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International Journal of Alzheimer’s Disease
Volume 2012 (2012), Article ID 731526, 13 pages
Review Article

Structure and Pathology of Tau Protein in Alzheimer Disease

1Laboratory of Biochemistry and Brain Pathophysiology and AD Center, Prague Psychiatric Center, Ústavní 91, 181 03 Prague 8, Czech Republic
2Third Faculty of Medicine, Charles University in Prague, Ruská 87, 100 00 Prague 10, Czech Republic
3Department of Cell Biology, Center of Research and Advanced Studies, National Polytechnic Institute, Avenue Instituto Politecnico Nacional 2508, 07360 Mexico City, DF, Mexico
4Department of Neurology, Third Faculty of Medicine, Faculty Hospital Královské Vinohrady, Charles University in Prague, Šrobárova 50, 100 34 Prague 10, Czech Republic

Received 19 January 2012; Revised 28 March 2012; Accepted 29 March 2012

Academic Editor: David Blum

Copyright © 2012 Michala Kolarova et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Alzheimer's disease (AD) is the most common type of dementia. In connection with the global trend of prolonging human life and the increasing number of elderly in the population, the AD becomes one of the most serious health and socioeconomic problems of the present. Tau protein promotes assembly and stabilizes microtubules, which contributes to the proper function of neuron. Alterations in the amount or the structure of tau protein can affect its role as a stabilizer of microtubules as well as some of the processes in which it is implicated. The molecular mechanisms governing tau aggregation are mainly represented by several posttranslational modifications that alter its structure and conformational state. Hence, abnormal phosphorylation and truncation of tau protein have gained attention as key mechanisms that become tau protein in a pathological entity. Evidences about the clinicopathological significance of phosphorylated and truncated tau have been documented during the progression of AD as well as their capacity to exert cytotoxicity when expressed in cell and animal models. This paper describes the normal structure and function of tau protein and its major alterations during its pathological aggregation in AD.