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Future Med Chem. 2009 May;1(2):267-83. doi: 10.4155/fmc.09.17.

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

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1
Department of Medicinal Chemistry, The University of Kansas, 1251 Wescoe Hall Drive, Malott 4070, Lawrence, KA 66045-7563, USA. bblagg@ku.edu

Abstract

BACKGROUND:

The 90-kDa heat-shock proteins (Hsp90) have rapidly evolved into promising therapeutic targets for the treatment of several diseases, including cancer and neurodegenerative diseases. Hsp90 is a molecular chaperone that aids in the conformational maturation of nascent polypeptides, as well as the rematuration of denatured proteins.

DISCUSSION:

Many of the Hsp90-dependent client proteins are associated with cellular growth and survival and, consequently, inhibition of Hsp90 represents a promising approach for the treatment of cancer. Conversely, stimulation of heat-shock protein levels has potential therapeutic applications for the treatment of neurodegenerative diseases that result from misfolded and aggregated proteins.

CONCLUSION:

Hsp90 modulation exhibits the potential to treat unrelated disease states, from cancer to neurodegenerative diseases, and, thus, to fold or not to fold, becomes a question of great value.

PMID:
20161407
PMCID:
PMC2784693
DOI:
10.4155/fmc.09.17
[Indexed for MEDLINE]
Free PMC Article
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