Abstract
BackgroundPhospho-tau deposition has been described in a rare genetic human prion disease, Gerstmann-Sträussler-Scheinker syndrome, but is not common neuropathological picture for other human and animal transmissible spongiform encephalopathies (TSEs). This study investigated the possible changes of tau and phosphorylated tau (p-tau, at Ser396, Ser404, and Ser202/Thr205) in scrapie experimental animals.MethodsThe profiles of tau and p-tau (p-tau, at Ser396, Ser404, and Ser202/Thr205) in the brain tissues of agents 263K- or 139A-infected hamsters were evaluated by Western blots and real-time PCR. Meanwhile, the transcriptional and expressive levels of GSK3β and CDK5 in the brains were tested.ResultsThe contents of total tau and p-tau at Ser202/Thr205 increased, but p-tau at Ser396 and Ser404 decreased at the terminal stages, regardless of scrapie strains. Transcriptional levels of two tau isoforms were also increased. Additionally, it showed higher CDK5, but lower GSK3β transcriptional and expressive levels in the brains of scrapie-infected animals. Analysis of brain samples collected from different times after inoculated with agent 263 K revealed that the changes of tau profiles and phosphate kinases were time-relative events.ConclusionThese data suggest that changes of profiles of p-tau at Ser396, Ser404 and Ser202/Thr205 are illness-correlative phenomena in TSEs, which may arise of the alteration of phosphate kinases. Alteration of tau, p-tau (Ser396, Ser404, and Ser202/Thr205), GSK3β and CDK5 were either intermediate or consequent events in TSE pathogenesis and proposed the potential linkage of these bioactive proteins with the pathogenesis of prion diseases.
Highlights
Phospho-tau deposition has been described in a rare genetic human prion disease, GerstmannSträussler-Scheinker syndrome, but is not common neuropathological picture for other human and animal transmissible spongiform encephalopathies (TSEs)
Regardless of the primary etiology, the central event in the pathogenesis is the conformational conversion from the cellular prion protein (PrPC) into its insoluble and protease-resistant forms that accumulate in central nervous system (CNS) [1]
Increase of total tau in the brain tissues of the scrapieinfected hamsters To address the presences of PrPSc in the brain tissues of scrapie-infected animals, 10% brain homogenates of five strain 263K- and five 139A-infected hamsters were digested by proteinase K (PK) and analyzed with PrP specific Western blots
Summary
Phospho-tau deposition has been described in a rare genetic human prion disease, GerstmannSträussler-Scheinker syndrome, but is not common neuropathological picture for other human and animal transmissible spongiform encephalopathies (TSEs). Known as transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases of animals and humans causing severe spongiform degeneration and neuronal loss in central nervous system (CNS). This relatively diverse group includes bovine spongiform encephalopathy in cattle (BSE), scrapie in sheep and goat, chronic wasting disease (CWD) in deer and elk, and kuru, Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI) and Gerstmann-.
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