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

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Hargitai J, Lewis H, Boros I, Racz T, Fiser A, Kurucz I, Benjamin I, Vigh L, Penzes Z, Csermely P, Latchman DS

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.

PubMed ID

12893279 [ View in PubMed

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Abstract

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.

DrugBank Data that Cites this Article

Drugs

Bimoclomol

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Bimoclomol	Heat shock factor protein 1	Protein	Humans	Unknown	Not Available	Details