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Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease
Alpha-synuclein is a presynaptic protein expressed throughout the central nervous system, and it is the main component of Lewy bodies, one of the histopathological features of Parkinson's disease (PD) which is a progressive and irreversible neurodegenerative disorder. The conformational flexibi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4353246/ https://www.ncbi.nlm.nih.gov/pubmed/25805964 http://dx.doi.org/10.3389/fnins.2015.00059 |
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author | Gallegos, Scarlet Pacheco, Carla Peters, Christian Opazo, Carlos M. Aguayo, Luis G. |
author_facet | Gallegos, Scarlet Pacheco, Carla Peters, Christian Opazo, Carlos M. Aguayo, Luis G. |
author_sort | Gallegos, Scarlet |
collection | PubMed |
description | Alpha-synuclein is a presynaptic protein expressed throughout the central nervous system, and it is the main component of Lewy bodies, one of the histopathological features of Parkinson's disease (PD) which is a progressive and irreversible neurodegenerative disorder. The conformational flexibility of α-synuclein allows it to adopt different conformations, i.e., bound to membranes or form aggregates, the oligomers are believed to be the more toxic species. In this review, we will focus on two major features of α-synuclein, transmission and toxicity, that could help to understand the pathological characteristics of PD. One important feature of α-synuclein is its ability to be transmitted from neuron to neuron using mechanisms such as endocytosis, plasma membrane penetration or through exosomes, thus propagating the Lewy body pathology to different brain regions thereby contributing to the progressiveness of PD. The second feature of α-synuclein is that it confers cytotoxicity to recipient cells, principally when it is in an oligomeric state. This form causes mitochondrial dysfunction, endoplasmic reticulum stress, oxidative stress, proteasome impairment, disruption of plasma membrane and pore formation that lead to apoptosis pathway activation and consequent cell death. The complexity of α-synuclein oligomerization and formation of toxic species could be a major factor for the irreversibility of PD and could also explain the lack of successful therapies to halt the disease. |
format | Online Article Text |
id | pubmed-4353246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-43532462015-03-24 Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease Gallegos, Scarlet Pacheco, Carla Peters, Christian Opazo, Carlos M. Aguayo, Luis G. Front Neurosci Psychiatry Alpha-synuclein is a presynaptic protein expressed throughout the central nervous system, and it is the main component of Lewy bodies, one of the histopathological features of Parkinson's disease (PD) which is a progressive and irreversible neurodegenerative disorder. The conformational flexibility of α-synuclein allows it to adopt different conformations, i.e., bound to membranes or form aggregates, the oligomers are believed to be the more toxic species. In this review, we will focus on two major features of α-synuclein, transmission and toxicity, that could help to understand the pathological characteristics of PD. One important feature of α-synuclein is its ability to be transmitted from neuron to neuron using mechanisms such as endocytosis, plasma membrane penetration or through exosomes, thus propagating the Lewy body pathology to different brain regions thereby contributing to the progressiveness of PD. The second feature of α-synuclein is that it confers cytotoxicity to recipient cells, principally when it is in an oligomeric state. This form causes mitochondrial dysfunction, endoplasmic reticulum stress, oxidative stress, proteasome impairment, disruption of plasma membrane and pore formation that lead to apoptosis pathway activation and consequent cell death. The complexity of α-synuclein oligomerization and formation of toxic species could be a major factor for the irreversibility of PD and could also explain the lack of successful therapies to halt the disease. Frontiers Media S.A. 2015-03-09 /pmc/articles/PMC4353246/ /pubmed/25805964 http://dx.doi.org/10.3389/fnins.2015.00059 Text en Copyright © 2015 Gallegos, Pacheco, Peters, Opazo and Aguayo. 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) or licensor 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 | Psychiatry Gallegos, Scarlet Pacheco, Carla Peters, Christian Opazo, Carlos M. Aguayo, Luis G. Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title | Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title_full | Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title_fullStr | Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title_full_unstemmed | Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title_short | Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease |
title_sort | features of alpha-synuclein that could explain the progression and irreversibility of parkinson's disease |
topic | Psychiatry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4353246/ https://www.ncbi.nlm.nih.gov/pubmed/25805964 http://dx.doi.org/10.3389/fnins.2015.00059 |
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