Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection

Nat Biotechnol. 1998 Sep;16(9):833-8. doi: 10.1038/nbt0998-833.

Abstract

Molecular chaperones protect proteins against environmental and physiologic stress and from the deleterious consequences of an imbalance in protein homeostasis. Many of these stresses, if prolonged, result in defective development and pathologies associated with a diverse array of diseases due to tissue injury and repair including stroke, myocardial reperfusion damage, ischemia, cancer, amyloidosis, and other neurodegenerative diseases. We discuss the molecular nature of the stress signals, the mechanisms that underlie activation of the heat shock response, the role of heat shock proteins as cytoprotective molecules, and strategies for pharmacologically active molecules as regulators of the heat shock response.

Publication types

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

MeSH terms

  • Animals
  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology
  • Benzoquinones
  • Cell Survival / drug effects*
  • Drug Design
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / physiology*
  • Heat-Shock Response
  • Humans
  • Hydroxylamine / pharmacology
  • Lactams, Macrocyclic
  • Oxidative Stress / drug effects*
  • Quinones / pharmacology
  • Rifabutin / analogs & derivatives

Substances

  • Anti-Inflammatory Agents, Non-Steroidal
  • Benzoquinones
  • Heat-Shock Proteins
  • Lactams, Macrocyclic
  • Quinones
  • Rifabutin
  • Hydroxylamine
  • herbimycin