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Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration

1
Department of Clinical and Movement Neurosciences, UCL Queen Square Institute of Neurology, Queen Square, London WC1N 3BG, UK
2
Cell Physiology and Pathology Laboratory, Orel State University, Orel 302026, Russia
3
Aston Institute of Photonic Technologies, School of Engineering and Applied Science, Aston University, Birmingham B4 7ET, UK
*
Author to whom correspondence should be addressed.
Life 2020, 10(7), 101; https://doi.org/10.3390/life10070101
Received: 30 May 2020 / Revised: 21 June 2020 / Accepted: 28 June 2020 / Published: 30 June 2020
Aggregation of the misfolded proteins β-amyloid, tau, huntingtin, and α-synuclein is one of the most important steps in the pathology underlying a wide spectrum of neurodegenerative disorders, including the two most common ones—Alzheimer's and Parkinson's disease. Activity and toxicity of these proteins depends on the stage and form of aggregates. Excessive production of free radicals, including reactive oxygen species which lead to oxidative stress, is proven to be involved in the mechanism of pathology in most of neurodegenerative disorders. Both reactive oxygen species and misfolded proteins play a physiological role in the brain, and only deregulation in redox state and aggregation of the proteins leads to pathology. Here, we review the role of misfolded proteins in the activation of ROS production from various sources in neurons and glia. We discuss if free radicals can influence structural changes of the key toxic intermediates and describe the putative mechanisms by which oxidative stress and oligomers may cause neuronal death.
Keywords: neurodegeneration; reactive oxygen species; β-amyloid; α-synuclein; tau protein; mutant huntingtin protein; oxidative stress neurodegeneration; reactive oxygen species; β-amyloid; α-synuclein; tau protein; mutant huntingtin protein; oxidative stress
MDPI and ACS Style

Abramov, A.Y.; Potapova, E.V.; Dremin, V.V.; Dunaev, A.V. Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration. Life 2020, 10, 101.

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