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- W1982487616 abstract "There is a growing interest in the potential roles of misfolded protein interactions in neurodegeneration. To investigate this issue, we inoculated 3 prion strains intracerebrally into transgenic (TgM83) mice that overexpress human A53T α-synuclein. In comparison to nontransgenic controls, there was a striking decrease in the incubation periods of scrapie, classic and H-type bovine spongiform encephalopathies(C-BSE and H-BSE), with conservation of the histopathologic and biochemical features characterizing these 3 prion strains. TgM83 mice died of scrapie or C-BSE prion diseases before accumulating the insoluble and phosphorylated forms of α-synuclein specific to late stages of synucleinopathy. In contrast, the median incubation time for TgM83 mice inoculated with H-BSE was comparable to that observed when these mice were uninfected, thereby allowing the development of molecular alterations of α-synuclein. The last 4 mice of this cohort exhibited early accumulations of H-BSE prion protein along with α-synuclein pathology. The results indicate that a prion disease was triggered concomitantly with an overt synucleinopathy in some transgenic mice overexpressing human A53T α-synuclein after intracerebral inoculation with an H-BSE prion strain." @default.
- W1982487616 created "2016-06-24" @default.
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- W1982487616 date "2011-05-01" @default.
- W1982487616 modified "2023-10-18" @default.
- W1982487616 title "Transmission of Prion Strains in a Transgenic Mouse Model Overexpressing Human A53T Mutated α-Synuclein" @default.
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- W1982487616 doi "https://doi.org/10.1097/nen.0b013e318217d95f" @default.
- W1982487616 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21487306" @default.
- W1982487616 hasPublicationYear "2011" @default.
- W1982487616 type Work @default.