What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?

α-Synuclein is a key protein in Parkinson disease. Not only is it the major protein component of Lewy bodies, but it is implicated in several cellular processes that are disrupted in Parkinson disease. Misfolded α-synuclein has also been shown to spread from cell-to-cell and, in a prion-like fashion...

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Detalles Bibliográficos
Autores principales: Dunning, Christopher J.R., George, Sonia, Brundin, Patrik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Mini Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3609056/
https://www.ncbi.nlm.nih.gov/pubmed/23360753
http://dx.doi.org/10.4161/pri.23806
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author Dunning, Christopher J.R.
George, Sonia
Brundin, Patrik
author_facet Dunning, Christopher J.R.
George, Sonia
Brundin, Patrik
author_sort Dunning, Christopher J.R.
collection PubMed
description α-Synuclein is a key protein in Parkinson disease. Not only is it the major protein component of Lewy bodies, but it is implicated in several cellular processes that are disrupted in Parkinson disease. Misfolded α-synuclein has also been shown to spread from cell-to-cell and, in a prion-like fashion, trigger aggregation of α-synuclein in the recipient cell. In this mini-review we explore the evidence that misfolded α-synuclein underlies the spread of pathology in Parkinson disease and discuss why it should be considered a prion-like protein.
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spelling pubmed-36090562013-03-29 What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease? Dunning, Christopher J.R. George, Sonia Brundin, Patrik Prion Mini Review α-Synuclein is a key protein in Parkinson disease. Not only is it the major protein component of Lewy bodies, but it is implicated in several cellular processes that are disrupted in Parkinson disease. Misfolded α-synuclein has also been shown to spread from cell-to-cell and, in a prion-like fashion, trigger aggregation of α-synuclein in the recipient cell. In this mini-review we explore the evidence that misfolded α-synuclein underlies the spread of pathology in Parkinson disease and discuss why it should be considered a prion-like protein. Landes Bioscience 2013-01-01 /pmc/articles/PMC3609056/ /pubmed/23360753 http://dx.doi.org/10.4161/pri.23806 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Mini Review
Dunning, Christopher J.R.
George, Sonia
Brundin, Patrik
What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title_full What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title_fullStr What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title_full_unstemmed What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title_short What’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in Parkinson disease?
title_sort what’s to like about the prion-like hypothesis for the spreading of aggregated α-synuclein in parkinson disease?
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3609056/
https://www.ncbi.nlm.nih.gov/pubmed/23360753
http://dx.doi.org/10.4161/pri.23806
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