Generic placeholder image

Current Alzheimer Research

Editor-in-Chief

ISSN (Print): 1567-2050
ISSN (Online): 1875-5828

Tau Oligomerization: A Role for Tau Aggregation Intermediates Linked to Neurodegeneration

Author(s): N. Sahara, S. Maeda and A. Takashima

Volume 5, Issue 6, 2008

Page: [591 - 598] Pages: 8

DOI: 10.2174/156720508786898442

Price: $65

Abstract

Intracellular accumulation of filamentous tau proteins is a defining feature of neurodegenerative diseases, including Alzheimers disease, progressive supranuclear palsy, corticobasal degeneration, Picks disease, and frontotemporal dementia with Parkinsonism linked to chromosome 17, all known collectively as tauopathies. Tau protein is a member of microtubule (MT)-associated proteins. Tau is a highly soluble and natively unfolded protein dominated by a random coil structure in solution. It is believed that aberrant modifications of tau, including phosphorylation, truncation, and conformational changes, induce filamentous aggregation. However, the mechanism underlying the conversion of tau protein from a soluble state to one of insoluble aggregates still remains elusive. The importance of tau aggregation intermediates (e.g. tau dimer, tau multimer, and granular tau oligomer) in disease pathogenesis was suggested by recent studies. Here, we review the latest developments in tracking the structural changes of tau protein and discuss the utility improving our understanding of tau aggregation pathway leading to human tauopathies.

Keywords: Tau, aggregation intermediates, granular tau oligomer, tau dimer, tau multimer, atomic force microscopy, Alzheimer's disease, tauopathy


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy