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

Judit Hargitai, Hannah Lewis, Imre Boros, Tímea Rácz, András Fiser, István Kurucz, Ivor Benjamin, László Vígh, Zoltán Pénzes, Péter Csermely, David S. Latchman

Research output: Contribution to journalArticlepeer-review

118 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)689-695
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Aug 1 2003
Externally publishedYes


  • Bimoclomol
  • Chaperones
  • HSF-1
  • Hsp47
  • Hsp70
  • Hsp90

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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