Sabate Raimon
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.
Prion. 2014;8(3):233-9. doi: 10.4161/19336896.2014.968464. Epub 2014 May 15.
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.
与蛋白质聚集成淀粉样构象相关的构象疾病，范围从非传染性神经退行性疾病，如阿尔茨海默病（AD），到高度传染性疾病，如人类可传播性海绵状脑病（TSEs）。它们通常被称为朊病毒疾病。然而，由于所有淀粉样蛋白都可被视为朊病毒（从参与细胞间传播的那些到负责真正神经元侵袭的那些），有必要找出每种易于形成淀粉样蛋白的蛋白质感染能力不同的潜在原因。如本文所提出的，内在细胞毒性和每个细胞的聚集核数量可能是每种淀粉样蛋白这种传播能力的关键因素。
