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Interaction of misfolded proteins and mitochondria in neurodegenerative disorders

Abramov, AY; Berezhnov, AV; Fedotova, EI; Zinchenko, VP; Dolgacheva, LP; (2017) Interaction of misfolded proteins and mitochondria in neurodegenerative disorders. Biochemical Society Transactions , 45 (4) pp. 1025-1033. 10.1042/BST20170024. Green open access

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Abstract

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.

Type: Article
Title: Interaction of misfolded proteins and mitochondria in neurodegenerative disorders
Open access status: An open access version is available from UCL Discovery
DOI: 10.1042/BST20170024
Publisher version: https://doi.org/10.1042/BST20170024
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, ALPHA-SYNUCLEIN, ALZHEIMERS-DISEASE, PARKINSONS-DISEASE, OXIDATIVE STRESS, CELL-DEATH, CALCIUM HOMEOSTASIS, HUNTINGTONS-DISEASE, NEURONAL DEATH, NADPH OXIDASE, TAU-PROTEIN
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Queen Square Institute of Neurology > Clinical and Movement Neurosciences
URI: https://discovery.ucl.ac.uk/id/eprint/1567529
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