From nucleation to widespread propagation: A prion-like concept for ALS.

Maniecka Z; Polymenidou M

doi:10.1016/j.virusres.2014.12.032

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Journal article

From nucleation to widespread propagation: A prion-like concept for ALS.

Maniecka Z Institute of Molecular Life Sciences, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
Polymenidou M Institute of Molecular Life Sciences, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. Electronic address: magdalini.polymenidou@imls.uzh.ch.

2015-02-07

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Virus research. - 2015

Protein Aggregation, Pathological

English Propagation of pathological protein assemblies via a prion-like mechanism has been suggested to drive neurodegenerative diseases, such as Parkinson's and Alzheimer's. Recently, amyotrophic lateral sclerosis (ALS)-linked proteins, such as SOD1, TDP-43 and FUS were shown to follow self-perpetuating seeded aggregation, thereby adding ALS to the group of prion-like disorders. The cell-to-cell spread of these pathological protein assemblies and their pathogenic mechanism is poorly understood. However, as ALS is a non-cell autonomous disease and pathology in glial cells was shown to contribute to motor neuron damage, spreading mechanisms are likely to underlie disease progression via the interplay between affected neurons and their neighboring glial cells.

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