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- W2088411252 abstract "The present study was designed to observe the effects of HSF1 and HSP70 on the expression of cytokines and analyze their mechanisms. Inflammatory response was induced by exposure of the mice or RAW 264.7 macrophages to E. coli lipopolysaccharide (LPS). The expression of cytokines was assayed with microarray membranes. The mechanisms by which HSF1 regulates the transcription of cytokines were analyzed by EMSA and reporter genes. The results showed that: 1. HSF1 gene knock out increased the sensitivity of the mice to endotoxemia (15mg/kg, i.p.), with an higher mortality rate in HSF1 −/− mice (65.0 %) than in wild-type mice (36.8 %); 2. fifteen cytokine genes were up-regulated in the lung tissues of HSF1 −/− mice, and of which nine cytokine genes contain heat shock element (HSE) in their promoters; 3. HSF1 overexpression inhibited the expression of proinflammatory cytokine TNF-α, IL- 1, IL-15 and G-CSF but promoted the expression of antiinflammatory cytokine IL-10; 4. HSF1 activated the transcription of IL-10 gene by binding to HSE in the promoter of IL-10 gene, and inhibited the transcription of G-CSF gene by its interaction with NF-IL6; 5. overexpression of HSP70 inhibited the release of late inflammatory mediator high mobility group box 1 protein (HMGB1). 6. HSP70 inhibited the expression of inflammatory cytokines by inhibiting the activation of NF-êB rather than MAPK pathways. It was concluded that HSF1 and HSP70 could inhibit LPS-induced inflammatory response by modulating the expression and release of cytokines." @default.
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- W2088411252 date "2006-06-01" @default.
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- W2088411252 title "GENE EXPRESSION REGULATION OF CYTOKINES BY HEAT SHOCK FACTOR 1 (HSF1) AND HSP70 DURING ENDOTOXEMIA" @default.
- W2088411252 doi "https://doi.org/10.1097/00024382-200606001-00192" @default.
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