Abstract
The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer's disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion), it is necessary to find an underlying cause of the different capacity to infect that each of the proteins prone to form amyloids has. As proposed here, both the intrinsic cytotoxicity and the number of nuclei of aggregation per cell could be key factors in this transmission capacity of each amyloid.
Disclosure of Potential Conflicts of Interest
No potential conflicts of interest were disclosed.
Funding
I am the beneficiary of a contract under the Ramón y Cajal program financed by the Spanish Ministerio de Ciencia e Innovación.
Supplemental Material
Supplemental data for this article can be accessed on the publisher's website.