The heat-shock response attenuates lipopolysaccharide-mediated apoptosis in cultured sheep pulmonary artery endothelial cells.

Wong, Hector R.; Mannix, Robert; Rusnak, James M.; Boota, Ahmad; Zar, Harvey; Watkins, Simon C.; Lazo, John S.; Pitt, Bruce R.

doi:10.1165/ajrcmb.15.6.8969269

Cited by 79 publications

(45 citation statements)

References 16 publications

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“…Perhaps more interesting from a clinical standpoint is the phenomenon of cross-tolerance, whereby induction of the stress response confers protection against non-thermal cytotoxic stimuli. For example, in vitro experiments have demonstrated that induction of the stress response protects endothelial cells against endotoxin-mediated apoptosis (8). Other examples include stress response-dependent protection against nitric oxide (9), peroxynitrite (10), and hydrogen peroxide (11).…”

Section: -Hippocratesmentioning

confidence: 99%

“…More importantly, in vitro data, as well as data from various animal models of acute lung injury, demonstrate that stress proteins have an important cytoprotective role during lung inflammation and injury (128). For example, induction of the stress response by either thermal stress or sodium arsenite attenuates LPSmediated apoptosis in cultured sheep pulmonary artery endothelial cells (8), perhaps via an anti-oxidant mechanism, as induction of the stress response was temporally associated with a reduction in LPS-mediated superoxide anion production. Hsp70 appears to be directly involved in this cytoprotective response, as overexpression of Hsp70 via stable transfection inhibited LPS-mediated apoptosis compared to wild-type cells and cells transfected with a control plasmid (8).…”

Section: Hsp70mentioning

confidence: 99%

“…For example, induction of the stress response by either thermal stress or sodium arsenite attenuates LPSmediated apoptosis in cultured sheep pulmonary artery endothelial cells (8), perhaps via an anti-oxidant mechanism, as induction of the stress response was temporally associated with a reduction in LPS-mediated superoxide anion production. Hsp70 appears to be directly involved in this cytoprotective response, as overexpression of Hsp70 via stable transfection inhibited LPS-mediated apoptosis compared to wild-type cells and cells transfected with a control plasmid (8). Similarly, induction of Hsp70 by thermal stress protected cultured murine lung epithelial cells and bovine pulmonary artery endothelial cells from oxidant-mediated injury (11,129).…”

Section: Hsp70mentioning

confidence: 99%

“…Hsp70 is the most highly induced stress protein in cells and tissues undergoing the stress response (3), and is known to be induced in patients with a variety of critical illnesses or injuries (140)(141)(142)(143). Microinjection of anti-Hsp70 antibody into cells impairs their ability to achieve thermotolerance (144), and increased expression of Hsp70 by gene transfer/transfection has been demonstrated to confer protection against in vitro toxicity secondary to lethal hyperthermia (145), endotoxin (8), nitric oxide (9), hyperoxia (130), and in vivo ischemia-reperfusion injury (146)(147)(148). In addition, in vitro delivery of mature Hsp70 into the intracellular compartment has been shown to protect fibroblasts against lethal thermal injury and hyperoxia (133), and neuronal cells against nitrosative stress and excitotoxicity (149).…”

Section: Stress Proteins and Cytoprotectionmentioning

confidence: 99%

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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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Section: -Hippocratesmentioning

confidence: 99%

Section: Hsp70mentioning

confidence: 99%

Section: Hsp70mentioning

confidence: 99%

Section: Stress Proteins and Cytoprotectionmentioning

confidence: 99%

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Heat shock response and acute lung injury☆

Wheeler

Wong

2007

Free Radical Biology and Medicine

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“…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). However, the mechanisms by which the HSPs exert a cytoprotective effect are not well understood.…”

mentioning

confidence: 99%

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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