Heat shock proteins as potential targets for protective strategies in neurodegeneration.
Protein aggregates are hallmarks of nearly all age-related neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and several polyglutamine diseases such as Huntington's disease and different forms of spinocerebellar ataxias (SCA; SCA1-3, SCA6, and SCA7). The collapse of cellular protein homoeostasis can be both a cause and a consequence of this protein aggregation. Boosting components of the cellular protein quality control system has been widely investigated as a strategy to counteract protein aggregates or their toxic consequences. Heat shock proteins (HSPs) play a central part in regulating protein quality control and contribute to protein aggregation and disaggregation. Therefore, HSPs are viable targets for the development of drugs aimed at reducing pathogenic protein aggregates that are thought to contribute to the development of so many neurodegenerative disorders.
Department of Cell Biology, University Medical Center Groningen, Rijksuniversiteit Groningen, Groningen, Netherlands. Electronic address: h.h.kampinga@umcg.nl.
Harm H
HH
Kampinga
Department of Cell Biology, University Medical Center Groningen, Rijksuniversiteit Groningen, Groningen, Netherlands.
Steven
S
Bergink
D000818:Animals; D006360:Heat-Shock Proteins / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000378:metabolism*
D006360:Heat-Shock Proteins