The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease

Increasing evidence suggests that abnormally hyperphosphorylated tau plays a vital role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial dysfunction also has a recognized role in the pathophysiology of AD. In recent years, mitochondrial dysfunction has been strongly associated wit...

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Main Authors: Ying Cheng, Feng Bai
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-03-01
Series:Frontiers in Neuroscience
Subjects:
tau
Online Access:http://journal.frontiersin.org/article/10.3389/fnins.2018.00163/full
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spelling doaj-9ba8be611a16446da37f1bd1a50d0bb82020-11-24T22:28:20ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2018-03-011210.3389/fnins.2018.00163320523The Association of Tau With Mitochondrial Dysfunction in Alzheimer's DiseaseYing Cheng0Feng Bai1Department of Neurology, Affiliated ZhongDa Hospital, School of Medicine, Southeast University, Nanjing, ChinaDepartment of Neurology, Drum Tower Hospital, Medical School of Nanjing University, Nanjing, ChinaIncreasing evidence suggests that abnormally hyperphosphorylated tau plays a vital role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial dysfunction also has a recognized role in the pathophysiology of AD. In recent years, mitochondrial dysfunction has been strongly associated with tau pathology in AD. Overexpression of hyperphosphorylated and aggregated tau appears to damage the axonal transport, leading to abnormal mitochondrial distribution. In addition, pathological tau impairs mitochondrial dynamics by regulating mitochondrial fission/fusion proteins, and further causes mitochondrial dysfunction and neuronal damage. Moreover, mitochondrial dysfunction is also involved in promoting tau pathology in AD. In this article, we evaluate the relationship between phosphorylated tau and mitochondrial dysfunction in AD.http://journal.frontiersin.org/article/10.3389/fnins.2018.00163/fullAlzheimer's diseasetaumitochondrial transportmitochondrial dynamicsmitochondrial dysfunction
collection DOAJ
language English
format Article
sources DOAJ
author Ying Cheng
Feng Bai
spellingShingle Ying Cheng
Feng Bai
The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
Frontiers in Neuroscience
Alzheimer's disease
tau
mitochondrial transport
mitochondrial dynamics
mitochondrial dysfunction
author_facet Ying Cheng
Feng Bai
author_sort Ying Cheng
title The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_short The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_full The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_fullStr The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_full_unstemmed The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_sort association of tau with mitochondrial dysfunction in alzheimer's disease
publisher Frontiers Media S.A.
series Frontiers in Neuroscience
issn 1662-453X
publishDate 2018-03-01
description Increasing evidence suggests that abnormally hyperphosphorylated tau plays a vital role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial dysfunction also has a recognized role in the pathophysiology of AD. In recent years, mitochondrial dysfunction has been strongly associated with tau pathology in AD. Overexpression of hyperphosphorylated and aggregated tau appears to damage the axonal transport, leading to abnormal mitochondrial distribution. In addition, pathological tau impairs mitochondrial dynamics by regulating mitochondrial fission/fusion proteins, and further causes mitochondrial dysfunction and neuronal damage. Moreover, mitochondrial dysfunction is also involved in promoting tau pathology in AD. In this article, we evaluate the relationship between phosphorylated tau and mitochondrial dysfunction in AD.
topic Alzheimer's disease
tau
mitochondrial transport
mitochondrial dynamics
mitochondrial dysfunction
url http://journal.frontiersin.org/article/10.3389/fnins.2018.00163/full
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