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Cell. 2011 Oct 28;147(3):498-508. doi: 10.1016/j.cell.2011.10.011.

The seeds of neurodegeneration: prion-like spreading in ALS.

Author information

1
Ludwig Institute for Cancer Research and Department of Cellular and Molecular Medicine, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0670, USA.

Abstract

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.

PMID:
22036560
PMCID:
PMC3220614
DOI:
10.1016/j.cell.2011.10.011
[Indexed for MEDLINE]
Free PMC Article

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