Invited Review: The role of prion-like mechanisms in neurodegenerative diseases.
Neuropathol Appl Neurobiol
; 46(6): 522-545, 2020 10.
Article
em En
| MEDLINE
| ID: mdl-31868945
ABSTRACT
The prototype of transmissible neurodegenerative proteinopathies is prion diseases, characterized by aggregation of abnormally folded conformers of the native prion protein. A wealth of mechanisms has been proposed to explain the conformational conversion from physiological protein into misfolded, pathological form, mode of toxicity, propagation from cell-to-cell and regional spread. There is increasing evidence that other neurodegenerative diseases, most notably Alzheimer's disease (Aß and tau), Parkinson's disease (α-synuclein), frontotemporal dementia (TDP43, tau or FUS) and motor neurone disease (TDP43), exhibit at least some of the misfolded prion protein properties. In this review, we will discuss to what extent each of the properties of misfolded prion protein is known to occur for Aß, tau, α-synuclein and TDP43, with particular focus on self-propagation through seeding, conformational strains, selective cellular and regional vulnerability, stability and resistance to inactivation, oligomers, toxicity and summarize the most recent literature on transmissibility of neurodegenerative disorders.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Doenças Priônicas
/
Doenças Neurodegenerativas
/
Proteínas Priônicas
Limite:
Humans
Idioma:
En
Revista:
Neuropathol Appl Neurobiol
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Reino Unido