Heat Shock Proteins, Unfolded Protein Response Chaperones and Alzheimer’s Disease

  • Jordi Magrané
  • Henry W. Querfurth
Part of the Heat Shock Proteins book series (HESP, volume 3)

Abstract

Molecular chaperones interact with cellular proteins to ensure proper folding and transport between or into organelles. They also associate with mature proteins that have unfolded (and become prone to aggregation) because of an environmental insult such as heat shock. There is a large body of evidence that protein quality control mechanisms involving the HSP family of molecular chaperones, as well as proteasomal and lysosomal functions, become impaired with aging and contribute to a variety of neurodegenerative diseases. Promising therapeutic approaches tested in animal models of Parkinson’s and polyglutamine diseases include the up-regulation of molecular chaperones to prevent protein misfolding and aggregation and to facilitate clearance mechanisms. In spite of a slow start, the role of molecular chaperones in Alzheimer’s disease is increasingly being elucidated at the molecular level. This chapter summarizes the nature of the cellular stress response that is induced in Alzheimer’s disease and examines current research related to the function of molecular chaperones in the cellular metabolism of tau and β-amyloid peptide

β-amyloid tau Alzheimer’s disease neurodegeneration heat shock proteins protein misfolding 

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • Jordi Magrané
    • 1
  • Henry W. Querfurth
    • 2
  1. 1.Department of Neurology and NeuroscienceWeill Medical College of Cornell UniversityNew YorkUSA
  2. 2.Department of Neurology, Caritas St Elizabeth’s Medical CenterTufts University School of MedicineBostonUSA

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