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Tauopathy in human and experimental variant Creutzfeldt‐Jakob disease
Author(s) -
Tagliavini Fabrizio,
Mangieri Michela,
Capobianco Raffaella,
Hauw JeanJacques,
Haik Staphane,
Limido Lucia,
Fociani Paolo,
Bugiani Orso,
Giaccone Giorgio
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a29-c
Subject(s) - tauopathy , pathology , neuropil , creutzfeldt jakob syndrome , senile plaques , prion protein , disease , cerebral cortex , amyloid (mycology) , tau protein , cerebellum , alzheimer's disease , neuroscience , cortex (anatomy) , degenerative disease , chemistry , biology , medicine , neurodegeneration , central nervous system
The molecular basis of intraneuronal accumulation of hyperphosphorylated tau (ph‐tau) in neurodegenerative conditions such as Alzheimer disease is unknown. Ph‐tau deposition also occurs in other cerebral amyloidoses, including Gerstmann‐Sträussler‐Scheinker disease (GSS), a rare genetic form of prion disease. Aim of our study was to investigate whether neuronal changes related to ph‐tau accumulation are present in variant Creutzfeldt‐Jakob disease (vCJD), an acquired form of prion disease that shares with GSS abundant prion protein (PrP) deposition in amyloid form. The results were verified in a mouse model of vCJD. Immunohistochemistry showed a large number of ph‐tau immunoreactive round or rod‐shaped neuritic profiles, often clustered around PrP amyloid deposits, in the cerebral cortex and cerebellum of all vCJD patients examined, in the absence of Aβ deposition. Although less consistently, ph‐tau was localized in some perikaria and dendrites of cortical neurons as well as in Purkinje cells. Similar ph‐tau immunoreactive structures were found in association with PrP deposits in the mouse model of vCJD. These results support the view that ph‐tau abnormalities may be the consequence of amyloid deposition in the neuropil regardless of its chemical composition and provide a paradigm for the early stages of tau pathology in cerebral amyloidoses including Alzheimer disease.