Tamoxifen enhances the Hsp90 molecular chaperone ATPase activity

PLoS One. 2010 Apr 1;5(4):e9934. doi: 10.1371/journal.pone.0009934.

Abstract

Background: Hsp90 is an essential molecular chaperone that is also a novel anti-cancer drug target. There is growing interest in developing new drugs that modulate Hsp90 activity.

Methodology/principal findings: Using a virtual screening approach, 4-hydroxytamoxifen, the active metabolite of the anti-estrogen drug tamoxifen, was identified as a putative Hsp90 ligand. Surprisingly, while all drugs targeting Hsp90 inhibit the chaperone ATPase activity, it was found experimentally that 4-hydroxytamoxifen and tamoxifen enhance rather than inhibit Hsp90 ATPase.

Conclusions/significance: Hence, tamoxifen and its metabolite are the first members of a new pharmacological class of Hsp90 activators.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / drug effects*
  • Adenosine Triphosphatases / metabolism
  • Antineoplastic Agents, Hormonal
  • Computer Simulation
  • Drug Evaluation, Preclinical
  • HSP90 Heat-Shock Proteins / agonists*
  • Humans
  • Molecular Chaperones / drug effects
  • Tamoxifen / analogs & derivatives
  • Tamoxifen / pharmacology*

Substances

  • Antineoplastic Agents, Hormonal
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Tamoxifen
  • afimoxifene
  • Adenosine Triphosphatases