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PubMed2006

Increased proteolysis of diphtheria toxin by human monocytes after heat shock: a subsidiary role for heat-shock protein 70 in antigen processing.

The expression of heat-shock proteins (hsp) increases after exposure to various stresses including elevated temperatures, oxidative injury, infection and inflammation. As molecular chaperones, hsp have been shown to participate in antigen processing and presentation, in part through increasing the stability and expression of major histocompatibility complex molecules. Heat shock selectively increases human T-cell responses to processed antigen, but does not affect T-cell proliferation induced by non-processed antigens. Here, we have analysed the mechanisms by which stress such as heat shock, and the ensuing hsp over-expression affect the processing of diphtheria toxin (DT) in peripheral blood monocytes. We found that heat shock increased DT proteolysis in endosomes and lysosomes while the activities of the cathepsins B and D, classically involved in DT proteolysis, were decreased. These effects correlated with the heat-shock-mediated increase in hsp 70 expression observed in endosomes and lysosomes. Actinomycin D or blocking anti-hsp 70 antibodies abolished the heat-shock-mediated increase in DT proteolysis. These data indicate that the increased expression of hsp 70 constitutes a subsidiary mechanism that facilitates antigen proteolysis in stressed cells. Confirming these data, presentation by formaldehyde-fixed cells of DT proteolysates that were obtained with endosomes and lysosomes from heat-shocked peripheral blood monocytes showed higher stimulation of T cells than those generated with endosomes and lysosomes from control peripheral blood monocytes.

Antigen Presentation↗

PubMed2006

The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor.

In Saccharomyces cerevisiae, the intracellular concentration of trehalose increases rapidly in response to many environmental stresses, including heat shock. These high trehalose levels have been correlated with tolerance to adverse conditions and led to the model that trehalose functions as a chemical cochaperone. Here, we show that the transcriptional activity of Hsf1 during the heat shock response depends on trehalose. Strains with low levels of trehalose have a diminished transcriptional response to heat shock, while strains with high levels of trehalose have an enhanced transcriptional response to heat shock. The enhanced transcriptional response does not require the other heat-responsive transcription factors Msn2/4 but is dependent upon heat and Hsf1. In addition, the phosphorylation levels of Hsf1 correlate with both transcriptional activity and the presence of trehalose. These in vivo results support a new role for trehalose, where trehalose directly modifies the dynamic range of Hsf1 activity and therefore influences heat shock protein mRNA levels in response to stress.

DNA-Binding Proteins↗

PubMed1996

The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress.

Heat shock factor (HSF) activates transcription in response to cellular stress. Human HSF1 has a central regulatory domain which can repress the activity of its activation domains at the control temperature and render them heat shock inducible. To determine whether the regulatory domain works in tandem with specific features of the HSF1 transcriptional activation domains, we first used deletion and point mutagenesis to define these activation domains. One of the activation domains can be reduced to just 20 amino acids. A GAL4 fusion protein containing the HSF 1 regulatory domain and this 20-amino-acid activation domain is repressed at the control temperature but potently activates transcription in response to heat shock. No specific amino acids in this activation domain are required for response to the regulatory domain; in particular, none of the potentially phosphorylated serine and threonine residues are required for heat induction, implying that heat-induced phosphorylation of the transcriptional activation domains is not required for induction. The regulatory domain is able to confer heat responsiveness to an otherwise completely heterologous chimeric activator that contains a portion of the VP16 activation domain, suggesting that the regulatory domain can sense heat in the absence of other portions of HSF1.

Amino Acid Sequence↗

PubMedDate not supplied

Endogenous tumour necrosis factor regulates heat-inducible heat shock protein 72 synthesis.

Endogenous tumour necrosis factor (enTNF) acts as a resistant factor against cytotoxicity of heat by induction of manganous superoxide dismutase (MnSOD), thereby scavenging reactive oxygen free radicals. On the other hand, it is also well known that heat shock proteins (HSPs), which are induced by heat-stress, behave as cytoprotecting factor against this stress. However, the relationship of these two resistant factors is not yet elucidated. In the present study we would therefore propose the possibility that enTNF enhances HSP72 expression. Heat-sensitive L-M (mouse tomourigenic fibroblast) cells, which normally do not express enTNF, were transfected with a nonsecretory-type human TNF expression vector to produce enTNF. Stable transfectants showed resistance to heat treatment and an increase of HSP72 expression. Conversely, when HeLa (human uterine cervical cancer) cells, which normally produce an appreciable amount of enTNF, were transfected with an antisense TNF mRNA expression vector to inhibit enTNF synthesis, their heat sensitivity was enhanced and HSP72 expression was reduced by half. In conclusion, these findings indicate that enTNF regulates heat-inducible HSP72 synthesis.

Animals↗

PubMed2000

[A study on relationship between plasma heat stress protein 70 and cytokine in patients with heat apoplexy].

OBJECTIVE: To study the change of levels of plasma heat stress protein 70 (HSP70) and cytokine and their interrelationship in pathogenicity of heat apoplexy. METHODS: Plasma HSP70 was determined with Western blot, and plasma interleukin-2 (IL-2), soluble interleukin-2 receptor (sIL-2R) and interleukin-6 (IL-6) were determined with enzyme-linked immunosorbent assay (ELISA). RESULTS: Plasma level of HSP70 was 4 211.2 +/- 1,286.2 (integral optical density) in average in the patients of heat apoplexy group, 4,137.8 +/- 1, 207.5 in those of severe heat apoplexy group, and 6,043.5 +/- 1,354.8 in control group, with very significant difference (P < 0.01). Plasma IL-2 level was (64.3 +/- 32.3) pg/ml and (200.0 +/- 50.0) pg/ml and sIL-2R (54.9 +/- 33.3) U/ml and (167.5 +/- 89.0) U/ml in the patients with heat apoplexy and in controls, respectively, with very significant difference. But, there was no significant difference in IL-6 between varied groups. CONCLUSIONS: The above-mentioned results suggest that establishment of heat acclimatization correlates to the interaction of network of neuroendocrine-cytokine-HSP, in which decrease in plasma IL-2 was one of the important factors causing reduction of HSP70 expression. Balance of network regulation was broken by pathological factors, finally resulting in heat apoplexy.

Adolescent↗

PubMed2006

Heat-directed suicide gene therapy mediated by heat shock protein promoter for gastric cancer.

The prognosis of patients with metastatic gastric cancer, particularly peritoneal carcinomatosis, remains poor despite intensive interventions. Gene therapy and hyperthermia can be promising strategies for such advanced disease. The study was conducted to explore the possible effective therapeutic approach of suicide gene therapy with herpes simplex virus thymidine kinase (HSV-tk) in combination with hyperthermia for advanced gastric cancer. The heat shock protein (hsp) 70B gene promoter-oriented HSV-tk (HSP-tk)/ganciclovir (GCV) system directed by heat shock was developed. Hsp promoter activity under the control of heating was assessed by dual luciferase assay in gastric cancer cell lines and implanted tumors of nude mice. In vitro cytotoxic assay was performed using the HSP-tk/GCV delivered by the hemagglutinating virus of Japan (HVJ) liposome, with or without heating. Mice with subcutaneously xenografted tumors and peritoneal carcinomatosis were treated with hyperthermia and gene therapy using the HVJ-liposome-carrying HSP-tk. Assessment by luciferase assay demonstrated highly inducible and tumor-specific promoter activity in vitro and in vivo. Cytotoxic assays showed that cells transfected with HSP-tk became more sensitive to GCV with heating. A synergistic effect was also observed when treated with a non-heat-inducible cytomegalovirus (CMV) promoter-mediated HSV-tk/GCV and heating, indicating bystander killing. The HVJ-liposome-carrying HSP-tk/GCV combined with hyperthermia significantly inhibited the growth of subcutaneous tumors and prolonged survival of mice with peritoneal carcinomatosis. We conclude that the combination of suicide gene therapy with hyperthermia can provide a promising treatment modality for advanced gastric cancer.

Animals↗

PubMed2005

Anti-apoptotic effects of L-glutamine-mediated transcriptional modulation of the heat shock protein 72 during heat shock.

BACKGROUND & AIMS: During physiologic stress, L-glutamine becomes conditionally essential. Its deficiency results in altered epithelial barrier competence, bacterial translocation, and decreased survival. L-glutamine may attenuate these effects by modulating heat shock protein expression, a well-described effect in vitro. We sought to characterize L-glutamine-dependent transcriptional regulation in heat-shocked intestinal cells and to determine its physiologic relevance. METHODS: IEC-18 and H4 intestinal cells were used. Heat shock protein 72 (Hsp72) gene expression was determined by Northern blotting and luciferase assays. Heat shock factor-1 (HSF-1) activation was assessed by electromobility shift assay, Western blotting, and HSF-1 minimal promoters. Phosphorylation and trimerization of HSF-1 were determined by immunoprecipitation and native nonreducing gradient polyacrylamide gel electrophoresis (PAGE). Camptothecin-induced apoptosis was monitored using caspase-3 and poly (ADP-ribose) polymerase [PARP]-specific antibodies and DNA Elisa +/- Hsp72 siRNA. RESULTS: L-glutamine specifically augmented Hsp72 transcript abundance and HSF-1 DNA binding during heat shock. No glutamine-dependent differences in HSF-1 phosphorylation, trimerization, nuclear localization during heat shock, or HSF-1 minimal promoter activity were observed. Nevertheless, the presence of L-glutamine was an important determinant of wild-type Hsp72 promoter transcriptional activation. Reduced Hsp72 was associated with increased camptothecin-induced caspase-3 and PARP cleavage in glutamine-deficient cells. siRNA treated cells were less resistant to camptothecin. CONCLUSIONS: Taken together, the data suggest that glutamine does not affect the classical pathway of HSF-1 activation and that glutamine-dependent upstream trans -factor binding elsewhere in the Hsp72 promoter or coactivator recruitment may determine Hsp72 abundance. L-glutamine potentiation of Hsp72 is associated with increased epithelial resistance to apoptotic injury.

Apoptosis↗

PubMed2026

Heat-responsive ONSEN long terminal repeats integrate heat shock factor motifs, DNA methylation and natural sequence variation in Arabidopsis.

ONSEN is a heat-activated Ty1/copia retrotransposon in Arabidopsis thaliana controlled by heat shock factors (HSFs) and epigenetic silencing. Heat shock element (HSE)-like sequences in ONSEN long terminal repeats (LTRs) contribute to heat responsiveness, but relationships among sequence architecture, basal DNA methylation and natural variation remain unclear. We combined transcription-factor motif prediction, transposable-element comparisons, methylome and RNA sequencing (RNA-seq) data, and Arabidopsis genome assemblies. In silico disruption of five HSE cores eliminated HSF-family motif compatibility in the selected design and all 5119 exact-guanine-cytosine (GC) alternatives. Across 16 curated Columbia-0 terminal windows, ONSEN contained 33-49 non-redundant HSF motif-coordinate placements per 800 bp window and was strongly enriched relative to 1930 non-ONSEN transposable elements across score thresholds and continuous metrics. Direct comparison with 779 non-ONSEN LTR retrotransposons showed selectively elevated basal CHH methylation (where H = A, C or T) at ONSEN termini. Genome-wide RNA-seq analysis revealed broad heat-responsive gene and transposable-element changes, including strong ONSEN induction, whereas candidate-window analysis distinguished ONSEN from most HSF-rich non-ONSEN outliers. ONSEN-like variants across eight accessions generally retained HSF-compatible motifs while altering predicted DNA binding with one finger-family motif composition. Together, these findings define ONSEN terminal regions as HSF-rich regulatory sequences that retain heat-responsive potential within a methylated chromatin context and identify candidates for functional analysis.

DNA Methylation↗

PubMed1988

Enhanced constitutive expression of the 27-kDa heat shock proteins in heat-resistant variants from Chinese hamster cells.

Four heat-resistant variants were isolated after treatment of Chinese hamster lung cells with the mutagen ethyl methane sulfonate, followed by a single-step selection procedure consisting in a severe hyperthermic treatment of 4 h at 44 degrees C. The isolated clones had a stable resistant phenotype for at least 150 generations during which they showed a 5,000-fold increased survival to a 4-h treatment at 44 degrees C when compared to wild-type cells. Comparative two-dimensional electrophoretic analyses of proteins revealed that, like induced thermotolerant wild-type cells (i.e., cells induced to a transient physiological state of thermotolerance by a sublethal heat conditioning treatment administered 18 h before), the heat-resistant variants had, at normal temperature, an increased content of a heat-shock protein with Mr of 27,000 (HSP27). In three of the four heat-resistant variants, the increased content of HSP27 was correlated with a two-fold increase in the constitutive level of the mRNA encoding HSP27. Chinese hamster HSP27 is composed of three species that differ in their relative isoelectric point, among which the two most acidic forms are phosphoproteins. In both the heat-resistant variant and wild-type cells, heat shock induces a rapid enhancement of the phosphorylation of HSP27: maximal phosphorylation occurs within 10 min upon changing the incubation temperature from 35 degrees to 44 degrees C. A concomitant shift in silver-staining intensity is rapidly detectable between the three isoforms, which seems to indicate that the two phosphorylated species represent post-translational modifications of the more basic species. It is concluded that most likely the enhanced expression of HSP27 is linked to the resistant phenotype of the variants. The study provides supporting evidence that both the content and phosphorylation status of HSP27 are determining factors in the ability of cells to survive hyperthermic treatments.

Animals↗

PubMed1987

Thermal injury by laser pulses: protection by heat shock despite failure to induce heat-shock response.

Pulsed lasers produce a variety of therapeutically useful effects in tissues by thermal mechanisms. In contrast with conventional hyperthermia, pulsed lasers rapidly induce extremely high temperatures confined to small areas within the tissues. It is not established, however, how cellular damage and repair responses differ between conventional and pulsed laser-induced hyperthermia. We have addressed this question by examining the induction of cellular heat-shock proteins (HSPs) and protection by heat-shock response against pulsed laser vs conventional hyperthermia. Cultured human dermal fibroblasts at confluency were exposed to single microsecond, 10.6-microns-wavelength pulses from a pulsed CO2 laser at radiant exposures between 0 and 1.3 J/cm2. Cell monolayers were directly exposed after removal of overlying medium. Positive control for the ability of the cells to synthesize of HSPs was obtained by heating the cells for 20 min in a water bath at 45 degrees C or 47 degrees C. The cultures were then labeled with L-[35S] methionine (Met), and proteins analyzed by sodium dodecyl sulfate polyacrylamide and two-dimensional gel electrophoresis 2 hr after exposure. The morphological alterations induced by laser or heat were similar under phase contrast microscopy. Conventional heating induced a heat-shock response, with the appearance of HSPs 2 hours after heating. In contrast, synthesis of HSPs could not be detected following laser irradiation, even at exposures decreasing both cell viability and incorporation of [35S] Met into cellular protein. Pre-exposure of cells to temperatures which induced synthesis of HSPs, however, significantly decreased cell death induced by subsequent laser irradiation.(ABSTRACT TRUNCATED AT 250 WORDS)

Cell Line↗

PubMed1991

Response to heat shock of gene 1, a Drosophila melanogaster small heat shock gene, is developmentally regulated.

The expression of gene 1, a member of the small heat shock gene family from the Drosophila melanogaster chromosomal locus 67B was studied. In contrast to the other heat shock genes, the response of gene 1 to stress was modulated during development. In the absence of stress, gene 1 was expressed at the beginning of pupation, and at a very low level in adult males. Expression of gene 1 was substantially increased by heat shock in pupae, but was one to two orders of magnitude lower in adults or in embryos. Under the same conditions, hsp70 or hsp26 were induced to similar levels in all stages. This developmental effect could be mimicked in cultured Drosophila cells: expression of gene 1 was stimulated by heat shock in the presence, but not in the absence, of the moulting hormone ecdysterone, while the level of expression of hsp26 and hsp70 in response to heat shock was independent of the presence of the hormone. Thus, the presence and activity of the heat shock transcription factor are not sufficient for the maximal response of gene 1 to stress. These results suggest that the heat shock activator protein requires additional factors, which are developmentally regulated, to activate transcription of gene 1. Furthermore, S1 nuclease mapping analysis revealed several gene 1 mRNA species, which are generated by the use of alternative polyadenylation sites and by the use of differentially regulated transcriptional initiation sites.

Animals↗

PubMed1987

Isoproterenol sensitivity in heat tolerant and relatively heat intolerant men.

Recent research has demonstrated that pharmacologic blockade of beta-adrenoceptors predisposes to hyperthermia during prolonged exercise. To investigate the hypothesis that beta-adrenoceptor sensitivity to catecholamines may be an important determinant of exertional heat tolerance, we performed a cross-sectional study comparing the heart rate responses to graded doses of isoproterenol in 6 heat tolerant and 6 relatively heat intolerant men. We observed no significant difference (p greater than 0.1) between the heat tolerant (0.9 +/- 0.68 microgram) and heat intolerant (1.19 +/- 0.61 microgram) subjects in the dose of isoproterenol that produced a 25 beat.min-1 increment in heart rate. Although the possibility of a relationship between beta-adrenoceptor sensitivity and the ability to tolerate exercise in heat cannot be entirely excluded on the basis of these data, our study clearly demonstrates the lack of a correlation between cardiac pacemaker sensitivity to isoproterenol and exertional heat tolerance.

Adolescent↗

PubMed2000

Heat defense control in an experimental heat disorder.

Both whole-body heat exposure and intraperitoneal heating (IPH) result in a body temperature (T(b)) fall that occurs once heating is abated ("hyperthermia-induced hypothermia"). This phenomenon involves a decrease in the threshold T(b) (T(b-thresh)) for activation of metabolic heat production (cold defense). Whether the T(b-thresh) for ear skin vasodilation (heat defense) also changes during hyperthermia-induced hypothermia remains unknown. In experiment 1, we applied IPH to guinea pigs by perfusing water through a preimplanted intraperitoneal thermode and delivered the total heat load of either approximately 1.5 kJ ("short" IPH; perfusion duration: 14 min) or approximately 3.0 kJ ("long" IPH; 40 min). Short IPH caused skin vasodilation and a 1.1 degrees C rise in T(b); no hypothermia occurred when IPH ceased. Long IPH caused vasodilation and hyperthermia of a comparable magnitude (1.4 degrees C) that were followed by a T(b) fall to 1.9 degrees C below the preheating value. In experiment 2, the Tb-thresh for skin vasodilation was measured twice: at the beginning of long IPH and at the nadir of the post-IPH hypothermia. The two T(b-thresh) values were 39.0 (SEM 0.1)degrees C and 39.2 (SEM 0.2)degrees C respectively. In the controls, the T(b-thresh) was measured at the beginning and after short IPH; both control values were 39.0 (SEM 0.2)degrees C. We conclude that the hyperthermia-induced hypothermia, although previously shown to be coupled with a decrease in the T(b-thresh) for cold defense, occurs without any substantial change in the T(b-thresh) for heat defense. We speculate that postheating thermoregulatory disorders are associated with threshold dissociation, thus representing the poikilothermic (wide dead-band) type of T(b) control.

Animals↗

PubMed1987

Accumulation of heat shock protein 70 RNA and its relationship to protein synthesis after heat shock in mammalian cells.

Heat stress induces a set of heat shock proteins (hsps) in a wide variety of species. In response to either a mild (5 min X 45 degrees C) or severe (30 min X 45 degrees C) heat shock, the timing of expression of the hsps and the recovery of general protein synthesis in rat embryonic fibroblasts was dependent on the duration of the hyperthermic exposure. Synthesis of mRNA coding for an hsp of Mr approximately equal to 70,000 (hsp 70) followed immediately after the mild heat shock but was delayed after the severe heat shock. Appearance of the hsps paralleled the synthesis and decay of RNA and was indicative that new RNA synthesis was required for hsp 70 expression. Inhibition of protein synthesis by cycloheximide after the mild heat shock increased the maximal accumulation of hsp 70 encoding mRNA but did not prevent the subsequent decrease in this mRNA species. These results suggest that mammalian cells control the expression of hsp 70 primarily at the level of transcription, and that the normal pattern of hsp 70 mRNA turnover after an inducing heat stress is not dependent on new protein synthesis.

Animals↗

PubMed1986

Loss of heat-shock acquisition of thermotolerance in yeast is not correlated with loss of heat-shock proteins.

Yeast cells when subjected to a primary heat shock, defined as a temperature shift from 23 to 37 degrees C for 30 min, acquired tolerance to heat stress (52 degrees C/5 min). Primary heat shocked cells incubated at 23 degrees C for up to 3 h, progressively lost thermotolerance but retained high levels of the major heat-shock proteins as observed on polyacrylamide gels. On the other hand, a temperature shift back up to 37 degrees C for 30 min fully restored thermotolerance. The major high-molecular-mass heat-shock proteins (hsp) identified were of approximate molecular mass 100 kDa (hsp 100), 80 kDa (hsp 80) and 70 kDa (hsp 70). The results indicate that loss of heat-shock acquisition of thermotolerance is not correlated with loss of heat-shock proteins.

Heat-Shock Proteins↗

PubMed1983

Accumulation of a specific subset of D. melanogaster heat shock mRNAs in normal development without heat shock.

During normal development in D. melanogaster, messenger RNAs for three of the seven heat shock proteins (hsp83, hsp28 and hsp26) accumulate in adult ovaries and are abundant in embryos until blastoderm. The three mRNAs appear to originate in nurse cells and subsequently pass, during stages 10-11, into the oocyte. Little if any of the four other heat shock mRNAs is present in unshocked ovaries or embryos at any time examined. Pre-blastoderm embryos fail to accumulate these heat shock mRNAs even if subjected to heat shock. The accumulation in normal oogenesis of mRNAs for only three of the seven heat shock proteins indicates the existence of differential, possibly multiple controls of heat shock gene expression, and suggests that heat shock proteins hsp83, hsp28 and hsp26 function in the oocyte or early embryo.

Animals↗

PubMed1996

Indoor air pollution by different heating systems: coal burning, open fireplace and central heating.

Investigations of indoor air pollution by different heating systems in private homes are described. Sixteen homes, 7 with coal burning, 1 with open fireplace (wood burning) and 8 with central heating have been investigated. We measured the concentrations of carbon monoxide, carbon dioxide and sedimented dust in indoor air, of total suspended particulates, heavy metals and of polycyclic aromatic hydrocarbons in indoor and outdoor air. Measurements were taken during winter (heating period) and during summer (non-heating period). Generally, we found higher indoor air pollution in homes with coal burning and open fireplace than in homes with central heating. Especially, the concentrations of carbon monoxide, sedimented dust and of some heavy metals were higher. In one case, we found also high indoor air pollution in a home with central heating. This apartment is on the ground floor of a block of flats, and the central heating system in the basement showed a malfunctioning of the exhaust system.

Air Pollutants↗

PubMed1989

Response of cultured Müller cells to heat shock--an immunocytochemical study of heat shock and intermediate filament proteins in response to temperature elevation.

Müller cells from adult rabbit retina were cultured at normal (37 degrees C) temperature and under heat shock conditions (42-43 degrees C) for either 1.5 hr or 4 hr. The presence of heat shock proteins of three different molecular weights, and of vimentin, was identified by the use of monoclonal antibodies and of GFAP by a suitable polyclonal antibody coupled in each instance with immunofluorescence microscopy or immuno-electron microscopy. Heat shock conditions resulted in the expression of HSP of molecular weights in the ranges 57-61 kD, 68 kD and 90 kD. The high level of expression of GFAP in unshocked Müller cell cultures (80-90% of cells) was reduced after 1.5 hr of heat shock to 20-30% of cells, and after 4 hr to only 5%. Although the expression of vimentin (90% of untreated cells) was only slightly reduced by heat shock (60-80% of cells) the intracellular staining pattern of vimentin was greatly altered by heat shock. Changes in the expression of HSP, GFAP and vimentin can all be regarded as part of the Müller cell response to heat shock conditions.

Animals↗