Literature DB >> 18725048

Heat shock factor 1 inhibits nuclear factor-kappaB nuclear binding activity during endotoxin tolerance and heat shock.

Mingchen Song1, Michael R Pinsky, John A Kellum.   

Abstract

RATIONALE: Sepsis, endotoxin tolerance, and heat shock (HS) all display down-regulation of innate immunity. We hypothesize that HS factor 1 (HSF-1) induces competitive inhibition of nuclear factor-kappaB (NF-kappaB)-induced signal transduction in both endotoxin tolerance and HS.
OBJECTIVES: We compared endotoxin tolerance and HS in RAW 264.7 cells. We transfected cells with an HS protein 70 (HSP70) plasmid to test whether HSP70 is the mediator of HS-induced NF-kappaB inhibition. We studied the effects of endotoxin stimulation and HS, both separately and together, on "wild-type" cells, cells transfected with the HSP70 plasmid, and cells transfected with vehicle.
FINDINGS: Heat shock protein 70 plasmid-transfected cells had increased HSP70 expression and demonstrated decreased nitric oxide (NO) release and inducible NO synthase messenger RNA expression in response to endotoxin compared with wild-type and empty plasmid-transfected cells. Heat shock completely abolished subsequent NO and inducible NO synthase messenger RNA expression in wild-type cells. Heat shock factor 1 reached maximum expression 60 to 90 minutes after HS. Heat shock protein 70-transfected cells still displayed endotoxin-induced NF-kappaB nuclear binding, whereas endotoxin tolerance, HS, and exposure to HSF-1, but not exposure to an unrelated promoter, inhibited NF-kappaB nuclear binding.
CONCLUSIONS: Endotoxin tolerance and HS appear to share a common immune suppressive effect, possibly through HSF-1-mediated competitive inhibition of NF-kappaB nuclear binding.

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Year:  2008        PMID: 18725048     DOI: 10.1016/j.jcrc.2007.09.007

Source DB:  PubMed          Journal:  J Crit Care        ISSN: 0883-9441            Impact factor:   3.425


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