Bimoclomol, a heat shock protein co-inducer, acts by the prolonged activation of heat shock factor-1

Biochem Biophys Res Commun. 2003 Aug 1;307(3):689-95. doi: 10.1016/s0006-291x(03)01254-3.


The novel hydroxylamine derivative, bimoclomol, has been shown previously to act as a co-inducer of several heat shock proteins (Hsp-s), enhancing the amount of these proteins produced following a heat shock compared to heat shock alone. Here we show that the co-inducing effect of bimoclomol on Hsp expression is mediated via the prolonged activation of the heat shock transcription factor (HSF-1). Bimoclomol effects are abolished in cells from mice lacking HSF-1. Moreover, bimoclomol binds to HSF-1 and induces a prolonged binding of HSF-1 to the respective DNA elements. Since HSF-1 does not bind to DNA in the absence of stress, the bimoclomol-induced extension of HSF-1/DNA interaction may contribute to the chaperone co-induction of bimoclomol observed previously. These findings indicate that bimoclomol may be of value in targeting HSF-1 so as to induce up-regulation of protective Hsp-s in a non-stressful manner and for therapeutic benefit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Cells, Cultured
  • DNA-Binding Proteins / drug effects*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins / biosynthesis
  • Humans
  • Imides / metabolism
  • Imides / pharmacology*
  • Kinetics
  • Macromolecular Substances
  • Mice
  • Mice, Knockout
  • Phosphorylation
  • Pyridines / metabolism
  • Pyridines / pharmacology*
  • RNA Stability
  • Response Elements
  • Transcription Factors


  • DNA-Binding Proteins
  • HSP70 Heat-Shock Proteins
  • Heat Shock Transcription Factors
  • Heat-Shock Proteins
  • Imides
  • Macromolecular Substances
  • Pyridines
  • Transcription Factors
  • bimoclomol