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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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Detalles Bibliográficos
Autores principales: Cheng, Ying, Bai, Feng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5874499/
https://www.ncbi.nlm.nih.gov/pubmed/29623026
http://dx.doi.org/10.3389/fnins.2018.00163
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author Cheng, Ying
Bai, Feng
author_facet Cheng, Ying
Bai, Feng
author_sort Cheng, Ying
collection PubMed
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.
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spelling pubmed-58744992018-04-05 The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease Cheng, Ying Bai, Feng Front Neurosci Neuroscience 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. Frontiers Media S.A. 2018-03-22 /pmc/articles/PMC5874499/ /pubmed/29623026 http://dx.doi.org/10.3389/fnins.2018.00163 Text en Copyright © 2018 Cheng and Bai. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Cheng, Ying
Bai, Feng
The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title 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_short The Association of Tau With Mitochondrial Dysfunction in Alzheimer's Disease
title_sort association of tau with mitochondrial dysfunction in alzheimer's disease
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5874499/
https://www.ncbi.nlm.nih.gov/pubmed/29623026
http://dx.doi.org/10.3389/fnins.2018.00163
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