Heat shock proteins as potential targets for protective strategies in neurodegeneration

Harm H. Kampinga*, Steven Bergink

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

70 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)748-759
Number of pages12
JournalLancet Neurology
Volume15
Issue number7
DOIs
Publication statusPublished - Jun-2016

Keywords

  • AMYOTROPHIC-LATERAL-SCLEROSIS
  • SPINOCEREBELLAR ATAXIA TYPE-3
  • CHAPERONE-MEDIATED AUTOPHAGY
  • ALPHA-SYNUCLEIN
  • QUALITY-CONTROL
  • MOLECULAR CHAPERONES
  • HUNTINGTONS-DISEASE
  • POLYGLUTAMINE AGGREGATION
  • MISFOLDED PROTEINS
  • CONFORMATIONAL SWITCH

Cite this