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Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Author(s) -
Andorfer Cathy,
Kress Yvonne,
Espinoza Marisol,
De Silva Rohan,
Tucker Kerry L.,
Barde YvesAlain,
Duff Karen,
Davies Peter
Publication year - 2003
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2003.01879.x
Subject(s) - hyperphosphorylation , tau protein , tau pathology , gene isoform , microtubule , neuroscience , alzheimer's disease , microtubule associated protein , neurofibrillary tangle , mutant , chemistry , senile plaques , microbiology and biotechnology , tauopathy , tangle , amyloid (mycology) , biology , pathology , neurodegeneration , phosphorylation , disease , biochemistry , medicine , gene , mathematics , pure mathematics
Neurofibrillary tangles are composed of insoluble aggregates of the microtubule‐associated protein tau. In Alzheimer's disease the accumulation of neurofibrillary tangles occurs in the absence of tau mutations. Here we present mice that develop pathology from non‐mutant human tau, in the absence of other exogenous factors, including β‐amyloid. The pathology in these mice is Alzheimer‐like, with hyperphosphorylated tau accumulating as aggregated paired helical filaments. This pathologic tau accumulates in the cell bodies and dendrites of neurons in a spatiotemporally relevant distribution.