期刊
JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY
卷 -, 期 -, 页码 -出版社
HINDAWI LTD
DOI: 10.1155/2011/798052
关键词
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资金
- Academy of Finland
- Emil Aaltonen Foundation
- Finnish Cultural Foundation
- Finnish Eye Foundation
- Finnish Eye and Tissue Bank Foundation
- Finnish Funding Agency for Technology
- Paivikki and Sakari Sohlberg Foundation
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.
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