title: Heat shock proteins: therapeutic drug targets for chronic neurodegeneration?
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.
authors.affiliation: Southampton Neuroscience Group, School of Biological Sciences, University of Southampton, Boldrewood Campus, Basset Crescent East, Southampton SO16 7PX, UK.
authors.forename: M U
authors.initials: MU
authors.lastname: Sajjad
authors.forename: B
authors.initials: B
authors.lastname: Samson
authors.forename: A
authors.initials: A
authors.lastname: Wyttenbach
mesh_terms: D000818:Animals; D001921:Brain / Q000187:drug effects / Q000378:metabolism; D002908:Chronic Disease; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D006801:Humans; D015394:Molecular Structure; D019636:Neurodegenerative Diseases / Q000188:drug therapy* / Q000235:genetics / Q000378:metabolism; D018696:Neuroprotective Agents / Q000009:adverse effects / Q000737:chemistry / Q000494:pharmacology* / Q000627:therapeutic use; D011328:Prions / Q000378:metabolism; D017510:Protein Folding
chemical_list: D006360:Heat-Shock Proteins; D018696:Neuroprotective Agents; D011328:Prions