HSP70 and HSP90 in neurodegenerative diseases

Neurosci Lett. 2020 Jan 18:716:134678. doi: 10.1016/j.neulet.2019.134678. Epub 2019 Dec 6.

Abstract

Molecular chaperones have a role to stabilize proteins or assist them in reaching their native fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins from cellular stress during the assembly of protein complexes and also prevent the proteins from aggregation and disassembly. The immediate increase of HSPs is crucial for cellular adaptation to environmental changes and protection of other proteins from denaturation, thereby maintaining the cellular homeostasis and increasing the longevity of an organism. HSP70 and HSP90 are the most studied HSPs in this very large HSP family. Notably, HSP90 also stabilizes the disease-related proteins in neurodegenerative disorders. Therefore, small molecules that inhibit the HSP90 but also increase the HSP70 has been tested as potential drugs for neurodegenerative disorders.

Keywords: HSP70; HSP90; Neurodegernative diseases; Protein folding; Stress.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • HSP70 Heat-Shock Proteins / metabolism*
  • HSP90 Heat-Shock Proteins / metabolism*
  • Humans
  • Neurodegenerative Diseases / metabolism*

Substances

  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins