Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Heating”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 397 records · Page 22Linked to original sources

Criteria for the diagnosis of heat-related deaths: National Association of Medical Examiners. Position paper. National Association of Medical Examiners Ad Hoc Committee on the Definition of Heat-Related Fatalities.

The National Association of Medical Examiners Ad Hoc Committee on the Definition of Heat-Related Fatalities recommends the following definition of "heat-related death": a death in which exposure to high ambient temperature either caused the death or significantly contributed to it. The committee also recommends that the diagnosis of heat-related death be based on a history of exposure to high ambient temperature and the reasonable exclusion of other causes of hyperthermia. The diagnosis may be established from the circumstances surrounding the death, investigative reports concerning environmental temperature, and/or measured antemortem body temperature at the time of collapse. In cases where the measured antemortem body temperature at the time of collapse was > or = 105 degrees F (> or = 40.6 degrees C), the cause of death should be certified as heat stroke or hyperthermia. Deaths may also be certified as heat stroke or hyperthermia with lower body temperatures when cooling has been attempted prior to arrival at the hospital and/or when there is a clinical history of mental status changes and elevated liver and muscle enzymes. In cases where the antemortem body temperature cannot be established but the environmental temperature at the time of collapse was high, an appropriate heat-related diagnosis should be listed as the cause of death or as a significant contributing condition.

Adult↗

Heat shock proteins, anti-heat shock protein reactivity and allograft rejection.

Heat shock proteins are families of highly conserved immunodominant molecules, reactivity to which has been implicated in the pathogenesis of a number of autoimmune and vascular disease states. However, heat shock proteins are cytoprotective, and in clinical and experimental arthritis, anti-heat shock protein reactivity can down modulate immune responses via a self-Hsp reactive, Th2-type mechanism. Despite a number of studies associating heat shock protein expression and anti-heat shock protein reactivity with allograft rejection, the balance between protective and damaging effects and the precise influence of these responses on graft outcome is unclear. This article reviews current knowledge surrounding heat shock proteins, autoimmunity, and allograft rejection and presents a perspective on the potential influence of these proteins and the stress response on allograft outcome.

Animals↗

Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress.

The yeast high-osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) pathway has been characterized as being activated solely by osmotic stress. In this work, we show that the Hog1 MAPK is also activated by heat stress and that Sho1, previously identified as a membrane-bound osmosensor, is required for heat stress activation of Hog1. The two-component signaling protein, Sln1, the second osmosensor in the HOG pathway, was not involved in heat stress activation of Hog1, suggesting that the Sho1 and Sln1 sensors discriminate between stresses. The possible function of Hog1 activation during heat stress was examined, and it was found that the hog1 delta strain does not recover as rapidly from heat stress as well as the wild type. It was also found that protein tyrosine phosphatases (PTPs) Ptp2 and Ptp3, which inactivate Hog1, have two functions during heat stress. First, they are essential for survival at elevated temperatures, preventing lethality due to Hog1 hyperactivation. Second, they block inappropriate cross talk between the HOG and the cell wall integrity MAPK pathways, suggesting that PTPs are important for maintaining specificity in MAPK signaling pathways.

Heat-Shock Response↗

Expression of 65- and 67-kilodalton heat-regulated proteins and a 70-kilodalton heat shock cognate protein of Leishmania donovani in macrophages.

Heat shock protein (HSP) expression was examined in murine bone marrow-derived macrophages infected with stationary-phase promastigotes of Leishmania donovani. Immunoblotting performed with a rabbit polyclonal antiserum raised against HSP60 from Heliothis virescens (moth) revealed the de novo appearance of 65- and 67-kDa proteins in leishmania-infected macrophages. A third protein of 60 kDa, which represented murine HSP60, was also detected, and its expression did not change in response to infection. In contrast, expression of the novel 65- and 67-kDa proteins in infected cells was coordinately regulated and, at 24 h of infection, reached maximal levels of 52 to 100% increases above initial levels determined at 3 h. Proteins which had identical electrophoretic mobilities and were similarly regulated in response to heat were also detected in promastigotes. The appearance of these proteins in macrophages was specific to leishmania infection in that neither protein was detected in noninfected cells either in the basal state or following several treatments, including (i) infection with Yersinia pseudotuberculosis, (ii) phagocytosis of Staphylococcus aureus, (iii) NaAsO2 treatment, and (iv) heat shock. Expression of the 65- and 67-kDa heat-regulated Leishmania proteins was also observed to be selective, in that as their concentration was increasing, the abundance of the Leishmania surface protease gp63 in infected cells was noted to decrease. Murine HSP60 but not the Leishmania heat-regulated proteins was also recognized by a distinct rabbit antiserum raised against human HSP60, suggesting the presence of specific determinants within these Leishmania proteins. A monoclonal antibody that recognizes both mammalian HSP70 and HSP70 from plasmodia detected single isoforms of both Leishmania and murine HSP70 in infected cells, and the level of neither protein changed during infection. Moreover, although a murine HSP of 73 kDa was induced in response to both heat shock and NaAsO2 treatment, it was not induced to detectable levels by infection. The rapid and relatively high level of expression of inducible HSP60-related proteins of L. donovani and Leishmania HSP70 in infected macrophages suggests that these proteins are involved in pathogenesis and may be important targets of the immune response.

Animals↗

Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting.

Genomic footprinting of the human hsp70 promoter reveals that heat shock induces a rapid binding of a factor, presumably heat shock transcription factor, to a region encompassing five contiguous NGAAN sequences, three perfect and two imperfect matches to the consensus sequence. Arrays of inverted NGAAN sequences have been defined as the heat shock element. No protein is bound to the heat shock element prior to or after recovery from heat shock. Heat shock does not perturb the binding of factors to other regulatory elements in the promoter which contribute to basal expression of the hsp70 gene.

Base Sequence↗

The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells.

A chicken genomic library was screened to obtain genomic clones for ubiquitin genes. Two genes that differ in their genomic location and organization were identified. One gene, designated Ub I, contains four copies of the protein-coding sequence arranged in tandem, while the second gene, Ub II, contains three. The origin of the two major mRNAs that are induced after heat shock in chicken embryo fibroblasts was determined by generating DNA probes from the 5'-and 3'-noncoding regions of the two genes. Both mRNAs are transcribed from Ub I, the larger being the unspliced precursor of the smaller. A 674-base-pair intron was located within the 5'-noncoding region of Ub I. The second gene, Ub II, does not appear to code for an RNA species in normal or heat-shocked chicken embryo fibroblasts. The expression of ubiquitin mRNA during heat shock and recovery was examined. Addition of actinomycin D before heat shock completely abolished the response of ubiquitin mRNA to the stress. Analysis of the stability of the mRNA during recovery revealed that the mRNA accumulated during the heat shock is rapidly degraded with a half-life of approximately 1.5 h, suggesting a specialized but transient role for ubiquitin during heat shock.

Animals↗

Sequence requirement for expression of the Drosophila melanogaster heat shock protein hsp22 gene during heat shock and normal development.

A 14-base-pair sequence element present in almost all Drosophila melanogaster heat shock genes has been implicated in the heat inducibility of transcription. The D. melanogaster gene encoding the smallest heat shock protein, hsp22, contains within its 5' flanking sequences three such repeats, two close to the transcription start site and a distally located third one 101 base pairs further upstream. Deletion analyses reveal that the 5' flanking sequences required for full expression of the hsp22 gene extend beyond the distal repeat. Deletion of the furthest upstream repeat results in a five to sixfold reduction of gene expression. The small heat shock genes are transiently expressed in the late third instar larval and early pupal stages without external stimulation. A deletion of 5' flanking sequences to position -194, which includes two nucleotides of the distal heat shock element, has no effect on the developmental expression, whereas removal of an additional 18 nucleotides, including 12 nucleotides of the distal heat shock element, severely reduces developmental expression.

Animals↗

Genetic regulation during heat shock and function of heat-shock proteins: a review.

The induction by thermal stress of certain specific genes (heat-shock genes) first described in Drosophila has recently been observed in a wide variety of unicellular and multicellular organisms, emphasizing the basic importance of this ubiquitous response. Recent data dealing with the molecular mechanisms involved in the intensive transcriptional and posttranscriptional regulation during heat shock is reviewed with emphasis on the induction of the response and the putative function of the heat-shock proteins. A model showing the various interactions of cellular regulatory mechanisms operating in the heat-shocked cell is presented. While the list of agents or treatments inducing heat-shock proteins (hsp's) in various organisms is increasing, the identification of a hypothetical common inducing factor is elusive. The recently described reorganization of some cytoskeletal elements upon heat shock is discussed both in terms of its potential involvement in transcriptional and (or) translational regulation and of its putative relation with the cellular localization of the hsp's. Studies on the cellular localization of hsp's in various organisms do not show a clear uniform pattern which could help in elucidating the function of hsp's. On the other hand, studies on the thermal resistance of various cells types show a strong correlation between the induction of hsp's and the development of transitory thermotolerance. Such a protective function for hsp's can probably be extended to other types of cellular aggression.

Animals↗

Regulation mode of evaporative cooling underlying a strategy of the heat-tolerant FOK rat for enduring ambient heat.

Compared with other rat strains, the inbred FOK rat is extremely heat tolerant. This increased heat tolerance is due largely to the animal's enhanced saliva spreading abilities. The aims of the present study were to 1) quantify the heat tolerance capacity of FOK rats and 2) determine the regulatory mode of the enhanced salivary cooling in these animals. Various strains of rats were acutely exposed to heat. In the heat-intolerant strains, saliva spreading was insufficient and the core temperature (Tc) rose rapidly. In contrast, FOK rats maintained an elevated Tc plateau (39.5 +/- 0.7 degrees C) for 5-6 h over a wide range of ambient temperatures (Ta) (37.5-42.5 degrees C). In hot environments the FOK rats secreted copious amounts of saliva and spread it over more than the entire ventral body surface. FOK rats had a low Tc threshold for salivation, and the salivation rate increased linearly in proportion to the Tc deviation from the threshold. No strain difference or temperature effect was observed in the saliva secretion rate from in vitro submandibular glands perfused by sufficient doses of ACh. These results suggest that 1) the ability of FOK rats to maintain a moderate steady-state hyperthermia (39.5 +/- 0.7 degrees C) over a wide Ta range is enabled by a lowered threshold Tc for salivation and functional negative-feedback control of saliva secretion and 2) strain differences in ability to endure heat stress are mainly attributable to changes in the thermoregulatory control system rather than altered secretory abilities of the salivary glands.

Adaptation, Physiological↗

Effect of heat acclimatization on intravascular responses to acute heat stress in man.

The effects of a 185-min exposure to 48 degrees C db/33 degrees C wb, on intravascular volume and osmolarity and on intravascular electrolyte, aldosterone, and cortisol concentrations have been studied in five male subjects before and after acclimatization to heat. Changes in the hematocrit and plasma protein concentration indicated that a hemodilution occurred during the first 35 min of the heat exposures, and that this was followed by a hemoconcentration. Although these changes in intravascular volume were not affected by acclimatization, the plasma volume after heat acclimatization was 6.7% greater than before. This increase in plasma volume was associated with an elevation in the ratio [Na]/[K]. However, since plasma osmolarity decreased the intravascular expansion could not be explained in terms of elevated electrolyte levels. Plasma aldosterone and cortisol levels were not affected by heat acclimatization, although both were elevated following exercise in the heat. It is concluded that the adrenal cortex is not an important factor in maintaining a state of heat acclimatization once a salt balance has been achieved.

Acclimatization↗

Heat shock response, heat shock transcription factor and cell aging.

A characteristic feature of aging is a progressive impairment in the ability to adapt to environmental challenges. The purpose of this article is to review the evidence of an attenuated response to heat and physiological stresses in a number of mammalian aging model systems, including the human diploid fibroblasts in culture, whole animals and animal-derived cells and cell cultures, as well as peripheral blood mononuclear cells obtained from human donors. Analyses of the regulation and function of heat shock factor 1 (HSF1), a transcription factor that mediates the response to heat shock, showed that while the relative abundance of both the hsf1 transcript and the HSF1 protein did not change as a function of age, the responsiveness of HSF1 to heat-induced activation, as measured by its trimerization and ability to bind to the heat shock element consensus sequence, was inversely related to the age of the cells used. Given the fundamentally important role of heat shock proteins (HSPs) in many aspects of protein homeostasis and signal transduction it seems likely that the inability, or compromised ability, of aging cells and organisms to activate HSF1 and produce HSPs in response to stress would contribute to the well-known increase in morbidity and mortality of the aged when challenged.

Aging↗

Myocardial protection after whole body heat stress in the rabbit is dependent on metabolic substrate and is related to the amount of the inducible 70-kD heat stress protein.

The aims of this study were to examine the effects of whole body heat stress and subsequent stress protein induction on glycolytic metabolism, mitochondrial metabolism, and calcium handling within the heart. The effect of heat stress on glycolytic and mitochondrial pathways was examined by measuring contractile performance in the presence of glucose and pyruvate, respectively. Calcium handling was assessed using force-interval relationships. Right ventricular papillary muscles taken from heat-stressed and control rabbit hearts were superfused with Kreb's solution containing either glucose or pyruvate and rendered hypoxic for 30 min. After reoxygenation, the greatest recovery of contractile function occurred in the heat-stressed muscles with pyruvate as substrate; there was, however, no difference in the force-interval relationship between the groups. The degree of contractile recovery was related to the content of the inducible 70-kD but not the 65-kD, heat stress protein. This study suggests that heat stress enhances the ability of rabbit papillary muscle to use pyruvate, but not glucose, after reoxygenation, and that the differences seen in contractility may be secondary to induction of the 72-kD stress protein.

Animals↗

Characteristic expression of 105-kDa heat shock protein (HSP105) in various tissues of nonstressed and heat-stressed rats.

Although the induction of heat shock proteins (HSP) has been studied extensively in cultured cells, comparatively few studies have examined their expression in vivo. In this report, we investigated the expression and the state of 105-kDa heat shock protein (HSP105) in various tissues of rats, and found that two isoforms of HSP105 (HSP105-a and HSP105-b) were both moderately expressed in adrenal, spleen, liver and heart, and both increased markedly after heat shock. However, in brain HSP105-a was characteristically highly expressed over HSP105-b, but neither increased after heat shock. In addition, a 100-kDa protein (p100), a possible testis-specific HSP105 homologue was found in testis. When the effects of adrenaline and its antagonists on the heat-inducibility of HSP105 were examined, the induction of HSP105 in adrenal gland seemed to be negatively regulated through the alpha-adrenergic receptor. Furthermore, HSP105 was found to be associated with HSC70/HSP70, and to exist as high molecular mass complexes of 300-800-kDa and of 300-500-kDa in various tissues of nonstressed and heat-stressed rats, respectively. The molecular interaction between HSP105 and HSC70 suggests the possibility that HSP105 functions with HSC70 cooperatively in various tissues of rats.

Adrenergic Agents↗

Stresgenin B, an inhibitor of heat-induced heat shock protein gene expression, produced by Streptomyces sp. AS-9.

Stresgenin B was isolated as an inhibitor of heat-induced heat shock protein (HSP) gene expression from a culture broth of Streptomyces sp. AS-9 by silica gel chromatography and HPLC. The molecular formula of the novel compound was determined as C11H13NO5 by high resolution FAB-MS analysis, and the structure was determined by UV, 1H NMR, 13C NMR, HMQC, HMBC, and NOESY spectra. Stresgenin B inhibited heat-induced luciferase reporter-gene expression directed by the human hsp70B promoter in Chinese hamster ovary (CHO) cells at concentrations lower than the concentrations for inhibition of dexamethasone-induced luciferase reporter-gene expression directed by the mouse mammary tumor virus (MMTV)-LTR promoter. The inhibition of heat-induced reporter gene expression was evident even when cells were exposed to stresgenin B only during heat stress treatment. Moreover, the compound inhibited heat-induced syntheses of hsp72/73, hsp90, and hsp110 and thereby suppressed the induction of thermotolerance. Stresgenin B showed moderate cytotoxic activities against several neoplastic cell lines and also showed antibacterial activities against Micrococcus luteus, Bacillus subtilis and Staphylococcus aureus strains.

Animals↗

Heat shock and heat shock protein 70i enhance the oncolytic effect of replicative adenovirus.

Replication-competent viruses are currently being evaluated for their cancer cell-killing properties. These vectors are designed to induce tumor regression after selective viral propagation within the tumor. However, replication-competent viruses have not resulted heretofore in complete tumor eradication in the clinical setting. Recently, heat shock has been reported to partially alleviate replication restriction on an avian adenovirus (Ad) in a human lung cancer cell line. Therefore, we hypothesized that heat shock and overexpression of heat shock protein (hsp) would support the oncolytic effect of a replication-competent human Ad. To this end, we tested the oncolytic and burst kinetics of a replication-competent Ad after exposure to heat shock or to inducible hsp 70 overexpression by a replication-deficient Ad (Adhsp 70i). Heat-shock resulted in augmentation of Ad burst and oncolysis while decreasing total intracellular Ad DNA. Overexpression of hsp 70i also enhanced Ad-mediated oncolysis but did not decrease intracellular Ad DNA levels. We conclude that heat shock and Adhsp 70i enhance the Ad cell-killing potential via distinct mechanisms. A potential therapeutic implication would be the use of local hyperthermia to augment oncolysis by increasing the burst of replication-competent Ad. The role of hsp in Ad-mediated oncolysis should be additionally explored.

Adenoviruses, Human↗

[Induction of chilling tolerance and heat shock protein synthesis in rice seedlings by heat shock].

Heat shock applied to germinated rice seeds increased the chilling tolerance of seedlings. Comparison with the control, brief heat shock applied before chilling at 4 degrees C for 2 days and recovery at 25 degrees C for another 2 days decreased the permeability of cellular membranes and increased the content of proline in rice seedlings. Heat shock applied before chilling also increased the activities of superoxide dismutase, catalase, and peroxidase and the content of ascorbate in rice seedlings. In contrast, the lipoxygenase activity and the malondialdehyde content in the heat-shocked rice seedlings were lower than those in the control. Germinated rice embryos synthesized heat shock proteins of Mr 78, 70, 64, 46, 38, 24, 17 and 16 kD during heat shock. The results of Western blot suggested that the binding protein (Bip) of HSP70 play an important role in protecting the rice seedling against chilling damage.

Arabidopsis Proteins↗

Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae.

Transcription of the Saccharomyces cerevisiae CTT1 gene encoding the cytosolic catalase T has been previously shown to be derepressed by nutrient stress. To investigate whether expression of this gene is also affected by other types of stress, the influence of heat shock on CTT1 expression was studied. The results obtained show that expression of the gene is low at 23 degrees C and is induced rapidly at 37 degrees C. By deletion analysis, a promoter element necessary for high level induction by heat shock was located between base pairs -340 and -364 upstream of the translation start codon. This region was demonstrated to be sufficient for heat shock control by placing it upstream of a S. cerevisiae LEU2-lacZ fusion gene. Mutagenesis of the region showed that the response to heat shock is not mediated by a sequence similar to canonical heat shock elements, but by DNA elements also involved in nutrient control of transcription. Catalase T appears to have a function in protecting yeast cells against oxidative damage under stress conditions. Catalase T-containing strains are less sensitive to exposure to 50 degrees C ("lethal heat shock") than isogenic catalase T-deficient mutants, and catalase T-containing strains pretreated by incubation at 37 degrees C are less sensitive to H2O2 than pretreated catalase-deficient mutants.

Base Sequence↗

Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells.

The intracellular location of the major induced mammalian heat shock (or stress) protein (Mr = 72,000) has been determined by both biochemical and immunological methods. This protein, shown here to be comprised of at least three structurally related isoforms, is produced at high levels within 30 min to 1 h following heat treatment of cells. Biochemical fractionation of cells grown under heat shock showed that following its synthesis a portion of the 72,000-Da protein (and its isoforms) becomes associated with the nucleus while some remains in the cytoplasm. Indirect immunofluorescence studies using antiserum directed against the major isoforms of the 72,000-Da protein were carried out in normal and heat-shocked cells as well as in cells grown under stress by exposure to either an amino acid analogue or to sodium arsenite. Diffuse cytoplasmic and nuclear staining was observed in cells grown at 37 degrees C. In cells grown under heat shock conditions, both the cytoplasmic staining and the nuclear staining were found to increase with the nuclear staining consisting of both granular and patch-like structures, the latter being coincident with phase-dense nucleoli. In the case of cells exposed to amino acid analogues or to sodium arsenite, only cytoplasmic and to a lesser extent nuclear staining was observed, i.e. no localized nucleolar fluorescence was observed. Following return of heat shock-treated cells to normal growth temperatures, both the synthesis of the 72,000-Dalton stress protein and its nucleolar staining were found to diminish.

Animals↗