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Are synucleinopathies prion-like disorders?

Angot, Elodie LU ; Steiner, Jennifer LU ; Hansen, Christian LU ; Li, Jia-Yi LU and Brundin, Patrik LU (2010) In Lancet Neurology Okt. p.1128-1138
Abstract
A shared neuropathological feature of idiopathic Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy is the development of intracellular aggregates of α-synuclein that gradually engage increasing parts of the nervous system. The pathogenetic mechanisms underlying these neurodegenerative disorders, however, are unknown. Several studies have highlighted similarities between classic prion diseases and these neurological proteinopathies. Specifically, identification of Lewy bodies in fetal mesencephalic neurons transplanted in patients with Parkinson's disease raised the hypothesis that α-synuclein, the main component of Lewy bodies, could be transmitted from the host brain to a graft of healthy neurons. These results... (More)
A shared neuropathological feature of idiopathic Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy is the development of intracellular aggregates of α-synuclein that gradually engage increasing parts of the nervous system. The pathogenetic mechanisms underlying these neurodegenerative disorders, however, are unknown. Several studies have highlighted similarities between classic prion diseases and these neurological proteinopathies. Specifically, identification of Lewy bodies in fetal mesencephalic neurons transplanted in patients with Parkinson's disease raised the hypothesis that α-synuclein, the main component of Lewy bodies, could be transmitted from the host brain to a graft of healthy neurons. These results and others have led to the hypothesis that a prion-like mechanism might underlie progression of synucleinopathy within the nervous system. We review experimental findings showing that misfolded α-synuclein can transfer between cells and, once transferred into a new cell, can act as a seed that recruits endogenous α-synuclein, leading to formation of larger aggregates. This model suggests that strategies aimed at prevention of cell-to-cell transfer of α-synuclein could retard progression of symptoms in Parkinson's disease and other synucleinopathies. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
in
Lancet Neurology
volume
Okt
pages
1128 - 1138
publisher
Lancet Publishing Group
external identifiers
  • wos:000284246800021
  • pmid:20846907
  • scopus:77957939093
ISSN
1474-4465
DOI
10.1016/S1474-4422(10)70213-1
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Neuronal Survival (013212041), Neural Plasticity and Repair (013210080)
id
1dfbd49d-a09a-468f-9d79-c67a4dad8dd8 (old id 1688149)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/20846907?dopt=Abstract
date added to LUP
2016-04-04 08:33:43
date last changed
2022-05-16 21:29:41
@article{1dfbd49d-a09a-468f-9d79-c67a4dad8dd8,
  abstract     = {{A shared neuropathological feature of idiopathic Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy is the development of intracellular aggregates of α-synuclein that gradually engage increasing parts of the nervous system. The pathogenetic mechanisms underlying these neurodegenerative disorders, however, are unknown. Several studies have highlighted similarities between classic prion diseases and these neurological proteinopathies. Specifically, identification of Lewy bodies in fetal mesencephalic neurons transplanted in patients with Parkinson's disease raised the hypothesis that α-synuclein, the main component of Lewy bodies, could be transmitted from the host brain to a graft of healthy neurons. These results and others have led to the hypothesis that a prion-like mechanism might underlie progression of synucleinopathy within the nervous system. We review experimental findings showing that misfolded α-synuclein can transfer between cells and, once transferred into a new cell, can act as a seed that recruits endogenous α-synuclein, leading to formation of larger aggregates. This model suggests that strategies aimed at prevention of cell-to-cell transfer of α-synuclein could retard progression of symptoms in Parkinson's disease and other synucleinopathies.}},
  author       = {{Angot, Elodie and Steiner, Jennifer and Hansen, Christian and Li, Jia-Yi and Brundin, Patrik}},
  issn         = {{1474-4465}},
  language     = {{eng}},
  pages        = {{1128--1138}},
  publisher    = {{Lancet Publishing Group}},
  series       = {{Lancet Neurology}},
  title        = {{Are synucleinopathies prion-like disorders?}},
  url          = {{http://dx.doi.org/10.1016/S1474-4422(10)70213-1}},
  doi          = {{10.1016/S1474-4422(10)70213-1}},
  volume       = {{Okt}},
  year         = {{2010}},
}