Jaunmuktane, Z;
Brandner, S;
(2020)
The role of prion-like mechanisms in neurodegenerative diseases.
Neuropathology and Applied Neurobiology
10.1111/nan.12592.
(In press).
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Abstract
The prototype of transmissible neurodegenerative proteinopathies is prion disease, characterised by aggregation of abnormally folded conformers of the native prion protein. A wealth of mechanisms have 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 (Aβ 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 Aβ, 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 summarise the most recent literature on transmissibility of neurodegenerative disorders.
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