Induction of heat-shock gene expression in postischemic pig liver depends on superoxide generation

Schoeniger, Luke O.; Andreoni, Kenneth A.; Ott, Gregory R.; Risby, Terence H.; Bulkley, Gregory B.; Udelsman, Robert; Burdick, James F.; Buchman, Timothy G.

doi:10.1016/s0016-5085(94)95209-4

Cited by 72 publications

(43 citation statements)

References 13 publications

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“…The origin of the ROS, however, remains to be determined. Noteworthy, ROS are also known to induce HSPs that are critical for cellular thermoresistance and the development of thermotolerance (2,17,18). Thus, heat-induced oxidative stress seems to play a pivotal role, i.e.…”

Section: Hyperthermia (Ht)mentioning

confidence: 99%

Pivotal Role of Reactive Oxygen Species as Intracellular Mediators of Hyperthermia-induced Apoptosis

Katschinski¹,

Boos²,

Schindler³

et al. 2000

Journal of Biological Chemistry

106

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The effects of cellular antioxidant capacity on hyperthermia (HT)-induced apoptosis and production of antiapoptotic heat shock proteins (HSPs) were investigated in HL-60 cells and in HL-60AR cells that are characterized by an elevated endogenous catalase activity. Exposure of both cell lines to 43°C for 1 h initiated apoptosis. Apoptosis peaked at 3-6 h after heat exposure in the HL-60 cells. Whereas HL-60AR cells were partially protected against HT-induced apoptosis at these early time points, maximal levels of apoptosis were detected later, i.e. 12-18 h after heat exposure. This differential induction of apoptosis was directly correlated to the induction of the antiapoptotic HSP27 and HSP70. In particular, in the HL-60 cells HSP27 was significantly induced at 12-18 h after exposure to 43°C when apoptosis dropped. In contrast, coinciding with the late onset of apoptosis in HL-60AR cells at that time HL-60AR cells lacked a similar HSP response. In line with the higher antioxidant capacity HL-60AR cells accumulated reactive oxygen species to a lesser degree than HL-60 cells after heat treatment. Protection from HT-induced apoptosis as well as diminished heat-induced HSP27 expression was also observed after cotreatment of HL-60 cells with 43°C and catalase but not with superoxide dismutase. These data emphasize the pivotal role of reactive oxygen species for HT induced pro-and antiapoptotic pathways.

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Section: Hyperthermia (Ht)mentioning

confidence: 99%

Pivotal Role of Reactive Oxygen Species as Intracellular Mediators of Hyperthermia-induced Apoptosis

Katschinski¹,

Boos²,

Schindler³

et al. 2000

Journal of Biological Chemistry

106

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“…Regulates Hypoxia/Reoxygenation-induced HSF Activation-Past studies have shown that exposure to hypoxia followed by reoxygenation (hypoxia/reoxygenation) results in a robust heat shock response (6,25,26). We examined the role of Rac1 in hypoxia/reoxygenation-induced HSF transcriptional activity.…”

Section: Rac1mentioning

confidence: 99%

“…In unstimulated cells, HSFs exist in the cytoplasm as inactive monomers that oligomerize as homotrimers with high DNA binding affinity after exposure to cellular stresses (3)(4)(5). Previous studies have linked the induction of the heat shock response in vitro and in vivo to redox changes (6,7). In particular, millimolar doses of H 2 O 2 can stimulate binding of HSFs to the heat shock element (HSE) and result in heat shock protein synthesis through a thioredoxin-dependent mechanism (8).…”

mentioning

confidence: 99%

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Ozaki¹,

Deshpande²,

Angkeow³

et al. 2000

Journal of Biological Chemistry

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The signaling pathway by which environmental stresses activate heat shock factors (HSFs) is not completely understood. We show that the small GTPase rac1, and Rac1-regulated reactive oxygen species (ROS) play an important role in stress-stimulated heat shock response. A dominant-negative allele of Rac1 (Rac1N17) inhibits the hypoxia/reoxygenation and sodium arsenite-induced transcriptional activity of HSF-1 and the transcription of heat shock protein 70. Rac1N17 also suppresses the production of intracellular ROS induced by hypoxia/reoxygenation or sodium arsenite. Moreover, direct suppression of intracellular ROS levels by antioxidants decreases stress-stimulated HSF activity. However, expression of a constitutively active mutant of Rac1 (Rac1V12) in the absence of extracellular stresses does not increase intracellular ROS levels or induce the heat shock response. These results show that Rac1 is a necessary but insufficient component of the stress-induced signaling pathway that leads to ROS production, activation of HSFs, and transcription of heat shock proteins.

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“…Recently, it has been demonstrated that the HSP70 family is induced in cultured gastric mucosal cells by heat stress, and this protein has cytoprotective function in vitro. 10,11 Such evidence led us to hypothesize that induction of HSP synthesis may play an essential role of rebamipide in attenuating ROM-mediated gastric mucosal cell cytotoxicity.…”

Section: / 2b25 2377 Mp 712 Tuesday Dec 10 10:22 Am El-frb 2377mentioning

confidence: 99%

Role of Rebamipide on Induction of Heat-Shock Proteins and Protection Against Reactive Oxygen Metabolite-Mediated Cell Damage in Cultured Gastric Mucosal Cells

Hahm

Park

Kim

et al. 1997

Free Radical Biology and Medicine

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Induction of heat-shock gene expression in postischemic pig liver depends on superoxide generation

Cited by 72 publications

References 13 publications

Pivotal Role of Reactive Oxygen Species as Intracellular Mediators of Hyperthermia-induced Apoptosis

Pivotal Role of Reactive Oxygen Species as Intracellular Mediators of Hyperthermia-induced Apoptosis

Rac1 Regulates Stress-induced, Redox-dependent Heat Shock Factor Activation

Role of Rebamipide on Induction of Heat-Shock Proteins and Protection Against Reactive Oxygen Metabolite-Mediated Cell Damage in Cultured Gastric Mucosal Cells

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