The Seeds of Neurodegeneration: Prion-like Spreading in ALS

Misfolded proteins accumulating in several neurodegenerative diseases (including Alzheimer, Parkinson, and Huntington diseases) can cause aggregation of their native counterparts through a mechanism similar to the infectious prion protein's induction of a pathogenic conformation onto its cellul...

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Bibliographic Details
Published in:Cell 2011-10, Vol.147 (3), p.498-508
Main Authors: Polymenidou, Magdalini, Cleveland, Don W.
Format: Article
Language:English
Subjects:
amyotrophic lateral sclerosis
Amyotrophic Lateral Sclerosis - metabolism
Animals
Humans
nervous system
Neurodegenerative Diseases - metabolism
Prion proteins
prions
Prions - metabolism
Protein Folding
seeds
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Summary:Misfolded proteins accumulating in several neurodegenerative diseases (including Alzheimer, Parkinson, and Huntington diseases) can cause aggregation of their native counterparts through a mechanism similar to the infectious prion protein's induction of a pathogenic conformation onto its cellular isoform. Evidence for such a prion-like mechanism has now spread to the main misfolded proteins, SOD1 and TDP-43, implicated in amyotrophic lateral sclerosis (ALS). The major neurodegenerative diseases may therefore have mechanistic parallels for non-cell-autonomous spread of disease within the nervous system.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2011.10.011