Tau phosphorylation and aggregation in Alzheimer's disease pathology
- 3 March 2006
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 580 (12), 2922-2927
- https://doi.org/10.1016/j.febslet.2006.02.067
Abstract
In this article I shall review how tau phosphorylation and aggregation participates in Alzheimer's disease (AD) and other tauopathies. Tau, a microtubule associated protein, is the main component, in phosphorylated form, of the aberrant paired helical filaments found in AD. Tau is present in phosphorylated and aggregated form not only in AD, but in other pathologies (tauopathies). In this review, the phosphorylation of tau, its aggregation, and the possible relation between tau phosphorylation and aggregation is, briefly, described. Also, it is discussed the toxicity of modified tau. In addition, I propose a working model detailing the progression of tau pathologies.Keywords
This publication has 79 references indexed in Scilit:
- Tau gene mutations and their effectsMovement Disorders, 2005
- Tau Suppression in a Neurodegenerative Mouse Model Improves Memory FunctionScience, 2005
- Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal deathNature, 2004
- PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutationsThe EMBO Journal, 2004
- Tau is a candidate gene for chromosome 17 frontotemporal dementiaAnnals of Neurology, 1998
- Neurons, intracellular and extracellular neurofibrillary tangles in subdivisions of the hippocampal cortex in normal ageing and Alzheimer's diseaseNeuroscience Letters, 1995
- Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinaseNeuroscience Letters, 1992
- Neuropathological stageing of Alzheimer-related changesActa Neuropathologica, 1991
- Proteolysis of tau by calpainBiochemical and Biophysical Research Communications, 1989
- Self assembly of microtubule associated protein tau into filaments resembling those found in alzheimer diseaseBiochemical and Biophysical Research Communications, 1986