Spreading of α-synuclein in the face of axonal transport deficits in Parkinson's disease: A speculative synthesis.
(2015) In Neurobiology of Disease 77(Jul 15). p.276-283- Abstract
- Parkinson's disease (PD) is mainly attributed to degeneration of dopamine neurons in the substantia nigra, but its etiopathogenesis also includes impaired protein clearance and axonal transport dysfunction, among others. The spread of α-synuclein (α-syn) aggregates from one neuron to another, in a prion-like manner, is hypothesized to contribute to PD progression. Axonal transport is likely to play a crucial role in this movement of α-syn aggregates between brain regions. At the same time, deficits in axonal transport are suggested to contribute to neuronal failure in PD. In this review, we discuss the apparent contradiction that axonal transport might be essential for disease progression, while dysfunction of axonal transport could... (More)
- Parkinson's disease (PD) is mainly attributed to degeneration of dopamine neurons in the substantia nigra, but its etiopathogenesis also includes impaired protein clearance and axonal transport dysfunction, among others. The spread of α-synuclein (α-syn) aggregates from one neuron to another, in a prion-like manner, is hypothesized to contribute to PD progression. Axonal transport is likely to play a crucial role in this movement of α-syn aggregates between brain regions. At the same time, deficits in axonal transport are suggested to contribute to neuronal failure in PD. In this review, we discuss the apparent contradiction that axonal transport might be essential for disease progression, while dysfunction of axonal transport could simultaneously be a cornerstone of PD pathogenesis. We speculate around models that reconcile how axonal transport can play such a paradoxical role. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4581561
- author
- Lamberts, Jennifer T ; Hildebrandt, Erin and Brundin, Patrik LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Neurobiology of Disease
- volume
- 77
- issue
- Jul 15
- pages
- 276 - 283
- publisher
- Academic Press
- external identifiers
-
- pmid:25046996
- wos:000353612200025
- pmid:25046996
- scopus:84927598926
- ISSN
- 0969-9961
- DOI
- 10.1016/j.nbd.2014.07.002
- language
- English
- LU publication?
- yes
- id
- 9be8ee5d-3dde-4f06-bf3e-d400e96483e9 (old id 4581561)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/25046996?dopt=Abstract
- date added to LUP
- 2016-04-01 10:24:46
- date last changed
- 2025-01-14 14:04:12
@article{9be8ee5d-3dde-4f06-bf3e-d400e96483e9,
abstract = {{Parkinson's disease (PD) is mainly attributed to degeneration of dopamine neurons in the substantia nigra, but its etiopathogenesis also includes impaired protein clearance and axonal transport dysfunction, among others. The spread of α-synuclein (α-syn) aggregates from one neuron to another, in a prion-like manner, is hypothesized to contribute to PD progression. Axonal transport is likely to play a crucial role in this movement of α-syn aggregates between brain regions. At the same time, deficits in axonal transport are suggested to contribute to neuronal failure in PD. In this review, we discuss the apparent contradiction that axonal transport might be essential for disease progression, while dysfunction of axonal transport could simultaneously be a cornerstone of PD pathogenesis. We speculate around models that reconcile how axonal transport can play such a paradoxical role.}},
author = {{Lamberts, Jennifer T and Hildebrandt, Erin and Brundin, Patrik}},
issn = {{0969-9961}},
language = {{eng}},
number = {{Jul 15}},
pages = {{276--283}},
publisher = {{Academic Press}},
series = {{Neurobiology of Disease}},
title = {{Spreading of α-synuclein in the face of axonal transport deficits in Parkinson's disease: A speculative synthesis.}},
url = {{http://dx.doi.org/10.1016/j.nbd.2014.07.002}},
doi = {{10.1016/j.nbd.2014.07.002}},
volume = {{77}},
year = {{2015}},
}