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Heat shock proteins: therapeutic drug targets for chronic neurodegeneration?

Heat shock proteins: therapeutic drug targets for chronic neurodegeneration?
Heat shock proteins: therapeutic drug targets for chronic neurodegeneration?
Intra- and extracellular protein misfolding and aggregation is likely to contribute to a number of age-related central nervous system diseases (“proteinopathies”). Therefore, molecular chaperones, such as heat shock proteins (HSPs), that regulate protein folding, misfolding and adaption to cellular stress are emerging as therapeutic targets. Here we review the current knowledge of HSP-modulating drugs and discuss the opportunities and difficulties of their therapeutic use to treat proteinopathies such as Alzheimer's- and Parkinson's disease, the polyglutamine- and prion disorders and Amyotrophic Lateral Sclerosis.
1389-2010
198-215
Sajjad, M. U.
6541cc5d-69ff-4aaf-925b-905fd05a6431
Samson, B.
4e0d51e6-ec22-46be-91e8-0e5d31918096
Wyttenbach, A.
69846a0f-fb60-4a28-84eb-ed865a5e31fa
Sajjad, M. U.
6541cc5d-69ff-4aaf-925b-905fd05a6431
Samson, B.
4e0d51e6-ec22-46be-91e8-0e5d31918096
Wyttenbach, A.
69846a0f-fb60-4a28-84eb-ed865a5e31fa

Sajjad, M. U., Samson, B. and Wyttenbach, A. (2010) Heat shock proteins: therapeutic drug targets for chronic neurodegeneration? Current Pharmaceutical Biotechnology, 11 (2), 198-215. (doi:10.2174/138920110790909641).

Record type: Article

Abstract

Intra- and extracellular protein misfolding and aggregation is likely to contribute to a number of age-related central nervous system diseases (“proteinopathies”). Therefore, molecular chaperones, such as heat shock proteins (HSPs), that regulate protein folding, misfolding and adaption to cellular stress are emerging as therapeutic targets. Here we review the current knowledge of HSP-modulating drugs and discuss the opportunities and difficulties of their therapeutic use to treat proteinopathies such as Alzheimer's- and Parkinson's disease, the polyglutamine- and prion disorders and Amyotrophic Lateral Sclerosis.

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Published date: February 2010

Identifiers

Local EPrints ID: 145341
URI: http://eprints.soton.ac.uk/id/eprint/145341
ISSN: 1389-2010
PURE UUID: 386353ee-d386-4fe4-86c6-98fed91cce3a

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Date deposited: 19 Apr 2010 08:30
Last modified: 14 Mar 2024 00:50

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Contributors

Author: M. U. Sajjad
Author: B. Samson
Author: A. Wyttenbach

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