The number of the people affected by neurodegenerative disorders is growing dramatically due to the ageing of population. The major neurodegenerative diseases share some common pathological features including the involvement of mitochondria in the mechanism of pathology and misfolding and the accumulation of abnormally aggregated proteins. Neurotoxicity of aggregated β-amyloid, tau, α-synuclein and huntingtin is linked to the effects of these proteins on mitochondria. All these misfolded aggregates affect mitochondrial energy metabolism by inhibiting diverse mitochondrial complexes and limit ATP availability in neurones. β-Amyloid, tau, α-synuclein and huntingtin are shown to be involved in increased production of reactive oxygen species, which can be generated in mitochondria or can target this organelle. Most of these aggregated proteins are capable of deregulating mitochondrial calcium handling that, in combination with oxidative stress, lead to opening of the mitochondrial permeability transition pore. Despite some of the common features, aggregated β-amyloid, tau, α-synuclein and huntingtin have diverse targets in mitochondria that can partially explain neurotoxic effect of these proteins in different brain regions.
Skip Nav Destination
Article navigation
August 2017
-
Cover Image
Cover Image
Activating and inhibitory long non-coding RNAs of the NF-κβ canonical pathway. In this issue, Magagula et al. explore the lncRNAs that are directly involved in regulating innate immunity at various branches of the NF-κβ pathway, and also consider their potential diagnostic and therapeutic significance. For further details, see pages 953–962
Review Article|
July 21 2017
Interaction of misfolded proteins and mitochondria in neurodegenerative disorders
Andrey Y. Abramov;
1Department of Molecular Neuroscience, UCL Institute of Neurology, London WC1N 3BG, U.K.
Correspondence: Andrey Y. Abramov (a.abramov@ucl.ac.uk)
Search for other works by this author on:
Alexey V. Berezhnov;
Alexey V. Berezhnov
2Institute of Cell Biophysics Russian Academy of Sciences, Pushchino 142290, Russia
Search for other works by this author on:
Evgeniya I. Fedotova;
Evgeniya I. Fedotova
2Institute of Cell Biophysics Russian Academy of Sciences, Pushchino 142290, Russia
Search for other works by this author on:
Valery P. Zinchenko;
Valery P. Zinchenko
2Institute of Cell Biophysics Russian Academy of Sciences, Pushchino 142290, Russia
Search for other works by this author on:
Ludmila P. Dolgacheva
Ludmila P. Dolgacheva
2Institute of Cell Biophysics Russian Academy of Sciences, Pushchino 142290, Russia
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
May 18 2017
Revision Received:
June 20 2017
Accepted:
June 23 2017
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (4): 1025–1033.
Article history
Received:
May 18 2017
Revision Received:
June 20 2017
Accepted:
June 23 2017
Citation
Andrey Y. Abramov, Alexey V. Berezhnov, Evgeniya I. Fedotova, Valery P. Zinchenko, Ludmila P. Dolgacheva; Interaction of misfolded proteins and mitochondria in neurodegenerative disorders. Biochem Soc Trans 15 August 2017; 45 (4): 1025–1033. doi: https://doi.org/10.1042/BST20170024
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.