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PubMed1993

[Experimental studies on the effect of heating on blood flow in the tongue of golden hamsters].

The effect of hyperthermia on the tongue of hamsters was evaluated histologically and by measuring blood flow. The dorsal tongue surface of the male mature golden hamster was heated at 41 degrees C-45 degrees C (surface temperature) by 2450 MHz microwave for 60 min, and the regional blood flow was measured using the hydrogen clearance method at 6, 24, 42, and 60 min during heating. When heated at 41 degrees C (9 animals), 42 degrees C (11 animals), 43 degrees C (8 animals), 44 degrees C (8 animals), or 45 degrees C (8 animals), the temperature of the measurement at 0.5 mm deep from the tongue surface was 38.4 +/- 1.0 degrees C, 39.3 +/- 0.6 degrees C, 40.2 +/- 0.6 degrees C, 40.8 +/- 0.5 degrees C, or 43.5 +/- 1.0 degrees C (Mean +/- S.D.), respectively. In the groups heated at 41 degrees C, 42 degrees C, 43 degrees C, 44 degrees C, the blood flow was significantly increased at the first measurement (6 min) and remained elevated during heating. The blood flow was further increased during the second heating which took place after a 2 hour interval. The group heated at 45 degrees C showed a gradual decrease in the blood flow after the initial increase. The second heating induced a slight increase to a lower blood flow than the control. Histologically, dilation and congestion of venules, hemorrhage, interstitial edema in the musculature, and swelling of muscle fibers were found. Dilation, congestion, and rapture of capillaries beneath the mucosal epithelial layer were found also. These damages were more severe with an increase in heating temperature and duration. Additionally, thromboses were found in the group heated at 45 degrees C which was examined 2 hours after heating. The heated part was necrosed in every case heated at 45 degrees C. These results suggest that the critical surface temperature at which the tongue of hamsters receive irreversible damage lies between 44 degrees C and 45 degrees C.

Animals↗
PubMed2005

Possible role of calcineurin in heating-related increase of rat muscle mass.

The purpose of this study was to investigate the contribution of calcineurin-related intracellular signal for heat-stress-associated muscle hypertrophy. Wistar strain male rats (7-week-old) were randomly divided into four groups: (1) control (CC, n=15), (2) control with the injection of cyclosporine A (CsA) (CA, n=15), (3) heat-stressed (HC, n=15), and (4) heat-stressed with the injection of CsA (HA, n=15). The heat-stress groups (HC and HA) were exposed to heat (41 degrees C for 60 min) in a controlled heat chamber without anesthesia. Soleus and extensor digitorum longus (EDL) muscles were dissected and weighed 1, 7, and 14 days after the exposure. Wet and dry weights of soleus were increased 7 days following heat exposure. The expressions of heat shock protein 72 (HSP72) and calcineurin in both muscles were also increased within 1 and 7 days following heat-stress, respectively. Administration of CsA, a specific inhibitor for calcineurin, depressed heat-stress-associated increase of muscle weight and calcineurin expression, especially in soleus. These observations suggest that a calcineurin-dependent signaling pathway may play an important role in the heat-stress-related skeletal muscular hypertrophy. Application of heat-stress to skeletal muscles may be a useful tool to gain muscular mass and force generation not only in athletes, but also in patients during rehabilitation.

Animals↗
PubMed2002

Heat shock and ceramide have different apoptotic pathways in radiation induced fibrosarcoma (RIF) cells.

Heat shock induces various cellular responses including inhibition of protein synthesis, production of heat shock proteins (HSPs) and induction of thermotolerance. The molecular mechanisms of the processes have not been well understood. It has been proposed that ceramide formation during heat shock mediates heat shock induced apoptosis. We examined whether C2-ceramide mimicked the cellular response to heat shock in RIF-1 cells and their thermotolerant derivative TR-RIF-1 cells. Discernible effects between heat shock and C2-ceramide treatments were observed in cellular changes such as total protein synthesis, HSP synthesis, stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) activity and PARP cleavage. Heat shock immediately inhibited cellular protein synthesis, which was recovered by synthesizing HSPs first and then whole proteins later. Heat shock also activated SAPK/JNK and increased PARP cleavage in dose-dependent manner. Thermotolerant TR-RIF-1 cells responded to heat shock more insensitively than RIF-1 cells. On the other hand, C2-ceramide treatment did not accompany any changes induced by heat shock. No discernible differences between RIF-1 and TR-RIF-1 cells were observed by C2-ceramide treatment. We tried to figure out how C2-ceramide interacts with cellular membrane and found that exogenous C2-ceramide was incorporated into the outer monolayer and flipped into the inner monolayer of human erythrocytes in ATP-dependent manner. However, the rate of C2-ceramide incorporation was similar in control and thermotolerant cells. In summary, thermotolerant cells are resistant to heat shock induced apoptotic signaling but not resistant, rather sensitive to membrane disturbing C2-ceramide mediated apoptosis. These results suggest that heat shock and ceramide have different signal transduction pathways.

Apoptosis↗
PubMed1998

The role of an inverted CCAAT element in transcriptional activation of the human DNA topoisomerase IIalpha gene by heat shock.

Expression of the DNA topoisomerase IIalpha (topoIIalpha) gene is highly sensitive to various environmental stimuli including heat shock. The amount of topoIIalpha mRNA was increased 1.5-3-fold 6-24 h after exposure of T24 human urinary bladder cancer cells to heat shock stress at 43 degreesC for 1 h. The effect of heat shock on the transcriptional activity of the human topoIIalpha gene promoter was investigated by transient transfection of T24 cells with luciferase reporter plasmids containing various lengths of the promoter sequence. The transcriptional activity of the full-length promoter (nucleotides (nt) -295 to +85) and of three deletion constructs (nt -197 to +85, -154 to +85, and -74 to +85) was increased approximately 3-fold 24 h after heat shock stress. In contrast, the transcriptional activity of the minimal promoter (nt -20 to +85), which lacks the first inverted CCAAT element (ICE1), the GC box, and the heat shock element located between nt -74 and -21, was not increased by heat shock. Furthermore, the transcriptional activity of promoter constructs containing mutations in the GC box or heat shock element, but not that of a construct containing mutations in ICE1, was significantly increased by heat shock. Electrophoretic mobility shift assays revealed reduced binding of a nuclear factor to an oligonucleotide containing ICE1 when nuclear extracts were derived from cells cultured for 3-24 h after heat shock. No such change in factor binding was apparent with an oligonucleotide containing the heat shock element of the topoIIalpha gene promoter. Finally, in vivo footprint analysis of the topoIIalpha gene promoter revealed that two G residues of ICE1 that were protected in control cells became sensitive to dimethyl sulfate modification after heat shock. These results suggest that transcriptional activation of the topoIIalpha gene by heat shock requires the release of a negative regulatory factor from ICE1.

Antigens, Neoplasm↗
PubMed1996

Mechanism of heat shock protein 72 induction in primary cultured astrocytes after oxygen-glucose deprivation.

Induction of stress proteins is thought to be important in the protection of cells from a variety of environmental insults including heat, hypoxia and ischemia. The aim of this study was to compare the mechanism of induction of heat shock protein 72 (HSP72) in primary cultures of murine cortical astrocytes by heat and combined oxygen-glucose deprivation (OGD), a model of in vitro ischemia. 35S-methionine labeling and immunoblotting showed increased HSP72 synthesis and accumulation lasting for up to 24 h following heat or OGD. Heat induced a markedly greater amount of HSP72 mRNA and protein than did OGD. We then sought evidence of heat shock transcription factor-1 (HSF-1) activation. An increase in apparent molecular weight of nuclear HSF-1 after heat or OGD was observed, consistent with increased phosphorylation. To seek an explanation of the difference between heat and OGD as inducers of HSP72 we examined the binding activity of HSP72 + 73 to other proteins. More cellular protein was found to co-immunoprecipitate with HSP72 + 73, and more HSP72 + 73 was found in the pellet fraction after heat shock compared to OGD. These results suggest that HSP72 induction is regulated in astrocytes at least in part at the level of HSF activation, by both heat and OGD. Reduced availability of free HSP72 + 73 in heated cells could be responsible for the greater magnitude of HSP72 induction after heat compared to OGD.

Animals↗
PubMed1998

Transcriptional and translational regulation of major heat shock proteins and patterns of trehalose mobilization during hyperthermic recovery in repressed and derepressed Saccharomyces cerevisiae.

Patterns of heat shock gene transcription and translation, as well as trehalose content, were investigated in both glucose (repressed) and acetate (derepressed) grown cells of Saccharomyces cerevisiae during heat shock and subsequent return of cells to 25 degrees C. Heat-shocked cells (37 degrees C for 30 min), grown in either glucose- or acetate-supplemented media, initially acquired high thermotolerance to a 50 degrees C heat stress, which was progressively lost when cultures were allowed to recover at 25 degrees C and subsequently exposed to a second heat stress. In all cases, with the notable exception of repressed cells of a relatively thermosensitive strain, inhibition of protein synthesis and coincident decrease in trehalose accumulation during the heat shock had little effect on the kinetics of loss of thermotolerance. Heat shock at 37 degrees C elicited a marked increase in transcription and translation of genes encoding major heat shock proteins (hsps). During recovery at 25 degrees C, both metabolic activities were suppressed followed by a gradual increase in hsp mRNA transcription to levels observed prior to heat shock. De novo translation of hsp mRNAs, however, was no longer observed during the recovery phase, although immunodetection analyses demonstrated persistence of high levels of hsps 104, 90, 70, and 60 in cells throughout the 240-min recovery period. In addition, while heat shock induced trehalose was rapidly degraded during recovery in repressed cells, levels remained high in derepressed cells. Results therefore indicated that the progressive loss of induced thermotolerance exhibited by glucose- and acetate-grown cells was not closely correlated with levels of hsp or trehalose. It was concluded that both constitutive and de novo synthesized hsps require heat shock associated activation to confer thermotolerance and this modification is progressively reversed upon release from the heat-shocked state.

Acetates↗
PubMed2001

Heat-activated transgene expression from adenovirus vectors infected into human prostate cancer cells.

Replication-deficient adenovirus expression vectors were used to introduce a recombinant DNA construct containing enhanced green fluorescent protein (EGFP) under control of a truncated, human heat shock promoter into human prostate cancer cells growing either exponentially or in plateau phase. This was done to measure controlled, heat shock-induced EGFP expression under conditions relevant to treating human cancers with heat-activated gene therapy. Both the temporal duration and magnitude of EGFP expression increased proportionately with stronger heat shocks (time at temperature) up to maximum values that were induced by 4 h at 41.0 degrees C or 2 h at 42.0 degrees C. Longer heat shocks at either temperature yielded no additional EGFP expression and ultimately reduced it. Maximal EGFP expression was induced in exponential cultures by heat shocks delivered 12-24 h after virus infection. Induction at progressively later postinfection times induced increasingly lower, peak EGFP expression. Maximal EGFP expression could not be induced until 48 h after infection of plateau phase cultures but could still be induced 180 h after virus infection. However, peak EGFP levels in plateau cultures were approximately 25-50% of those observed in identically induced exponential cultures. Ostensibly, the differences in expression from the heat shock promoter observed in exponential and plateau cultures were attributable to cell division diluting the vector within exponential cultures and the lower metabolic activity in serum-starved plateau cultures. For all experimental conditions, EGFP expression induced from the heat shock promoter was comparable with or higher than that from the constitutively active cytomegalovirus promoter over any 24-h period. The experimental results demonstrated that EGFP expression from the heat shock promoter was controllable in both exponential and plateau phase cultures and support the plausibility of using controlled heat shock activation of this promoter as a means of regulating both the spatial and temporal expression of therapeutic DNA constructs within human tissues. The ability to localize and regulate expression from the heat shock promoter may prove particularly advantageous for many cancer applications, especially if the therapeutic products are highly toxic, e.g., proteotoxins or cytokines. However, the results of this study suggest that differential growth conditions within tumors could markedly affect the expression of recombinant DNA under control of both inducible and constitutive promoters. Consequently, inducing schemes may need to be spatially adjusted to obtain the desired therapeutic results in all tumor domains using heat-activated gene therapy.

Adenoviridae↗
PubMed1998

Potential protective role of the heat shock response in sepsis.

The heat shock response, a primitive and highly conserved cellular defense mechanism, has broad protective effects against sepsis-induced injury. In various models of sepsis, induction of the heat shock response protects against sepsis-induced mortality, organ injury, cardiovascular dysfunction, and apoptosis. The mechanisms by which the heat shock response protects against sepsis-induced injury are currently under investigation. One potential mechanism involves the ability of the heat shock response to inhibit proinflammatory responses. The heat shock response has been demonstrated to inhibit expression of the cytokines tumor necrosis factor (TNF)-alpha and interleukin (IL)-1beta. The heat shock response has also been demonstrated to inhibit cytokine-mediated expression of inducible nitric oxide synthase. Recent studies demonstrated that the heat shock response inhibits nuclear translocation of nuclear factor-kappaB (NF-kappaB), a transcription factor involved in the regulation of many proinflammatory responses. Heat shock response-mediated inhibition of NF-kappaB nuclear translocation involves stabilization of an NF-kappaB inhibitory protein called I-kappaBalpha. The heat shock response also increases expression of I-kappaBalpha, thus providing another potential mechanism by which the heat shock response can modulate proinflammatory responses. Future studies designed to further understand the protective role of the heat shock response against sepsis-induced injury may allow for the development of rational pharmacologic agents or gene therapy methods to safely induce the heat shock response as a strategy to treat patients with sepsis.

Cytokines↗
PubMed1993

Heat shock induces changes in the expression and binding of ubiquitin in senescent Drosophila melanogaster.

We examined the effect of aging on the expression of ubiquitin RNA and the binding of the ubiquitin polypeptide to proteins following heat shock in Drosophila melanogaster. Heat-shocked adult flies transcribe two major RNA species--one of 4.4 kb and one of about 6 kb that hybridize to the polyubiquitin-encoding probe. Several less abundant RNAs were also observed but the 4.4-kb band was present as the major RNA species in both stressed and nonstressed flies of both ages. The 6-kb fragment was more abundant in heat shocked aged flies than in younger flies. The quantitative expression of the polyubiquitin gene increased in proportion to the duration of the heat stress. Moreover, the induction of the polyubiquitin RNA was markedly elevated during aging following heat shock. Hybridization of Northern blots with the monoubiquitin gene probe revealed a band of 0.9 kb that was not significantly affected by heat stress. We also investigated the relationship between the changes in polyubiquitin gene expression and the formation of ubiquitin-protein complexes in aging heat-shocked flies. Heat shock to old flies results in a significant increase in the level of proteins immunoprecipitated by anti-ubiquitin antibodies. In the case of proteins synthesized 2 h before heat shock, most of the ubiquitinated proteins were of high molecular weight. For those proteins synthesized during a 30-min heat shock and the 2 h following heat shock, two major immunoprecipitated bands were observed: an 80-kD and a 70-kD polypeptide. The ubiquitination of a 60 kD protein was also observed in nonstressed flies, but its formation was drastically reduced following heat shock.(ABSTRACT TRUNCATED AT 250 WORDS)

Age Factors↗
PubMed1982

Expression of a Drosophila heat-shock protein in Xenopus oocytes: conserved and divergent regulatory signals.

On injection of cloned Drosophila hsp70 heat-shock genes into Xenopus oocytes, heat-inducible expression is observed: the level of correctly initiated transcripts is increased 20- to 100-fold on heat shock at 34 degrees C. We show that this induction is due to activation of the heat-shock gene promoter, and that the DNA sequences required for induction lie between 10 and 66 bases upstream from the transcription start site. Most heat-induced transcripts have a correct 3' end, and hsp70 mRNA activity is detectable after extraction of the RNA from oocytes and subsequent in vitro translation. Drosophila heat-shock protein (hsp70) is synthesised in the injected oocytes after heat-shock, but only at low temperature. Under heat-shock conditions, Drosophila hsp70 mRNA translation is reduced 10-fold as is translation of the normal (25 degrees C) mRNAs, whereas translation of the endogenous Xenopus hsp70 mRNA is strongly induced. Translation of Drosophila heat-shock mRNAs extracted from flies and injected into the oocytes is also reduced by heat-shock. This suggests that Xenopus oocytes do not recognise the translational regulatory signals of Drosophila heat-shock mRNAs. In contrast, the signals for heat-induced transcription must be strongly conserved between Xenopus and Drosophila.

Animals↗
PubMed1987

Hydrogen peroxide or heat shock induces resistance to hydrogen peroxide in Chinese hamster fibroblasts.

Survival after H2O2 exposure or heat shock of asynchronous Chinese hamster ovary cells (HA-1) was assayed following pretreatment with mildly toxic doses of either H2O2 or hyperthermia. H2O2 cytotoxicity at 37 degrees C, expressed as a function of mM H2O2 was found to be dependent on cell density at the time of treatment. The density dependence reflected the ability of cells to reduce the effectiveness of H2O2 as a cytotoxic agent. When the survival data were plotted as a function of mumoles H2O2/cell at the beginning of the treatment, survival was independent of cell density. Cells pretreated with 0.1 mM (3-5 mumoles/cell X 10(-7)) H2O2 for 1 hr at 37 degrees C (30-50% survival) became resistant to a subsequent H2O2 treatment 16-36 hr after pretreatment [dose modifying factor (DMF) at 1% isosurvival = 4-6]. Their resistance to 43 degrees C heating, however, was only slightly increased over controls 16-36 hr following pretreatment (DMF at 1% isosurvival = 1.2). During this same interval, the synthesis of protein migrating in the 70 kD region of a one-dimensional SDS-polyacrylamide gel was enhanced twofold in the H2O2-pretreated cells. When the cells were heated for 15 min at 45 degrees C (40-60% survival), the survivors became extremely resistant to 43 degrees C heating and somewhat resistant to H2O2 (DMF at 1% isosurvival = 2). The heat-induced resistance to heat developed much more rapidly (reached a maximum between 6 and 13 hr) following pretreatment than the heat-induced resistance to H2O2 (16-36 hr). The enhanced synthesis of 70 kD protein after heat shock was greater in magnitude and occurred more rapidly following preheating than following H2O2 pretreatment. The cells that became resistant to H2O2 by either pretreatment (H2O2 or heat shock) also increased their ability to reduce the H2O2 cytotoxicity from the treatment medium beyond that of the untreated HA-1 cells. This may be one of the mechanisms involved in the increased resistance and a common adaptive mechanism induced by both stresses. These data indicate that mammalian cells develop resistance to H2O2 following mild pretreatment with H2O2 or heat shock. The cross-resistance induced by H2O2 and heat shock reinforce the hypothesis that some overlap in mechanisms exist between the cellular responses to these two stresses. However, the failure of H2O2 pretreatment to induce much resistance to heat indicates that there are also differences in the actions of the two agents.

Animals↗
PubMed1984

Development profile of the heat shock response in early embryos of Drosophila.

Drosophila melanogaster embryos reared at 22 degrees C were subjected to a mild heat shock (40 min at 37 degrees C) at various ages in order to determine whether there are changes in the heat shock response during embryogenesis. The effects of the heat shock were measured by assaying (1), subsequent developmental abnormalities (2), developmental time (3), hatchability, and (4), the ability to synthesize the heat shock proteins as assayed by 35S-methionine pulse labeling followed by protein separations using both one-and two-dimensional polyacrylamide gel electrophoresis. Our data show that, first, proteins with molecular weights similar to those of six of the seven major heat shock proteins are normally found in the embryo at control temperatures (22 degrees C); second, that the pregastrula embryo (stages 2-6) is not capable of displaying any aspect of the heat shock response upon treatment, although it may possess all of the so-called heat shock proteins; third, that the complete heat shock response is acquired very rapidly by early gastrula embryos; and fourth, that the heat shock treatment brings about developmental delays and/or abnormalities, depending on the developmental stage of the embryo at the time of the treatment. These developmental abnormalities appear to stem from the failure of early embryos to completely inhibit their synthesis of non-heat-shock proteins. In the light of these findings, it becomes important not to base conclusions about the putative presence of a heat shock response in a particular tissue or developmental stage solely on the presence or absence of the heat shock proteins.

Animals↗
PubMed1998

Heat-shock-specific phosphorylation and transcriptional activity of RNA polymerase II.

The carboxyl-terminal domain (CTD) of the largest RNA polymerase II (pol II) subunit is a target for extensive phosphorylation in vivo. Using in vitro kinase assays it was found that several different protein kinases can phosphorylate the CTD including the transcription factor IIH-associated CDK-activating CDK7 kinase (R. Roy, J. P. Adamczewski, T. Seroz, W. Vermeulen, J. P. Tassan, L. Schaeffer, E. A. Nigg, J. H. Hoeijmakers, and J. M. Egly, 1994, Cell 79, 1093-1101). Here we report the colocalization of CDK7 and the phosphorylated form of CTD (phosphoCTD) to actively transcribing genes in intact salivary gland cells of Chironomus tentans. Following a heat-shock treatment, both CDK7 and pol II staining disappear from non-heat-shock genes concomitantly with the abolishment of transcriptional activity of these genes. In contrast, the actively transcribing heat-shock genes, manifested as chromosomal puff 5C on chromosome IV (IV-5C), stain intensely for phosphoCTD, but are devoid of CDK7. Furthermore, the staining of puff IV-5C with anti-PCTD antibodies was not detectably influenced by the TFIIH kinase and transcription inhibitor 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). Following heat-shock treatment, the transcription of non-heat-shock genes was completely eliminated, while newly formed heat-shock gene transcripts emerged in a DRB-resistant manner. Thus, heat shock in these cells induces a rapid clearance of CDK7 from the non-heat-shock genes, indicating a lack of involvement of CDK7 in the induction and function of the heat-induced genes. The results taken together suggest the existence of heat-shock-specific CTD phosphorylation in living cells. This phosphorylation is resistant to DRB treatment, suggesting that not only phosphorylation but also transcription of heat-shock genes is DRB resistant and that CDK7 in heat shock cells is not associated with TFIIH.

Animals↗
PubMed1998

Heat shock effects on second messenger systems of Neurospora crassa.

Exposure of growing hyphae of Neurospora crassa to heat shock (44 degrees C) or ethanol (2.6 M) for 1 h induced a significant increase in the cAMP level, which reached a maximum approximately 2 min after the beginning of treatment and then decreased to control values despite continued heat or ethanol exposure. A 10-s heat shock or a 5-s ethanol shock also resulted in a transient cAMP increase 2 min after the pulse. Heat shock or ethanol treatment led to an increase in the amount of catalytic subunits of the cAMP-dependent protein kinase A in the nucleus almost synchronously with the increase of cAMP in the cytoplasm. The concentration of cGMP decreased a few seconds after the beginning of heat shock (44 degrees C) or ethanol treatment (2.6 M) to approximately 50% of the control level. Exposure to heat shock (44 degrees C, 1 h) led to an increase in the amount of inositol phosphates 0.5-2 min after the onset of heat shock. Thereafter, inositol phosphate levels dropped to control values despite continued heat exposure. Incubation of growing hyphae with cAMP or 8-Br-cAMP led to a two- to threefold increase of inositol phosphates 10-300 s after the beginning of incubation. Heat treatment furthermore caused a rapid release of calcium from vacuoles as determined by Fura-2 measurement of the calcium content released from isolated vacuoles. These heat-shock-dependent second messenger changes may play a role in the heat-shock-induced phase shifts of the circadian clock and heat-shock-induced conidiation.

Calcium↗
PubMed1992

The relationship between hsp 70 localization and heat resistance.

Using indirect immunofluorescence we have investigated the kinetics of nuclear accumulation and removal of hsp 70 in HA-1 Chinese hamster fibroblasts exposed to elevated temperatures. The kinetics of accumulation of hsp 70 in the nuclei were found to be time/temperature dependent at all temperatures tested (42-45 degrees C). At a given temperature, the fraction of cells manifesting nuclear localization of hsp 70 increased with exposure time. For a given duration of heating, the fraction of cells manifesting nuclear localization of hsp 70 increased with the temperature. The kinetics of the nuclear accumulation of hsp 70 were similar for normal HA-1 cells, their heat-resistant variants, and transiently thermotolerant cells (triggered by prior exposure to a brief heat shock or to sodium arsenite). Upon return to 37 degrees C after heat shock, the kinetics of removal of the hsp 70 associated with the nucleus was dependent on the severity of the initial heat challenge. However, for a given heat dose, the decay of nuclear localization of hsp 70 was more rapid in thermotolerant and heat-resistant cells than in their normal counterparts. These results suggest that the increased levels of hsp 70 associated with the transient or permanently heat-resistant state may play a direct role in restoring and/or repairing heat-induced nuclear and nucleolar alterations associated with heat-induced cell killing. Furthermore, they also suggest that the heat-resistant state may involve ameliorated repair of heat-induced cellular alterations.

Animals↗
PubMed1999

Vaginal heat shock protein expression in symptom-free women with a history of recurrent vulvovaginitis.

OBJECTIVES: The cause of recurrent vulvovaginitis remains unexplained in most cases. Heat shock protein synthesis is induced under conditions of stress; its presence in vaginal samples from women who were between episodes of recurrent vulvovaginitis thus might reflect a persistent perturbation in the local milieu. STUDY DESIGN: We undertook an evaluation by means of enzyme-linked immunosorbent assay of 60-kd heat shock protein and inducible 70-kd heat shock protein expressions in vaginal wash samples from 24 symptom-free women with a history of recurrent vulvovaginitis and 19 matched control subjects. The samples were also tested for Candida albicans, Chlamydia trachomatis, Ureaplasma urealyticum, Mycoplasma hominis, and human papillomavirus by polymerase chain reaction; for bacterial vaginosis by clinical and microbiologic evaluation; and for interleukin 10, interleukin 1, interleukin 8, RANTES, and eotaxin by enzyme-linked immunosorbent assay. RESULTS: The presence of 60-kd heat shock protein was detected in 11 women with recurrent vulvovaginitis (45.8%) and 1 control subject (5.3%, P =.005). Similarly, 70-kd heat shock protein was present in 8 patients with recurrent vulvovaginitis (33.3%) and no control subjects (P =.005). The presence of 60-kd heat shock protein and the presence of 70-kd heat shock protein were correlated with each other (P =.02), as were both 60-kd heat shock protein (P =.006) and 70-kd heat shock protein (P =.01) correlated with IL-10. There was no relation between the presence of 60-kd heat shock protein or 70-kd heat shock protein and detection of IL-1, IL-8, or any microorganism. CONCLUSION: The expression of heat shock proteins and IL-10 in the vaginas of women with a history of recurrent vulvovaginitis but not in the vaginas of control subjects suggests the existence of differences in the vaginal milieu between the 2 groups, even when both are without vaginal symptoms.

Adult↗
PubMed1992

Heat shock alters the composition of heteromeric steroid receptor complexes and enhances receptor activity in vivo.

Under normal cellular conditions, human progesterone receptors (PR), immune-isolated from cytosols of T47D breast cancer cells, associate with two heat shock proteins (hsps), hsp 90 and hsp 70. Receptors activated by hormone binding in vivo and extracted from nuclei with 0.5 M NaCl no longer associate with hsp 90 but retain association with hsp 70. We have examined the effect of heat shock treatment of cells on hsp-receptor interactions and on receptor function. Heat shock resulted in a partial reduction in cellular levels of PR, but receptors that remained were functional for both steroid and DNA binding activities. By steady-state [35S]methionine labeling prior to heat shock treatment, it was determined that heat shock did not affect the composition or maintenance of preexisting cytosolic PR.hsp 90.hsp 70 complexes. By contrast, immune isolation of PR complexes from cells pulse-labeled with [35S]methionine showed that heat shock altered the composition of newly synthesized hsps associated with PR. After heat shock, both the highly inducible form of hsp 70 (72K hsp) and a 100K hsp were bound to cytosol PR, and inducible 72K hsp remained bound with the nuclear-activated PR. Neither of these hsps were associated in detectable amounts with PR under normal cellular conditions. With respect to receptor function, heat shock treatment substantially enhanced the activity of PR in vivo as determined by measuring hormone-dependent PR-mediated transcription of a target reporter gene (MMTV-CAT) that was stably transfected into T47D cells. Heat shock treatment alone, in the absence of hormone, did not stimulate MMTV-CAT expression nor did it affect transcription from a control reporter gene, pSV2-CAT, suggesting that enhanced receptor activity was due to an effect on PR-mediated processes and not to a general effect on transcription. Induction of the heat shock response by a related chemical stress (sodium arsenite) also enhanced PR activity in vivo. Interestingly, sodium arsenite produced both a greater induction of hsp 90 and hsp 70 synthesis and a greater fold enhancement of PR-mediated gene transcription than did heat shock. This suggests that enhancement of PR activity is related not only to induction of hsp synthesis but also to the severity of the stress response. The present results provide an indication that in certain cells there may exist an interrelationship between the activation pathways by which cells respond to stress and to steroid hormones. Possible mechanisms responsible for heat shock effects on PR activity are discussed.

Arsenic↗
PubMed2004

Effect of heat stress on milk production, rectal temperature, respiratory rate and blood chemistry in Holstein, Jersey and Australian Milking Zebu cows.

The effect of heat stress on changes in milk production, rectal temperature, respiratory rate and blood chemistry was evaluated in three groups of six mature Holstein, Jersey and Australian Milking Zebu (AMZ) dairy cows. These animals were subjected to a cool environment when the mean temperature-humidity index (THI) was 72+/-1.4 (dry bulb temperature of 22.2-24.4 degrees C and relative humidity of 100-60%) during the month of December. This experiment was repeated during the hotter month of July of the following year, when the mean THI was 93+/-3.1 (dry bulb temperature of 35.6-43.9 degrees C and relative humidity 95-35%). Holstein cows produced more (p <0.01) milk than AMZ and Jersey cows during the cooler months of the year and all the cows were dry during the hotter months from June until September. Heat stress increased (p<0.01) rectal temperature and respiratory rate in all three breeds. Heat stress had no effect on blood pH in Holstein and AMZ cows but lowered (p <0.01) blood pH from 7.42 to 7.34 in Jersey cows. In addition, heat stress lowered (p <0.01) blood pCO2 (kPa), bicarbonate (HCO3, mmol/L), base excess (BE, mmol/L) and plasma chloride (Cl-, mmol/L) in all three breeds. The total haemoglobin (THb, g/dl) was elevated (p <0.01) in all three breeds when they were subjected to heat stress. Heat stress increased (p<0.01) oxygen saturation (O2SAT, %) in Jersey and AMZ cows but lowered it (p <0.01) in Holstein cows. On the other hand, heat stress increased (p <0.01)pO2 (kPa) in Holstein and Jersey cows but lowered it (p <0.01) in AMZ cows. Heat stress increased (p <0.01) plasma potassium (K, mmol/L) and calcium (Ca, mmol/L) only in Holstein and Jersey cows but lowered them (p<0.01) in AMZ cows. The plasma glucose (GLU, mmol/L) increased (p<0.01) with heat stress in Holstein and AMZ cows but decreased (p <0.01) in Jersey cows. Heat stress increased (p<0.01) plasma creatinine (CR, (mol/L) but lowered (p<0.01) plasma creatinine phosphokinase (CPK, IU/L), aspartate aminotransferase (AST, IU/L) and blood urea nitrogen (BUN, mmol/L) in all three breeds. These results indicate that heat-stressed Holstein and AMZ cows were able to maintain their acid-base balance with a marginal change in their pH of 0.02 when their rectal temperatures increased by 0.47 and 0.38 degrees C, respectively. When heat stress increased the rectal temperature in Jersey cows by 0.70 degrees C, the pH decreased (p<0.01) from 7.42 to 7.34. However, even with this decrease 0.08 the pH is still within the lower physiological limit of 7.31.

Acid-Base Equilibrium↗