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Dissecting the potential molecular mechanisms underlying alpha-synuclein cell-to-cell transfer in Parkinson's disease.

Angot, Elodie LU and Brundin, Patrik LU (2009) In Parkinsonism & Related Disorders 15 Suppl 3. p.143-147
Abstract
Alpha-synuclein (alpha-syn) aggregation is central to neuropathological changes in Parkinson's disease. The aggregates spread within the central nervous system according to a very predictable pattern. A prion-like transmission of alpha-syn aggregates has been recently proposed to explain this propagation pattern. First, we review the growing evidence for such a mechanism. This process is likely to occur in three consecutive steps: (i) exit of alpha-syn template from the donor cell, (ii) entry to the recipient cell and (iii) initiation of the nucleation. In a second part, we discuss the possible underlying mechanisms for each of these steps, based on our current knowledge about how cells handle alpha-syn but also other proteins involved in... (More)
Alpha-synuclein (alpha-syn) aggregation is central to neuropathological changes in Parkinson's disease. The aggregates spread within the central nervous system according to a very predictable pattern. A prion-like transmission of alpha-syn aggregates has been recently proposed to explain this propagation pattern. First, we review the growing evidence for such a mechanism. This process is likely to occur in three consecutive steps: (i) exit of alpha-syn template from the donor cell, (ii) entry to the recipient cell and (iii) initiation of the nucleation. In a second part, we discuss the possible underlying mechanisms for each of these steps, based on our current knowledge about how cells handle alpha-syn but also other proteins involved in neurodegenerative diseases with a prion-like propagation. Finally, we discuss which molecular species of alpha-syn (monomer, oligomer, fibril) could be the seeding-competent species and whether this seeding process could be a common mechanism in neurodegenerative diseases. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Parkinsonism & Related Disorders
volume
15 Suppl 3
pages
143 - 147
publisher
Elsevier
external identifiers
  • pmid:20082977
  • scopus:71849117852
ISSN
1873-5126
DOI
10.1016/S1353-8020(09)70802-8
language
English
LU publication?
yes
id
42897ebe-57fc-49c4-985f-b8a665904e6a (old id 1540493)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/20082977?dopt=Abstract
date added to LUP
2010-02-04 21:04:23
date last changed
2017-05-14 04:21:50
@article{42897ebe-57fc-49c4-985f-b8a665904e6a,
  abstract     = {Alpha-synuclein (alpha-syn) aggregation is central to neuropathological changes in Parkinson's disease. The aggregates spread within the central nervous system according to a very predictable pattern. A prion-like transmission of alpha-syn aggregates has been recently proposed to explain this propagation pattern. First, we review the growing evidence for such a mechanism. This process is likely to occur in three consecutive steps: (i) exit of alpha-syn template from the donor cell, (ii) entry to the recipient cell and (iii) initiation of the nucleation. In a second part, we discuss the possible underlying mechanisms for each of these steps, based on our current knowledge about how cells handle alpha-syn but also other proteins involved in neurodegenerative diseases with a prion-like propagation. Finally, we discuss which molecular species of alpha-syn (monomer, oligomer, fibril) could be the seeding-competent species and whether this seeding process could be a common mechanism in neurodegenerative diseases.},
  author       = {Angot, Elodie and Brundin, Patrik},
  issn         = {1873-5126},
  language     = {eng},
  pages        = {143--147},
  publisher    = {Elsevier},
  series       = {Parkinsonism & Related Disorders},
  title        = {Dissecting the potential molecular mechanisms underlying alpha-synuclein cell-to-cell transfer in Parkinson's disease.},
  url          = {http://dx.doi.org/10.1016/S1353-8020(09)70802-8},
  volume       = {15 Suppl 3},
  year         = {2009},
}