Heat shock protein 90 in neurodegenerative diseases Journal Article
| Authors: | Luo, W.; Sun, W.; Taldone, T.; Rodina, A.; Chiosis, G. |
| Article Title: | Heat shock protein 90 in neurodegenerative diseases |
| Abstract: | Hsp90 is a molecular chaperone with important roles in regulating pathogenic transformation. In addition to its well-characterized functions in malignancy, recent evidence from several laboratories suggests a role for Hsp90 in maintaining the functional stability of neuronal proteins of aberrant capacity, whether mutated or over-activated, allowing and sustaining the accumulation of toxic aggregates. In addition, Hsp90 regulates the activity of the transcription factor heat shock factor-1 (HSF-1), the master regulator of the heat shock response, mechanism that cells use for protection when exposed to conditions of stress. These biological functions therefore propose Hsp90 inhibition as a dual therapeutic modality in neurodegenerative diseases. First, by suppressing aberrant neuronal activity, Hsp90 inhibitors may ameliorate protein aggregation and its associated toxicity. Second, by activation of HSF-1 and the subsequent induction of heat shock proteins, such as Hsp70, Hsp90 inhibitors may redirect neuronal aggregate formation, and protect against protein toxicity. This mini-review will summarize our current knowledge on Hsp90 in neurodegeneration and will focus on the potential beneficial application of Hsp90 inhibitors in neurodegenerative diseases. © 2010 Luo et al; licensee BioMed Central Ltd. |
| Keywords: | protein expression; review; nonhuman; protein function; heat shock protein 90; heat shock protein 70; heat shock response; protein structure; nerve cell; degenerative disease; heat shock transcription factor 1; protein aggregation |
| Journal Title: | Molecular Neurodegeneration |
| Volume: | 5 |
| ISSN: | 1750-1326 |
| Publisher: | Biomed Central Ltd |
| Date Published: | 2010-06-03 |
| Start Page: | 24 |
| End Page: | 24 |
| Language: | English |
| DOI: | 10.1186/1750-1326-5-24 |
| PROVIDER: | scopus |
| PMCID: | PMC2896944 |
| PUBMED: | 20525284 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 1" - "Export Date: 20 April 2011" - "Art. No.: 24" - "Source: Scopus" |
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