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PubMed1995

Heat shock protein expression in testis and bladder cancer cell lines exhibiting differential sensitivity to heat.

Testis cancer cells are more sensitive than bladder and most other cancer cells to chemotherapeutic drugs both in the clinic and in vitro. In this study we show that they are also more sensitive than bladder cancer cells to heat. Since heat and drug sensitivity may be related to the ability of a cell to mount a stress response, constitutive and induced levels of heat shock proteins (HSPs) in three testis and three bladder human cancer cell lines were measured using Western blotting and scanning densitometry. No correlation between constitutive levels of HSP 90 or HSP 73/72 and cellular heat sensitivity was found. However, HSP 27 levels were much lower in the testis tumour cells, suggesting that low HSP 27 expression might contribute to heat sensitivity. Protein synthesis studies using [35S]methionine indicated that, for the same heat shocks, the kinetics of synthesis and decay of HSP 90 and HSP 73/72 in 833K (the most heat sensitive testis cells) was similar to or greater than that in HT1376 (the most heat-resistant bladder cells). Both 833K and HT1376 developed thermotolerance, and this followed an increase in synthesis of HSPs. These results indicate that, although there are differences in the constitutive levels of HSPs between testis and bladder cancer cells, both cell types are capable of mounting an induced heat shock response and can develop a similar degree of thermotolerance.

Cell Survival↗
PubMed2003

Warming by resistive heating maintains perioperative normothermia as well as forced air heating.

BACKGROUND: Even mild perioperative hypothermia is associated with several severe adverse effects. Resistive heating has possible advantages compared with other active warming systems because it can heat several fields independently. To assess this new warming system, we measured core temperature in patients during surgery who were warmed with circulating water mattresses, forced air covers or resistive heating covers. METHODS: Twenty-four patients undergoing laparoscopic cholecystectomy were randomly assigned to (i) circulating water mattress (38 degrees C), (ii) forced air warming (set to 'medium') or (iii) carbon-fibre resistive warming (38 degrees C). Warming was applied throughout anaesthesia and surgery. The groups were compared using one-way ANOVA and Student-Newman-Keuls tests. RESULTS: Confounding factors were similar among the groups. Core temperatures in each group decreased for 20 min, but subsequently increased in the forced air and resistive heating groups. There was no significant difference between the forced air and resistive heating groups at any time. In contrast, core temperature in the circulating water group continued to decrease. Consequently, core temperature in the circulating water group was significantly lower than in the other groups 30 min after anaesthetic induction and at later times. CONCLUSIONS: Resistive heating maintains core body temperature as well as forced air heating and both are better than circulating water. Resistive heating offers the advantage of adjustable heating pods.

Adult↗
PubMed1986

Induction of B2 RNA polymerase III transcription by heat shock: enrichment for heat shock induced sequences in rodent cells by hybridization subtraction.

When hybridization subtraction was used to enrich for sequences induced by heat shock in Chinese hamster cells, B2 sequences were found to be one of the major sequences enriched. With cloned B2 probes, we found that the level of the short, 0.1 to 0.6 kb, polyadenylated RNA polymerase III transcripts of this repetitive genetic element increased approximately 10 to 20 fold after heat shock. Transcription of B2 RNA by RNA polymerase III was rapidly induced after heat shock based on time course studies and nuclear runoff experiments. The induction of B2 RNA was not a nonspecific response to lethality or cellular injury because maximum B2 RNA induction was observed with even nontoxic heating while no induction occurred with other agents such as UV or X-radiation. Since B2 RNA increased after heat shock in several different Chinese hamster and mouse cell lines, induction of B2 RNA by heat shock is probably common in rodent cells. B2 RNA may also be the most abundant transcript induced by heat shock because the level of B2 RNA was substantially higher than several other abundant transcripts induced by heat shock including a rodent HSP70. Our finding of the induction of high levels of RNA polymerase III B2 transcripts in different rodent cells raise the possibility of a role in the heat shock response.

Animals↗
PubMed1992

The plasma membrane of yeast acquires a novel heat-shock protein (hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase.

Recent studies have revealed that the action of the proton-translocating ATPase of the plasma membrane of yeast is an important determinant of several stress tolerances and affects the capacity of cells to synthesise heat shock proteins in response to heat shock [Panaretou, B. & Piper, P. W. (1990) J. Gen. Microbiol. 136, 1763-1770; Coote, P. J., Cole, M. B. & Jones, M. V. (1991) J. Gen. Microbiol. 137, 1701-1708]. This study investigated the changes to the protein composition of the Saccharomyces cerevisiae plasma membrane that result from a heat shock to dividing cultures and the entry to stationary growth caused by carbon source limitation. Plasma membranes were prepared from exponential, heat-shocked and stationary yeast cultures. The proteins of these membrane preparations were then analysed by polyacrylamide gel electrophoresis and immunoblot measurement of ATPase levels. The protein composition of plasma membranes displayed two prominent changes in response to both heat shock and the entry to stationary phase: (a) a reduction in the level of the plasma membrane ATPase; and (b) the acquisition of a previously uncharacterised 30 kDa heat-shock protein (hsp30). The ATPase decline with heat shock probably exerts an important influence over the ability of the cell to maintain ATPase activity, and therefore intracellular pH, during extended periods of stress. Through in vivo pulse-labelling of plasma membrane proteins synthesised before and during heat shock, followed by subcellular fractionation, it was shown that hsp30 is the only protein induced by the yeast heat-shock response that substantially copurifies with plasma membranes. It might therefore exert a stress-protective function specifically at this membrane.

Cell Membrane↗
PubMed2004

A study of subcooled pool boiling of water: contact area of boiling bubbles with a heating surface during a heating process.

The contact area of bubbles with a transparent heating surface was optically measured during subcooled pool boiling of water on the ground. In the experiments, boiling bubbles were attached to the heating surface with a bubble holder and nearly reproduced the bubble behavior observed in low gravity. DC power was applied to the ITO heater and increased until the heater surface burned out. In quick heating, that is about 20 second until burnout and equal to the heating time during the low gravity period, the contact area was smaller than that for long time heating at the same heat flux. The experimental results suggest the reason why the critical heat flux in pool boiling is higher than the widely accepted predictions in microgravity. In a drop shaft experiment with constant heating, the contact area increased dramatically at the start of microgravity and became constant. Boiling bubbles coalesced and remained just over the heating surface.

Earth, Planet↗
PubMed2004

Assessment of heat tolerance for post exertional heat stroke individuals.

BACKGROUND: The aim of this study was to evaluate the heat tolerance test, which was performed by individuals with high risk for heat injuries, for exposure duration and climatic conditions. MATERIAL/METHODS: Nineteen young (19+/-1 yr) post heat stroke males performed 2 separate tolerance tests consisting of identical treadmill walking (5km.h-1, 2% grade) for 120 min during hot (40 degrees C, 40%RH) and comfort (20 degrees C, 50%RH) climate conditions. Physiological monitoring included rectal temperature (Tre), heart rate (HR), skin temperature and sweat rate (msw). Concomitantly, strain evaluation was assessed by the physiological strain index (PSI) and the cumulative heat strain index (CHSI). RESULTS: 14 subjects were categorized as heat tolerant (HT) and 5 subjects as heat intolerant (HI). The comfort tolerance test was found as irrelevant for heat intolerance assessment. PSI after 60 min (PSI60) was unable to predict PSI after 120 min (PSI120) whereas there was not a high enough correlation between CHSI60 and CHSI120. CONCLUSIONS: It was concluded that tolerance to heat must be tested during heat stress and the test duration cannot be shorter than 120 min.

Adult↗
PubMed1989

Heat stroke and related heat stress disorders.

Medical disorders related to environmental heat exposure are exceptionally common in persons who perform hard work in hot climates. They are also common in competitive athletes as well as in persons who participate in casual exercise to maintain health. The important issue of salt and water disturbances consequent to heavy sweating in hot climates is discussed in detail as are mechanisms of potassium deficiency and its implications. The major forms of environmental heat illness including heat syncope, heat cramp, heat exhaustion, and heat stroke are presented in detail with relevant clinical examples. A discussion of the differential diagnosis of hyperthermia and rhabdomyolysis follows. Because of the difference in treatment and complications, heat stroke is subdivided into the classic variety that affects the elderly and very young and that form that follows heavy physical work and is always associated with rhabdomyolysis. Because severe heat exhaustion and heat stroke are life-threatening disorders, the chapter includes a detailed discussion of complications and plans for treatment.

Animals↗
PubMed1986

Induction of heat shock gene expression without heat shock by hepatocarcinogens and during hepatic regeneration in rat liver.

We investigated the expression of the rat hepatic heat-shock protein (hsp) genes under the influence of hepatocarcinogens and during hepatic regeneration. This was undertaken because of the inducibility of the heat-shock response in rat liver and because heat-shock genes can be expressed with or without heat shock in various cell states in a developmentally regulated manner. We found that acute administration of hepatocarcinogens to rats induced an increased hsp gene transcription in a time- and dose-dependent manner. Chronic exposure of rats to complete hepatocarcinogens induced increased levels of mainly Mr 83,000 heat-shock protein gene transcription and, to a lesser extent, Mr 70,000 heat-shock protein. However, the tumor promoter phenobarbital did not induce increased hsp gene expression. Increased levels of both Mr 83,000 heat-shock protein and Mr 70,000 heat-shock protein gene transcription were found during hepatic regeneration. Thus, increased hsp gene transcription, which correlated with increased heat-shock protein synthesis, was observed under the acute and chronic influence of hepatocarcinogens and during normal hepatic proliferation. These results are similar to those observed for c-H-ras and c-myc expression in rat liver, and they suggest that a coordinate expression of these three genes may occur in hepatic regeneration and in the early stages of experimental chemical hepatocarcinogenesis.

2-Acetylaminofluorene↗
PubMed1996

Induction of autologous tumor killing by heat treatment of fresh human tumor cells: involvement of gamma delta T cells and heat shock protein 70.

Autologous tumor killing (ATK) has been implicated as an important prognostic factor in cancer patients since the ability of blood lymphocytes to kill freshly isolated autologous tumor cells was strongly associated with good prognosis of the patients. The present study was designed to induce or enhance ATK sensitivity of fresh human tumor cells by heat stress. Brief exposure of fresh human tumor cells to elevated temperature increased their susceptibility to lysis by autologous blood lymphocytes in a short-term (51)Cr release assay. In addition, the heat-elevated ATK sensitivity was confirmed by clonogenic assays. An increase in ATK was observed with unstimulated lymphocytes in 42% of the cases and OK432 (streptococcal preparation)-activated lymphocytes in 80% of the cases. Stimulation of blood lymphocytes with autologous, heat-stressed tumor cells and OK432 resulted in an increase in number of gamma delta T cells, which was associated with elevated ATK activity against the stressed tumor cells. At the clonal level, three gamma delta T-cell clones (V gamma 9/V delta 2+) proliferated in response to autologous, heat stressed tumor cells and/or OK432 and exhibited elevated cytotoxicity against the tumor cells. Western blot analysis revealed an increased expression of heat shock protein (HSP) 70 in heat- treated tumor cells. Some of them expressed HSP70 on their surfaces. The elevated cytoxicity against heat-stressed tumor cells was inhibited by treatment of targets with anti-HSP70 monoclonal antibody (mAb) or of effector cells with anti-V delta2 mAb. Reactivity of gamma delta T cells to autologous, heat- stressed tumor cells was also inhibited by anti-HSP70 mAb. These results indicate that exposure to heat of tumor cells induces ATK susceptibility, especially to OK432-activated effector cells, and suggest that gamma delta T cells may be involved in ATK against stressed tumor cells through recognition of HSP70 on the target cells.

Adult↗
PubMed1997

Heat shock protein 27 stimulates recovery of RNA and protein synthesis following a heat shock.

Constitutive expression of human hsp27 resulted in a 100-fold increase in survival to a single lethal heat shock in CHO cells without effecting the development of thermotolerance. A possible mechanism for the thermoprotective function of hsp27 may be increased recovery of protein synthesis and RNA synthesis following a heat shock. A lethal heat shock (44 degrees C, 30 min) results in a 90% reduction in the rate of protein synthesis in non-tolerant cells. Control transfected cells recovered protein synthesis to a pre-heat shock rate 10 h after the heat shock; while cell lines that constitutively express human hsp27 recovered 6 h after the heat shock. Thermotolerant cells had a 50% reduction in protein synthesis, which recovered within 7 h following the heat shock. The same lethal heat shock (44 degrees C, 30 min) reduced RNA synthesis by 60% in the transfected cell lines, with the controls recovering in 7 h; while the hsp27 expressing cell lines recovered within 5 h. Thermotolerant cells had a 40% reduction in RNA synthesis and were able to recover within 4 h. The enhanced ability of hsp27 to facilitate recovery of protein synthesis and RNA synthesis following a heat shock may provide the cell with a survival advantage.

Animals↗
PubMed2002

Heat shock inhibits activation of NF-kappaB in the absence of heat shock factor-1.

The heat shock response is known to inhibit NF-kappaB activation and NF-kappaB-dependent gene expression. Herein we determined if cells lacking heat shock factor-1 (HSF-1), the major transcription factor regulating heat shock protein gene expression, have an altered ability to modulate NF-kappaB activation. Embryonic fibroblasts from HSF-1-null mutant mice (HSF-1-/- cells) had a drastically reduced ability to express heat shock protein-70 in response to heat shock, compared to embryonic fibroblasts from wild-type mice (HSF+/+ cells). There was no difference, however, in the ability of heat shock to inhibit TNFalpha-mediated NF-kappaB activation, IkappaBalpha degradation, IkappaB kinase activation, and macrophage chemotactic protein-1 expression in the HSF-1-/- cells compared to the HSF-1+/+ cells. These data demonstrate that heat shock inhibits activation of the NF-kappaB/IkappaBalpha pathway and NF-kappaB-dependent gene expression in the absence of an intact heat shock response.

Animals↗
PubMed1998

Heat conditioning induces heat shock proteins in broiler chickens and turkey poults.

Peripheral leukocyte heat shock proteins (HSP: HSP90, HSP70, and HSP23) from broiler chickens and turkey poults were induced by in vitro and in vivo high temperature exposure. Heat conditioning, via a daily 1 h exposure to 41 C, enhanced in vitro HSP expression in leukocytes from chickens heat-conditioned for 1 to 2 wk, and a similar response was found in turkey poults with 3 wk of heat conditioning causing the greatest HSP expression. In vivo heat exposure trials caused maximization of HSP expression after 1 wk of daily heat conditioning exposures in broilers, but no additional enhancement was seen in chickens heat conditioned for 2 wk. Enhancement in HSP expression was evident for periods up to 4 wk after termination of the daily heat conditioning episodes.

Acclimatization↗
PubMed2006

Heat induction of heat shock protein 25 requires cellular glutamine in intestinal epithelial cells.

Glutamine is considered a nonessential amino acid; however, it becomes conditionally essential during critical illness when consumption exceeds production. Glutamine may modulate the heat shock/stress response, an important adaptive cellular response for survival. Glutamine increases heat induction of heat shock protein (Hsp) 25 in both intestinal epithelial cells (IEC-18) and mesenchymal NIH/3T3 cells, an effect that is neither glucose nor serum dependent. Neither arginine, histidine, proline, leucine, asparagine, nor tyrosine acts as physiological substitutes for glutamine for heat induction of Hsp25. The lack of effect of these amino acids was not caused by deficient transport, although some amino acids, including glutamate (a major direct metabolite of glutamine), were transported poorly by IEC-18 cells. Glutamate uptake could be augmented in a concentration- and time-dependent manner by increasing either media concentration and/or duration of exposure. Under these conditions, glutamate promoted heat induction of Hsp25, albeit not as efficiently as glutamine. Further evidence for the role of glutamine conversion to glutamate was obtained with the glutaminase inhibitor 6-diazo-5-oxo-l-norleucine (DON), which inhibited the effect of glutamine on heat-induced Hsp25. DON inhibited phosphate-dependent glutaminase by 75% after 3 h, decreasing cell glutamate. Increased glutamine/glutamate conversion to glutathione was not involved, since the glutathione synthesis inhibitor, buthionine sulfoximine, did not block glutamine's effect on heat induction of Hsp25. A large drop in ATP levels did not appear to account for the diminished Hsp25 induction during glutamine deficiency. In summary, glutamine is an important amino acid, and its requirement for heat-induced Hsp25 supports a role for glutamine supplementation to optimize cellular responses to pathophysiological stress.

Animals↗
PubMed1999

Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress.

The induction of the heat shock genes in eukaryotes by heat and other forms of stress is mediated by a transcription factor known as heat shock factor 1 (HSF1). HSF1 is present in unstressed metazoan cells as a monomer with low affinity for DNA, and upon exposure to stress it is converted to an 'active' homotrimer that binds the promoters of heat shock genes with high affinity and induces their transcription. The conversion of HSF1 to its active form is hypothesized to be a multistep process involving physical changes in the HSF1 molecule and the possible translocation of HSF1 from the cytoplasm to the nucleus. While all studies to date have found active HSF1 to be a nuclear protein, there have been conflicting reports on whether the inactive form of HSF is predominantly a cytoplasmic or nuclear protein. In this study, we have made antibodies against human HSF1 and have reexamined its localization in unstressed and heat-shocked human HeLa and A549 cells, and in green monkey Vero cells. Biochemical fractionation of heat-shocked HeLa cells followed by western blot analysis showed that HSF1 was mostly found in the nuclear fraction. In extracts made from unshocked cells, HSF1 was predominantly found in the cytoplasmic fraction using one fractionation procedure, but was distributed approximately equally between the cytoplasmic and nuclear fractions when a different procedure was used. Immunofluorescence microscopy revealed that HSF1 was predominantly a nuclear protein in both heat shocked and unstressed cells. Quantification of HSF1 staining showed that approximately 80% of HSF1 was present in the nucleus both before and after heat stress. These results suggest that HSF1 is predominantly a nuclear protein prior to being exposed to stress, but has low affinity for the nucleus and is easily extracted using most biochemical fractionation procedures. These results also imply that HSF1 translocation is probably not part of the multistep process in HSF1 activation for many cell types.

Animals↗
PubMed1993

Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins.

When cells are exposed to heat shock, heavy metals, amino acid analogues, and other stresses, the heat shock transcription factor (HSF) is activated. The HSF then binds to the promoter of the heat shock genes, stimulating transcription of the heat shock proteins. Here, we demonstrate that exposure of NIH-3T3 cells to oxidants (H2O2 or menadione) also causes activation of the HSF. This activation is not blocked by inhibitors of protein synthesis (cycloheximide) or by inhibitors of protein kinases (2-aminopurine or genistein). In addition, the oxidant activated HSF is located in the nucleus of the cells. However, oxidant activation of the HSF does not result in the accumulation of hsp70 mRNA or of heat shock proteins. This is in contrast to the accumulation of heat shock proteins seen after heat shock activation of the HSF. This suggests that oxidant induced activation of HSF binding may have a function different from that of heat induced activation of HSF binding.

3T3 Cells↗
PubMed1995

Relationship between the induction of heat shock proteins and the decrease in glucocorticoid receptor during heat shock response in human osteosarcoma cells.

Previously, it has been found that glucocorticoid receptor (GR) binding activity decreased rapidly during heat shock response in HOS-8603, a human osteosarcoma cell line. In this study, The relationship between the induction of heat shock proteins (HSPs) and the decrease in GR was further studied in the same cell line. It was found that even though quercetin could specifically inhibit the expression of hsp90 alpha and hsp70 mRNA, it could not prevent GR from the decrease in response to the heat shock treatment. This represents the first reported evidence that the induction of HSPs and the decrease in GR during heat shock response were 2 independent biological events. The results of the present study further showed that although the heat shock treatment alone had no effects on alkaline phosphatase (AKP) activity, it could completely block the induction of AKP activity in HOS-8603 cells by dexamethasone (Dex), a synthetic glucocorticoid. These results demonstrate that the heat shock-induced alteration in GR was accompanied by a decrease in GR functional activity. Furthermore, when the induction of HSPs was inhibited by the treatment of cells with quercetin, the stimulatory effects of Dex on AKP activity could still be inhibited completely by the heat shock treatment. The results of this part, on the basis of GR functional activity, further demonstrate that quercetin could not inhibit the heat shock-induced decrease in GR even though it could inhibit the induction of HSPs. To clarify further the effects of quercetin alone on GR binding activity in HOS-8603 cells, the regulation of GR by quercetin was also studied. It was found for the first time that quercetin could down-regulate GR in a time-dependent manner significantly, and that the down-regulation of GR by quercetin in HOS-8603 cells paralelled with a decrease in glucocorticoid-mediated functional responses, suggesting that the down-regulation of GR by quercetin is of biological significance.

Alkaline Phosphatase↗