Physiological Functions of Heat Shock Proteins

Curr Protein Pept Sci. 2020;21(8):751-760. doi: 10.2174/1389203720666191111113726.

Abstract

Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease.

Keywords: Heat shock proteins; antioxidation; heat shock factor; immunity; molecular chaperone; tumor.

Publication types

  • Review

MeSH terms

  • Animals
  • Antineoplastic Agents / therapeutic use
  • Apoptosis / genetics
  • Benzoquinones / therapeutic use
  • Gene Expression Regulation*
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / pharmacology
  • Humans
  • Lactams, Macrocyclic / therapeutic use
  • Male
  • Myocardial Reperfusion Injury / genetics*
  • Myocardial Reperfusion Injury / metabolism
  • Myocardial Reperfusion Injury / pathology
  • Myocardial Reperfusion Injury / therapy
  • Oxidative Stress
  • Plants / genetics
  • Plants / metabolism
  • Prostatic Neoplasms / drug therapy
  • Prostatic Neoplasms / genetics*
  • Prostatic Neoplasms / metabolism
  • Prostatic Neoplasms / pathology
  • Protein Refolding
  • Response Elements
  • Signal Transduction
  • Stress, Physiological / genetics

Substances

  • Antineoplastic Agents
  • Benzoquinones
  • Heat-Shock Proteins
  • Lactams, Macrocyclic
  • tanespimycin