Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys.

摘要: Proteins aggregate in several slowly progressive neurodegenerative diseases called ‘proteinopathies’. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding aggregation other as well – a possible common mechanism for some diseases. However, most proteinopathies are ‘sporadic’, without gene mutation or overexpression. Thus, WT animals genetically close to humans might be informative. Squirrel monkeys infected the classical bovine spongiform encephalopathy agent developed an resembling variant Creutzfeldt–Jakob disease accumulations not only abnormal prion (PrPTSE), but also three proteins: hyperphosphorylated tau (p-tau), α-synuclein ubiquitin; β-amyloid (Aβ) did accumulate. Severity brain lesions correlated degeneration. No amyloid was detected. These results PrPTSE enhanced formation p-tau ubiquitin, Aβ, providing new experimental model associated complex proteinopathies.