When amyloids become prions.
The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer 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.
Conformational Diseases Group; Department of Physical Chemistry; Faculty of Pharmacy; University of Barcelona (UB); Barcelona, Spain; Institut of Nanoscience and Nanotechnology of the University of Barcelona (IN2UB); Barcelona, Spain.
Raimon
R
Sabate
D000544:Alzheimer Disease / Q000378:metabolism / Q000503:physiopathology; D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D035843:Biomedical Research; D007562:Creutzfeldt-Jakob Syndrome / Q000378:metabolism / Q000503:physiopathology; D006801:Humans; D051379:Mice; D011328:Prions / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D000682:Amyloid; D011328:Prions
Alzheimer disease; Creutzfeldt–Jakob disease; amyloid; amyloid cytotoxicity; amyloid transmission; prion; transmissible spongiform encephalopathy