Heat shock proteins; an overview

Curr Pharm Biotechnol. 2010 Feb;11(2):216-22. doi: 10.2174/138920110790909632.

Abstract

Heat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Therefore, misfolded proteins must be properly folded or must be degraded through heat shock protein action. This function protects cells against cytotoxic outcomes. In addition to their cytoprotective roles, Hsps are involved in other functions since Hsps exist in all types of cells and tissues. Therefore, several diseases are associated with alterations of these biochemical functions. This first review of the theme issue will discuss general properties of Hsps concisely along with their potential use in pharmaceutical and biotechnological applications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyloid / metabolism
  • Animals
  • Biotechnology / methods
  • Heat-Shock Proteins / biosynthesis
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / physiology*
  • Humans
  • Inclusion Bodies / metabolism
  • Neurodegenerative Diseases / drug therapy
  • Neurodegenerative Diseases / metabolism
  • Protein Folding
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / pharmacology
  • Recombinant Proteins / therapeutic use
  • Substrate Specificity

Substances

  • Amyloid
  • Heat-Shock Proteins
  • Recombinant Proteins