Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
Article first published online: 27 JUN 2003
Journal of Neurochemistry
Volume 86, Issue 3, pages 582–590, August 2003
How to Cite
Andorfer, C., Kress, Y., Espinoza, M., De Silva, R., Tucker, K. L., Barde, Y.-A., Duff, K. and Davies, P. (2003), Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. Journal of Neurochemistry, 86: 582–590. doi: 10.1046/j.1471-4159.2003.01879.x
- Issue published online: 27 JUN 2003
- Article first published online: 27 JUN 2003
- Received March 20, 2003; revised manuscript received April 16, 2003; accepted April 17, 2003.
- Alzheimer's disease;
- non-mutant tau;
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.