The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

Pharmacol Ther. 1998 Aug;79(2):129-68. doi: 10.1016/s0163-7258(98)00013-8.


The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major molecular chaperones of the cytosol and of the endoplasmic reticulum, respectively) has become an increasingly active subject of research in the past couple of years. These ubiquitous, well-conserved proteins account for 1-2% of all cellular proteins in most cells. However, their precise function is still far from being elucidated. Their involvement in the aetiology of several autoimmune diseases, in various infections, in recognition of malignant cells, and in antigen-presentation already demonstrates the essential role they likely will play in clinical practice of the next decade. The present review summarizes our current knowledge about the cellular functions, expression, and clinical implications of the 90-kDa molecular chaperone family and some approaches for future research.

Publication types

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

MeSH terms

  • Animals
  • Autoimmune Diseases / physiopathology
  • Cell Nucleus / physiology
  • Cytoskeleton / physiology
  • Cytosol / physiology
  • Diabetes Mellitus / physiopathology
  • Gene Expression Regulation
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / physiology
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / physiology
  • Humans
  • Infections / physiopathology
  • Ischemia / physiopathology
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology
  • Molecular Chaperones / genetics
  • Molecular Chaperones / physiology*
  • Neoplasms / physiopathology


  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • glucose-regulated proteins