Tau protein; α7nAChR

摘要：The neuropathology associated with Alzheimer's disease (AD) is characterized by the presence of extracellularly neuritic plaques, intracellularly neurofibrillary tangles and the loss of basal forebrain cholinergic neurons. The neuritic plaque is composed of a core of amyloid-β peptide (Aβ) while the neurofibrillary tangles contain phosphorylated tau protein, and, as such, both Aβ and tau are important molecules associated with AD. In healthy human bodies, clearance mechanisms for Aβ are available; yet if clearance fails, Aβ accumulates, increasing the risk of neurotoxicity in the brain. Tau, one of the main microtubule-associated proteins, will be hyperphosphorylated and lose the ability to bind microtubules when the homeostasis of phosphorylation and dephosphorylation is disturbed in neurons. Accumulated Aβ and hyperphosphorylated tau are thought to be coexistent. Research on the pathological changes in AD indicates that accumulated Aβ in vivo may initiate the hyperphosphorylation of tau. Also, the signal transduction pathways of tau hyperphosphorylation may be related to accumulated Aβ. In this review, we will discuss how Aβ accumulates, how tau protein is hyperphosphorylated, and how accumulated Aβ initiates hyperphosphorylation of tau protein in AD. ? 2009 - IOS Press and the authors. All rights reserved.