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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 798052, 8 pages
Research Article

Influence of Hsp90 and HDAC Inhibition and Tubulin Acetylation on Perinuclear Protein Aggregation in Human Retinal Pigment Epithelial Cells

1Department of Ophthalmology, University of Eastern Finland, 70211 Kuopio, Finland
2Department of Ophthalmology, University of Tampere, 33014 Tampere, Finland
3Department of Neuroscience and Neurology, University of Eastern Finland, 70211 Kuopio, Finland
4Department of Neurology, Kuopio University Hospital, 70211 Kuopio, Finland
5Department of Ophthalmology, Kuopio University Hospital, 70211 Kuopio, Finland

Received 16 June 2010; Accepted 23 September 2010

Academic Editor: Patrick Matthias

Copyright © 2011 Tuomas Ryhänen 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.


Retinal pigment epithelial (RPE) cells are continually exposed to oxidative stress that contributes to protein misfolding, aggregation and functional abnormalities during aging. The protein aggregates formed at the cell periphery are delivered along the microtubulus network by dynein-dependent retrograde trafficking to a juxtanuclear location. We demonstrate that Hsp90 inhibition by geldanamycin can effectively suppress proteasome inhibitor, MG-132-induced protein aggregation in a way that is independent of HDAC inhibition or the tubulin acetylation levels in ARPE-19 cells. However, the tubulin acetylation and polymerization state affects the localization of the proteasome-inhibitor-induced aggregation. These findings open new perspectives for understanding the pathogenesis of protein aggregation in retinal cells and can be useful for the development of therapeutic treatments to prevent retinal cell deterioration.