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- W1992251936 abstract "Intraneuronal accumulation of hyperphosphorylated tau (phospho–tau) occurs in several neurodegenerative conditions including Alzheimer disease (AD), corticobasal degeneration, progressive supranuclear palsy, FTDP–17, and may also take place in the aging brain. In prion diseases, phospho–tau deposition has been described in many genetic variants of Gerstmann–Sträussler–Scheinker disease (GSS), whereas is not considered part of the neuropathological picture of Creutzfeldt–Jakob disease (CJD). Aim of this study was to investigate whether phospho–tau–related changes are present in variant CJD (vCJD) that shares with GSS abundant prion protein (PrP) deposition in amyloid form. Immunohistochemistry was carried out on brain sections from five vCJD patients (age at death 26–57 years, disease duration 12–27 months) using antibodies 3F4 and 6H4 to PrP, antibodies AT8 (epitope at residues 199–205), TG3 (epitope at residue 231) and AD2 (epitope at residues 396–404) to phosphorylation–dependent epitopes of tau, and antibodies to Aβ. A large number of phospho–tau immunoreactive round or rod–shaped profiles, often clustered around PrP amyloid deposits, were observed not only in the cerebral cortex, but also in the cerebellum of all vCJD patients, in the absence of Aβ. Furthermore, in two vCJD patients, phospho–tau was detected in some perikaria and dendrites of medium–size and large neurons of the cerebral cortex as well as in Purkinje cells. Since this immunoreactivity did not correspond to argyrophilia, these structures had the characteristics of pre–tangles described in AD and aging. Similar phospho–tau immunoreactive profiles surrounded PrP–amyloid deposits in an experimental mouse model of vCJD. There are several previous reports about Alzheimer–type changes in CJD elderly patients in which intraneuronal build up of phospho–tau is associated with Aβ deposits, likely representing co–occurence of AD or age–related phenomena. Our present finding about tauopathy in vCJD patients has a different significance because the young age and the absence of Aβ rule out the possibility of an incidental finding due to AD or aging. These results support the view that phospho–tau related abnormalities may be the consequence of amyloid deposition in the cortical neuropil regardless of its chemical composition and that PrP and Aβ amyloid share a toxic effect inducing a secondary taoupathy." @default.
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- W1992251936 date "2006-07-01" @default.
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- W1992251936 title "O2-01-08" @default.
- W1992251936 doi "https://doi.org/10.1016/j.jalz.2006.05.109" @default.
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