Subcellular distribution of the prion protein in sickness and in health.

摘要: Abstract The cellular prion protein (PrP C ) is an ubiquitously expressed glycoprotein that most abundant in the central nervous system. It thought to play a role many processes, including neuroprotection, but may also contribute Alzheimer's disease and some cancers. However, it best known for its diseases, such as Creutzfeldt-Jakob (CJD), bovine spongiform encephalopathy (BSE), scrapie. These misfolding diseases can be sporadic, acquired, or genetic are caused by refolding of endogenous PrP into beta sheet-rich, pathogenic form, Sc . Once prions present system, they increase spread during long incubation period followed relatively short clinical phase, ending death. molecules broadly categorized either ‘good’ (cellular) ‘bad’ (scrapie prion-type) , both populations heterogeneous different forms influence various activities. Both localized predominantly at cell surface, with C-terminus attached plasma membrane via glycosyl-phosphatidylinositol (GPI) anchor exist cleaved forms. has cytosolic transmembrane forms, variety conformations aggregation states. Here, we discuss roles isoforms sickness health, show subcellular distributions several particularly relevant conversion prion-induced pathology hippocampus.