Heat shock proteins and cardiovascular pathophysiology

Physiol Rev. 2001 Oct;81(4):1461-97. doi: 10.1152/physrev.2001.81.4.1461.


In the eukaryotic cell an intrinsic mechanism is present providing the ability to defend itself against external stressors from various sources. This defense mechanism probably evolved from the presence of a group of chaperones, playing a crucial role in governing proper protein assembly, folding, and transport. Upregulation of the synthesis of a number of these proteins upon environmental stress establishes a unique defense system to maintain cellular protein homeostasis and to ensure survival of the cell. In the cardiovascular system this enhanced protein synthesis leads to a transient but powerful increase in tolerance to such endangering situations as ischemia, hypoxia, oxidative injury, and endotoxemia. These so-called heat shock proteins interfere with several physiological processes within several cell organelles and, for proper functioning, are translocated to different compartments following stress-induced synthesis. In this review we describe the physiological role of heat shock proteins and discuss their protective potential against various stress agents in the cardiovascular system.

Publication types

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

MeSH terms

  • Animals
  • Cardiovascular Diseases / physiopathology*
  • Cardiovascular Physiological Phenomena*
  • Cardiovascular System / metabolism*
  • Cardiovascular System / physiopathology*
  • DNA-Binding Proteins / metabolism
  • Gene Expression Regulation
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / physiology*
  • Humans
  • Ischemic Preconditioning, Myocardial
  • Signal Transduction / physiology
  • Transcription Factors
  • Transcription, Genetic / physiology


  • DNA-Binding Proteins
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins
  • Transcription Factors