From nucleation to widespread propagation: A prion-like concept for ALS.
Virus Res
; 207: 94-105, 2015 Sep 02.
Article
en En
| MEDLINE
| ID: mdl-25656065
ABSTRACT
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Superóxido Dismutasa
/
Proteína FUS de Unión a ARN
/
Proteínas de Unión al ADN
/
Agregación Patológica de Proteínas
/
Esclerosis Amiotrófica Lateral
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Virus Res
Asunto de la revista:
VIROLOGIA
Año:
2015
Tipo del documento:
Article
País de afiliación:
Suiza