Survival of human epidermal keratinocytes after short-duration high temperature: synthesis of HSP70 and IL-8

Bowman, Phillip D.; Schuschereba, Steven T.; Lawlor, David; Gilligan, George R.; Mata, Jennifer R.; DeBaere, D. R.

doi:10.1152/ajpcell.1997.272.6.c1988

Cited by 34 publications

(30 citation statements)

References 14 publications

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“…Bowman and colleagues (25) showed that subjecting normal human epidermal keratinocytes to very brief exposure (1-30 s) at extreme hyperthermia (50-608C) causes marked induction of HSP72 expression and IL-8 release. In another study, Jaspers and coworkers (26) showed that sodium arsenite and vanadyl sulfate each enhanced IL-8 expression in normal human bronchial epithelial cells and increased activity of a 21370/182 nucleotide IL-8 promoter-luciferase reporter construct.…”

Section: Discussionmentioning

confidence: 99%

Heat Shock Co-Activates Interleukin-8 Transcription

Singh

Gupta

Nagarsekar

et al. 2008

Am J Respir Cell Mol Biol

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The heat shock (HS) response is a phylogenetically ancient cellular response to stress, including heat, that shifts gene expression to a set of conserved HS protein (HSP) genes. In our earlier studies, febrilerange hyperthermia (FRH) not only activated HSP gene expression, but also increased expression of CXC chemokines in mice, leading us to hypothesize that the CXC chemokine family of genes might be HSresponsive. To address this hypothesis we analyzed the effect of HS on the expression of IL-8/CXCL-8, a member of the human CXC family of ELR 1 chemokines. HS markedly enhanced TNF-a-induced IL-8 secretion in human A549 respiratory epithelial-like cells and in primary human small airway epithelial cells. IL-8 mRNA was also upregulated by HS, but the stability of IL-8 mRNA was not affected. TNF-a-induced reporter activity of an IL-8 promoter construct IL8 -1471/144 -luc stably transfected in A549 cells was also enhanced by HS. Electrophoretic mobility and chromatin immunoprecipitation assays showed that the stress-activated transcription factor heat shock factor-1 (HSF-1) binds to at least two putative heat shock response elements (HSE) present in the IL-8 promoter. Deletional reporter constructs lacking either one or both of these sites showed reduced HS responsiveness. Furthermore, depletion of HSF-1 using siRNA also reduced the effects HS on TNF-a-induced IL-8 expression, demonstrating that HSF-1 could also act to regulate IL-8 gene transcription. We speculate that during evolution the CXC chemokine genes may have co-opted elements of the HS response to amplify their expression and enhance neutrophil delivery during febrile illnesses.Keywords: neutrophil; hyperthermia; IL-8; chemokine; heat shock factor-1The heat shock (HS) response is a phylogenetically ancient cellular response to exogenous stress, including high temperatures, that shifts gene expression to a set of evolutionarily conserved HS proteins (HSPs) (1). In eukaryotes, HSP genes are regulated by HS-activated transcription factors (HSFs), which bind cis-acting HS response elements (HSEs) comprising inverted dyad nGAAn repeats (2). Of the three mammalian HSFs, HSF-1 is activated by exposure to HS (3) and required for HSinduced HSP72 expression (4). cDNA microarray (5-7) and in situ hybridization (8) studies indicate that HS-induced expression of genes is not limited to only the HSP family of genes.We have previously identified overlaps between the HS response to exogenous thermal stress, and fever, a state of regulated, endogenous hyperthermia (9). We have shown that temperatures within the usual febrile range are sufficient to activate HSF-1 and HSP expression in vitro and in vivo (10-13). We have also shown that whole body febrile range hyperthermia (FRH; core temperature z 39.58C) augments neutrophil recruitment, and accelerates pathogen clearance in diverse animal species (13-16), but also increases collateral tissue injury. In mouse models of pneumonia (13) and pulmonary oxygen toxicity (15), FRH increases neutrophil recruitment to the affected l...

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Section: Discussionmentioning

confidence: 99%

Heat Shock Co-Activates Interleukin-8 Transcription

Singh

Gupta

Nagarsekar

et al. 2008

Am J Respir Cell Mol Biol

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“…In contrast with the coincident exposure of A549 cells to heat shock and proinflammatory stimuli analyzed in the present study, the studies showing an inhibitory effect of heat shock on NF-B activation used a protocol in which the inflammatory stimulus was added after heat shock had been induced. On the other hand, Bowman et al (36) showed that exposing cultured human keratinocytes to 54°C for 4 s activated expression of both HSP72 and IL-8. These studies are limited to showing an association between heat shock activation and expression of ELR ϩ CXC chemokines.…”

Section: Figurementioning

confidence: 99%

Febrile-Range Hyperthermia Augments Neutrophil Accumulation and Enhances Lung Injury in Experimental Gram-Negative Bacterial Pneumonia

Rice

Martin

et al. 2005

The Journal of Immunology

101

109

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We previously demonstrated that exposure to febrile-range hyperthermia (FRH) accelerates pathogen clearance and increases survival in murine experimental Klebsiella pneumoniae peritonitis. However, FRH accelerates lethal lung injury in a mouse model of pulmonary oxygen toxicity, suggesting that the lung may be particularly susceptible to injurious effects of FRH. In the present study, we tested the hypothesis that, in contrast with the salutary effect of FRH in Gram-negative peritonitis, FRH would be detrimental in multilobar Gram-negative pneumonia. Using a conscious, temperature-clamped mouse model and intratracheal inoculation with K. pneumoniae Caroli strain, we showed that FRH tended to reduce survival despite reducing the 3 day-postinoculation pulmonary pathogen burden by 400-fold. We showed that antibiotic treatment rescued the euthermic mice, but did not reduce lethality in the FRH mice. Using an intratracheal bacterial endotoxin LPS challenge model, we found that the reduced survival in FRH-treated mice was accompanied by increased pulmonary vascular endothelial injury, enhanced pulmonary accumulation of neutrophils, increased levels of IL-1β, MIP-2/CXCL213, GM-CSF, and KC/CXCL1 in the bronchoalveolar lavage fluid, and bronchiolar epithelial necrosis. These results suggest that FRH enhances innate host defense against infection, in part, by augmenting polymorphonuclear cell delivery to the site of infection. The ultimate effect of FRH is determined by the balance between accelerated pathogen clearance and collateral tissue injury, which is determined, in part, by the site of infection.

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“…We previously showed that cultured human epidermal keratinocytes could not survive a 1-second exposure above 58°C, but responded by synthesizing heat shock protein 70 (hsp70) and the chemokine interleukin-8. 8 The purpose of the present study was to determine whether burn injury simulated by short pulses of high temperature causes cell death by apoptosis or by accidental cell death (ACD).…”

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confidence: 99%