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Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?

Parkinson's disease (PD), a progressive neurodegenerative disease primarily affecting voluntary and controlled movement, is characterized by abnormal accumulations of α-synuclein (α-syn) in intraneuronal Lewy bodies. In the last years, the increased number of evidences from both the in vitro an...

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Autores principales: Busquets, Maria Antònia, Espargaró, Alba, Estelrich, Joan, Sabate, Raimon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383319/
https://www.ncbi.nlm.nih.gov/pubmed/25866763
http://dx.doi.org/10.1155/2015/172018
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author Busquets, Maria Antònia
Espargaró, Alba
Estelrich, Joan
Sabate, Raimon
author_facet Busquets, Maria Antònia
Espargaró, Alba
Estelrich, Joan
Sabate, Raimon
author_sort Busquets, Maria Antònia
collection PubMed
description Parkinson's disease (PD), a progressive neurodegenerative disease primarily affecting voluntary and controlled movement, is characterized by abnormal accumulations of α-synuclein (α-syn) in intraneuronal Lewy bodies. In the last years, the increased number of evidences from both the in vitro and in vivo studies has shown the ability of α-syn to misfold in amyloid conformations and to spread via neuron-to-neuron transmission, suggesting a prion-like behaviour. However, in contrast to prion protein (PrP), α-syn transmission is far from neuronal invasion. The high neuronal toxicity of both mature fibres and oligomeric species, as well as the intracellular localization of the protein and the difficulty to be secreted, could be key factors impeding the prion ability of α-syn aggregates.
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spelling pubmed-43833192015-04-12 Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion? Busquets, Maria Antònia Espargaró, Alba Estelrich, Joan Sabate, Raimon Biomed Res Int Review Article Parkinson's disease (PD), a progressive neurodegenerative disease primarily affecting voluntary and controlled movement, is characterized by abnormal accumulations of α-synuclein (α-syn) in intraneuronal Lewy bodies. In the last years, the increased number of evidences from both the in vitro and in vivo studies has shown the ability of α-syn to misfold in amyloid conformations and to spread via neuron-to-neuron transmission, suggesting a prion-like behaviour. However, in contrast to prion protein (PrP), α-syn transmission is far from neuronal invasion. The high neuronal toxicity of both mature fibres and oligomeric species, as well as the intracellular localization of the protein and the difficulty to be secreted, could be key factors impeding the prion ability of α-syn aggregates. Hindawi Publishing Corporation 2015 2015-03-19 /pmc/articles/PMC4383319/ /pubmed/25866763 http://dx.doi.org/10.1155/2015/172018 Text en Copyright © 2015 Maria Antònia Busquets et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Busquets, Maria Antònia
Espargaró, Alba
Estelrich, Joan
Sabate, Raimon
Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title_full Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title_fullStr Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title_full_unstemmed Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title_short Could α-Synuclein Amyloid-Like Aggregates Trigger a Prionic Neuronal Invasion?
title_sort could α-synuclein amyloid-like aggregates trigger a prionic neuronal invasion?
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4383319/
https://www.ncbi.nlm.nih.gov/pubmed/25866763
http://dx.doi.org/10.1155/2015/172018
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