Heat stress increases survival rates in lipopolysaccharide-stimulated rats

Chu, Eric K.; Ribeiro, Sérgio Pinto; Slutsky, Arthur S.

doi:10.1097/00003246-199710000-00025

Cited by 109 publications

(85 citation statements)

References 35 publications

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“…This inhibitory effect may be related to stabilization of I B␣, possibly through the prevention of IKK activation. Taken together with protective effects of HSP induction in an in vivo animal model of ALI (13,14), the findings presented here suggest that HSP induction may be utilized a novel therapeutic modality in ALI.…”

Section: Discussionsupporting

confidence: 55%

“…Recently, RANTES and inducible NO synthase gene expressions were shown to be inhibited by prior HSP induction in human and murine lung epithelial cells, respectively (22,23). In addition to these in vitro studies, the protective effect of HSP induction was documented to be related to the attenuation of plasma IL-1␤ concentrations in an in vivo model of ALI (14). These findings suggest that one potential mechanism of protection may be the ability of HSPs to inhibit pro-inflammatory responses in lung cells.…”

mentioning

confidence: 99%

“…Lung damage was also attenuated by prior HSP induction in an animal model of sepsis-induced ALI (13). Recently, induction of the HSPs even after endotoxin challenge was demonstrated to be protective (14). Considering the fact that in vitro induction of the heat shock (HS) response protected lung cells against endotoxin and oxidants, the in vivo protective effect may be through protecting lung cells (15,16).…”

mentioning

confidence: 99%

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Anti-Inflammatory Effect of Heat Shock Protein Induction Is Related to Stabilization of IκBα Through Preventing IκB Kinase Activation in Respiratory Epithelial Cells

Yoo

Lee

et al. 2000

The Journal of Immunology

246

171

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Heat shock protein (HSP) induction confers protection against diverse forms of cellular and tissue injury. However, the mechanism by which HSP exerts cytoprotective effects is unclear. Because HSP induction inhibits genetic expression of pro-inflammatory cytokines, the transcription of which is dependent on NF-κB activation, we explored the relationship between the anti-inflammatory effect of HSP induction and the NF-κB/IκBα pathway. Both HS and sodium arsenite treatment increased HSP70 expression time dependently at mRNA and protein levels. Prior induction of HSP suppressed cytokine-induced IL-8 and TNF-α expression at both mRNA and protein levels. Although HSP induction did not affect total cellular expression of NF-κB, TNF-α-induced increase in NF-κB-DNA binding activity and nuclear translocation of the p65 subunit of NF-κB were inhibited by prior HSP induction, suggesting that activation of NF-κB was blocked. Cytokine-induced IκBα phosphorylation and its degradation were blocked in HSP-induced cells. Immune complex kinase assays demonstrated that TNF-α induced increase in IκB kinase activity was suppressed by prior HSP induction. These results suggest that the anti-inflammatory effect of HSP induction in respiratory epithelial cells is related to stabilization of IκBα, possibly through the prevention of IκB kinase activation, which thereby inhibits activation of NF-κB.

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Section: Discussionsupporting

confidence: 55%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Anti-Inflammatory Effect of Heat Shock Protein Induction Is Related to Stabilization of IκBα Through Preventing IκB Kinase Activation in Respiratory Epithelial Cells

Yoo

Lee

et al. 2000

The Journal of Immunology

246

171

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“…In addition, intracellular problems (spontaneous transcriptional and translational errors, sudden increase in protein synthesis or excess of synthesized subunits, incorrect cellular localization, or the damaging effect of highly reactive free radicals) as well as extracellular stressors (high temperature, hypoxia, radiation, toxic chemicals, endotoxins, and osmotic pressure) can alter the folding capacity of a cell leading to translational arrest as well as the accumulation of misfolded or unfolded proteins. [9][10][11][12][13][14] To insure protein homeostasis, cells employ several systems. These include intracellular removal or processing of misfolded proteins, 15 involving cellular chaperones, the ubiquitin-proteasome system, and autophagy.…”

Section: Basic Conceptsmentioning

confidence: 99%

Heat shock response and autophagy—cooperation and control

2015

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Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

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“…For example, heat-accelerated apoptosis could result in proinflammatory removal of apoptotic neutrophils, particularly when these apoptotic cells become opsonized with ANCAs (30)(31)(32). However, other investigators have found that, based on observations in animal and human studies, fever is beneficial in host defense reactions, and also that antipyretic treatment interferes with this effect (19)(20)(21)33).…”

mentioning

confidence: 99%

Febrile temperatures control antineutrophil cytoplasmic autoantibody–induced neutrophil activation via inhibition of phosphatidylinositol 3‐kinase/Akt

Vietinghoff¹,

Choi²,

Rolle³

et al. 2007

Arthritis & Rheumatism

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Objective. Neutrophil activation by antineutrophil cytoplasmic autoantibodies (ANCAs) is central to the pathogenesis of the ANCA-associated vasculitides. Febrile infections occur frequently during these diseases, often in the context of immunosuppressive treatment. Heat exposure may affect the underlying pathophysiologic processes of the vasculitis. In this study we tested the hypothesis that short-term exposure to heat inhibits ANCA-induced neutrophil activation.Methods. After exposure to temperatures from 37°C to 42°C, human neutrophils were primed with either tumor necrosis factor ␣ (TNF␣) or granulocytemacrophage colony-stimulating factor (GM-CSF) and stimulated with monoclonal antibodies to myeloperoxidase or to proteinase 3. Respiratory burst activity was assayed using rhodamine and a nitroblue tetrazolium reduction assay. Specific inhibition experiments against p38 MAPK, ERK, and phosphatidylinositol 3-kinase (PI 3-kinase)/Akt, and Western blotting with phosphospecific antibodies were used to identify key components in the antibody-induced respiratory burst.

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Heat stress increases survival rates in lipopolysaccharide-stimulated rats

Abstract: We conclude that heat stress applied after the initiation of endotoxemia can provide protection against an otherwise lethal stimulus and that the mechanism of protection may be related to the attenuation of plasma IL-1 beta concentrations.

Cited by 109 publications

References 35 publications

Anti-Inflammatory Effect of Heat Shock Protein Induction Is Related to Stabilization of IκBα Through Preventing IκB Kinase Activation in Respiratory Epithelial Cells

Anti-Inflammatory Effect of Heat Shock Protein Induction Is Related to Stabilization of IκBα Through Preventing IκB Kinase Activation in Respiratory Epithelial Cells

Heat shock response and autophagy—cooperation and control

Febrile temperatures control antineutrophil cytoplasmic autoantibody–induced neutrophil activation via inhibition of phosphatidylinositol 3‐kinase/Akt

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