Abstract
Pathological tau protein aggregates can be found in brain of patients with some of the neurodegenerative diseases collectively known as tauopathies, which include Alzheimers disease (AD). Since tau post-translational modifications including phosphorylations, glycosylations, truncation and the subsequent aggregation in oligomers, paired helical filaments (PHFs) and neurofibrillary tangles (NFTs), correlate with cognitive impairment and neurodegeneration in AD, a pathogenic role for tau and its modifications has been raised. Here we summarize the current status of knowledge about tau modifications under pathologic conditions and the evidence supporting neurotoxic - or neuroprotective - roles of the diverse forms of modified and aggregated tau. Finally, we analyze the structural and functional tau alterations found in different tauopathies and how these modifications are related to the pathophysiologic mechanisms of neurodegeneration.
Keywords: Tau self-aggregation, tau modifications, tauopathies, Alzheimer's disease, tau toxicity, MAPs, CNS, projection domain, C-terminal region, MBD, KXGS-motifs, heparin, poly-Glu
Current Alzheimer Research
Title: Mechanisms of Tau Self-Aggregation and Neurotoxicity
Volume: 8 Issue: 6
Author(s): G. Farias, A. Cornejo, J. Jimenez, L. Guzman and R. B. Maccioni
Affiliation:
Keywords: Tau self-aggregation, tau modifications, tauopathies, Alzheimer's disease, tau toxicity, MAPs, CNS, projection domain, C-terminal region, MBD, KXGS-motifs, heparin, poly-Glu
Abstract: Pathological tau protein aggregates can be found in brain of patients with some of the neurodegenerative diseases collectively known as tauopathies, which include Alzheimers disease (AD). Since tau post-translational modifications including phosphorylations, glycosylations, truncation and the subsequent aggregation in oligomers, paired helical filaments (PHFs) and neurofibrillary tangles (NFTs), correlate with cognitive impairment and neurodegeneration in AD, a pathogenic role for tau and its modifications has been raised. Here we summarize the current status of knowledge about tau modifications under pathologic conditions and the evidence supporting neurotoxic - or neuroprotective - roles of the diverse forms of modified and aggregated tau. Finally, we analyze the structural and functional tau alterations found in different tauopathies and how these modifications are related to the pathophysiologic mechanisms of neurodegeneration.
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Cite this article as:
Farias G., Cornejo A., Jimenez J., Guzman L. and B. Maccioni R., Mechanisms of Tau Self-Aggregation and Neurotoxicity, Current Alzheimer Research 2011; 8 (6) . https://dx.doi.org/10.2174/156720511796717258
DOI https://dx.doi.org/10.2174/156720511796717258 |
Print ISSN 1567-2050 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5828 |
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