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 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.
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.
Magdalini
M
Polymenidou
Don W
DW
Cleveland
D000690:Amyotrophic Lateral Sclerosis / Q000378:metabolism*; D000818:Animals; D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism; D011328:Prions / Q000378:metabolism*; D017510:Protein Folding
D011328:Prions