Induction of the heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model

Villar, Jesús; Ribeiro, Sérgio Pinto; Mullen, J. B. M.; Kuliszewski, Michael A.; Post, Martin; Slutsky, Arthur S.

doi:10.1097/00003246-199406000-00007

Cited by 305 publications

(158 citation statements)

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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%

“…Villar et al (12) first demonstrated that pretreatment with heat induces the synthesis of the HSPs in the lungs and attenuates lung damage in a rat model of ALI induced by intratracheal instillation of phospholipase A 2 . 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).…”

mentioning

confidence: 95%

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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: 95%

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, whole body hyperthermia increased both Hsp70 mRNA and protein as measured by Northern and Western blot analysis, respectively. These findings were further corroborated by these same investigators in a rat model of acute lung injury induced by cecal ligation and puncture (CLP) (134). Again, induction of Hsp70 mRNA and protein expression in the lung was temporally associated with reduced lung injury and improved survival.…”

Section: Hsp70mentioning

confidence: 53%

Heat shock response and acute lung injury☆

Wheeler

Wong

2007

Free Radical Biology and Medicine

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All cells respond to stress through the activation of primitive, evolutionarily conserved genetic programs that maintain homeostasis and assure cell survival. Stress adaptation, which is known in the literature by a myriad of terms, including tolerance, desensitization, conditioning, and reprogramming, is a common paradigm found throughout nature, in which a primary exposure of a cell or organism to a stressful stimulus (e.g., heat) results in an adaptive response by which a second exposure to the same stimulus produces a minimal response. More interesting is the phenomenon of cross-tolerance, by which a primary exposure to a stressful stimulus results in an adaptive response whereby the cell or organism is resistant to a subsequent stress that is different from the initial stress (i.e. exposure to heat stress leading to resistance to oxidant stress). The heat shock response is one of the more commonly described examples of stress adaptation and is characterized by the rapid expression of a unique group of proteins collectively known as heat shock proteins (also commonly referred to as stress proteins). The expression of heat shock proteins is well described in both whole lungs and in specific lung cells from a variety of species and in response to a variety of stressors. More importantly, in vitro data, as well as data from various animal models of acute lung injury, demonstrate that heat shock proteins, especially Hsp27, Hsp32, Hsp60, and Hsp70 have an important cytoprotective role during lung inflammation and injury.

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“…In Sprague-Dawley rats, HSP70 is maximally induced in each organ at between 18 hours and 24 hours after heat exposure, and consequently in a number of experimental models, hyperthermia-induced protection has been investigated at one time point. 18,28,29 So far, few attempts have been made to examine the time-dependent protective effect of hyperthermic preconditioning. Karmazyn et al 30 studied the time course of HSP70 induction at 0, 24, 48, 96, and 192 hours following whole-body hyperthermia.…”

Section: Resultsmentioning

confidence: 99%

Impact of hyperthermic preconditioning on postischemic hepatic microcirculatory disturbances in an isolated perfusion model of the rat liver

et al. 2000

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Sublethal hyperthermia and the following recovery from this heat exposure, referred to as hyperthermic preconditioning, elicits a transient state of tolerance to oxidative insults through an intracellular protective response: stress response. The impact of hyperthermic preconditioning on hepatic microcirculatory disturbance, which is one of the determinants of ischemia/reperfusion-induced injury of the liver, was investigated by using intravital fluorescence microscopy. Thirty minutes of ischemia and a subsequent 120 minutes of reperfusion was induced in an in situ isolated perfusion model of Sprague-Dawley rats. Heat stress was given by whole-body hyperthermia, and a subsequent recovery was allowed for 18 or 48 hours, respectively. Postischemic decrease in sinusoidal perfusion rate and sinusoidal diameter, leukocyte stagnation in sinusoids, and leukocyte adhesion in postsinusoidal venules were significantly attenuated in both hyperthermia-pretreated groups. A recovery of bile production, a reduction of liver enzyme release, and an attenuation of tissue edema and histological damage were also observed. A marked expression of heat shock protein (HSP) 70 and heme oxygenase (HO-1)/HSP32 was correlatively observed in the liver tissue coincident with the induction of these protective effects. Hyperthermic preconditioning provides a continuous long-term and constant inhibitory effect (up to 48 hours after heat exposure) on postischemic injury of the liver through the attenuation of microcirculatory disturbances. These beneficial effects might be associated with a concomitant increase in HSP70 and HO-1/HSP32 expression. (HEPATOLOGY 2000;31:407-415.)Ischemia/reperfusion-induced injury is one of the major perioperative complications in liver surgery and liver transplantation. The administration of specific protective agents has been attempted to reduce postischemic hepatic injury. [1][2][3] To the contrary, preconditioning therapies based on an endogenous protection response against stressful events, referred to as heat stress response, have been studied as another therapeutic strategy. Hyperthermic preconditioning, the exposure to a transient sublethal hyperthermia, and the following appropriate recovery develops protection not only to subsequent thermal stress, but also to oxidative stress such as ischemia/reperfusion. [4][5][6][7][8] Heat stress response has been reported to be associated with the induction of specific heat shock proteins (HSPs). In particular, HSP70 is generally considered to contribute to the protective mechanism of hyperthermic preconditioning, based on the finding that overexpression of HSP70 in a transgenic mouse increases the resistance of the heart to ischemic injury. 9,10 Heme oxygenase (HO)-1/HSP32 is another HSP playing a role in the modulation of the inflammatory response. HO catabolizes intracellular heme to biliverdin, which is converted to bilirubin by bilirubin reductase. During this degradation process, carbon monoxide (CO) is released. 11 HO consists of HO-1 (inducible isoenzyme) and ...

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Induction of the heat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model

Cited by 305 publications

References 0 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 acute lung injury☆

Impact of hyperthermic preconditioning on postischemic hepatic microcirculatory disturbances in an isolated perfusion model of the rat liver

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