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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Animals
-
Brain / drug effects
-
Brain / metabolism
-
Chronic Disease
-
Heat-Shock Proteins / biosynthesis*
-
Heat-Shock Proteins / genetics
-
Heat-Shock Proteins / physiology
-
Humans
-
Molecular Structure
-
Neurodegenerative Diseases / drug therapy*
-
Neurodegenerative Diseases / genetics
-
Neurodegenerative Diseases / metabolism
-
Neuroprotective Agents / adverse effects
-
Neuroprotective Agents / chemistry
-
Neuroprotective Agents / pharmacology*
-
Neuroprotective Agents / therapeutic use
-
Prions / metabolism
-
Protein Folding
Substances
-
Heat-Shock Proteins
-
Neuroprotective Agents
-
Prions