Table of Contents Author Guidelines Submit a Manuscript
International Journal of Cell Biology
Volume 2010 (2010), Article ID 717520, 10 pages
http://dx.doi.org/10.1155/2010/717520
Research Article

The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration

Department of Biology, Molecular Neurobiology, University of Oldenburg, POB 2503, 26111 Oldenburg, Germany

Received 12 August 2009; Revised 14 October 2009; Accepted 5 November 2009

Academic Editor: Afshin Samali

Copyright © 2010 Lisa Schwarz 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.

Abstract

Filamentous tau-positive protein inclusions in neurons and glia are prominent features of a number of neurodegenerative disorders termed tauopathies. These inclusions are further characterized by the presence of heat shock proteins (HSPs). The group of small HSPs, namely, HSP27 and B-crystallin, interact with the cytoskeleton, bind to nonnative proteins, and prevent their aggregation after stress. To further investigate their contribution to neurodegenerative diseases, we have analyzed the association of HSP27 with pathological lesions of tauopathies. Microarray and immunoblot analysis revealed that HSP27 is enhanced at the mRNA and protein levels in affected brains, and that it is associated with astrocytic pathology. The upregulation of HSP27 in tauopathies with gial pathology implies distinct mechanisms for glial and neuronal cells. This was sustained by cell culture studies, demonstrating that the small HSPs are specifically and prominently expressed in unstressed astrocytes and not in neurons and in neurons remained at a rather low level even after stress situations.