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At least 379 records · Page 21Linked to original sources
PubMed1982

A synthetic heat-shock promoter element confers heat-inducibility on the herpes simplex virus thymidine kinase gene.

Previous deletion analysis of the Drosophila hsp70 heat-shock promoter has identified a sequence upstream of the TATA box that is required for heat induction. This region contains homology to other heat-shock promoters, and it was proposed that the common sequence is an important element in the regulation of the heat-shock genes. We have constructed sequences similar to the consensus CT-GAA-TTC-AG from synthetic oligonucleotides and placed them upstream of the TATA box of the herpes virus thymidine kinase gene, in place of the normal upstream promoter element. The resultant genes are heat-inducible both in monkey COS cells and in Xenopus oocytes. We conclude that the transcriptional heat-shock response is mediated by some factor that interacts with this sequence.

Animals↗
PubMed2001

Contrasting effects of midazolam on induction of heat shock protein 27 by vasopressin and heat in aortic smooth muscle cells.

We previously showed that vasopressin stimulates the induction of heat shock protein (HSP) 27, a low molecular-weight HSP, through protein kinase C activation in aortic smooth muscle A10 cells. In the present study, we examined the effects of midazolam, an intravenous anesthetic, on the HSP27 induction stimulated by vasopressin, heat, or sodium arsenite (arsenite) in A10 cells. Midazolam inhibited the accumulation of HSP27 induced by vasopressin or 12-O-tetradecanoylphorbol 13-acetate (TPA), a direct activator of protein kinase C. Midazolam also reduced the vasopressin-induced level of the mRNA for HSP27. In contrast, midazolam enhanced the HSP27-accumulation induced by heat or arsenite. Midazolam also enhanced the heat-increased level of the mRNA for HSP27. However, midazolam had no effect on the dissociation of the aggregated form of HSP27 following stimulation by vasopressin, heat, or arsenite. These results suggest that midazolam suppresses vasopressin-stimulated HSP27 induction in vascular smooth muscle cells, and that this inhibitory effect is exerted at a point downstream from protein kinase C. In contrast, midazolam enhanced heat- or arsenite-stimulated HSP27 induction. Thus, midazolam has dual effects on the HSP27 induction stimulated by various stresses in vascular smooth muscle cells.

Anesthetics, Intravenous↗
PubMed1995

MAPKAP kinase 2 is activated by heat shock and TNF-alpha: in vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade.

The activation of MAPKAP kinase 2 was investigated under heat-shock conditions in mouse Ehrlich ascites tumor cells and after treatment of human MO7 cells with tumor necrosis factor-alpha (TNF-alpha). MAPKAP kinase 2 activity was determined using the small heat-shock proteins (sHsps) Hsp25 and Hsp27 as substrates. In both cell types, about a threefold increase in MAPKAP kinase 2 activity could be detected in a time interval of about 10-15 min after stimulation either by heat shock or TNF-alpha. Phosphorylation of MAPKAP kinase 2, but not the level of MAPKAP kinase 2 mRNA, was increased after heat shock in EAT cells. It is further shown that activation of MAPKAP kinase 2 in MO7 cells is accompanied by increased MAP kinase activity. These data strongly suggest that increased phosphorylation of the sHsps after heat shock or TNF-alpha treatment results from phosphorylation by MAPKAP kinase 2, which itself is activated by phosphorylation through MAP kinases. Hence, we demonstrate that MAPKAP kinase 2 is responsible not only for phosphorylation of sHsps in vitro but also in vivo. The findings link sHsp phosphorylation to the MAP kinase cascade, explaining the early phosphorylation of sHsp that is stimulated by a variety of inducers such as mitogens, phorbol esters, thrombin, calcium ionophores, and heat shock.

Animals↗
PubMed1991

Heat shock proteins in human and mouse embryonic cells after exposure to heat shock or teratogenic agents.

In human chorionic villus tissue at the 10-17th week of a normal pregnancy, heat shock proteins (hsp70, hsp73, hsp85, and hsp105) were induced in vitro by a heat shock or by exposure to sodium arsenite or cadmium chloride. In dispersed cells of the whole mouse embryo on the 11th day of development, heat shock proteins (hsp73 and hsp105) were induced by a heat shock or by exposure to sodium arsenite, but not by exposure to cadmium chloride. After a maternal hyperthermia or an intraperitoneal injection of sodium arsenite or cadmium chloride into a pregnant mouse, heat shock proteins accumulated in the embryo on the 9th day of development, especially in the neuroepithelial tissue. The significance of heat shock proteins in the embryo is discussed.

Animals↗
PubMed1979

Cardiovascular and metabolic manifestations of heat stroke and severe heat exhaustion.

We prospectively studied the clinical, biochemical (including creatine phosphokinase (CPK) isoenzymes) and electrocardiographic features of exertional heat stroke in 13 patients (group 1) and severe heat exhaustion in 14 patients (group 2). Despite initial presentations with severe hyperthermia, tachycardia and hypotension, only one patient with heat stroke had myocardial ischemia. The CPK isoenzymes were not indicative of myocardial damage in any patient. The patients with heat stroke were somewhat more dehydrated than those with heat exhaustion as measured by differences in serum creatinine, sodium and osmolality, and the former (group 1) had a significantly lower initial glucose level (P less than 0.05). Although significant differences in potassium were not observed in the pretreatment samples, at 12 hours the serum potassium was significantly lower in group 1 (P less than 0.05). This suggests that this group may have been more potassium-depleted at the time of heat stroke. Prompt recognition and vigorous therapy were successful in rapidly lowering high temperatures and in preventing serious complications.

Alanine Transaminase↗
PubMed1992

Effect of heat-shock on Plasmodium falciparum viability, growth and expression of the heat-shock protein 'PFHSP70-I' gene.

Cultures of the human malaria parasite Plasmodium falciparum were subjected to heat-shock for varying times and temperatures and then tested for their viability, growth and expression of heat-shock protein. Results show that the majority of parasites remained viable after heat-shock but their growth was affected. However, the expression of the heat-shock protein 'PFHSP70-I' gene was enhanced after heat-shock. We conclude that malarial parasites are able to survive in vivo during fever probably due to the overexpression of the heat-shock protein gene.

Animals↗
PubMed2005

CHIP interacts with heat shock factor 1 during heat stress.

Heat shock factor 1 (HSF1) is a major transactivator of heat shock genes in response to stress and mediates cell protection against various harmful conditions. In this study, we identified the interaction of CHIP (carboxyl terminus of the heat shock cognate protein 70-interacting protein) with the N-terminus of HSF1. Using GST full-down assay, we found that CHIP directly interacts with C-terminal deleted HSF1 (a.a. 1-290) but not with full-length HSF1 under non-stressed conditions. Interestingly, interaction of CHIP with full-length HSF1 was induced by heat shock treatment. The structural change of HSF1 was observed under heat stressed conditions by CD spectra. These observations demonstrate the direct interaction between HSF1 and CHIP and this interaction requires conformational change of HSF1 by heat stress.

Binding Sites↗
PubMed1982

Effects of forced convection of heated air on insensible water loss and heat loss in preterm infants in incubators.

To assess the effect of forced convection of heated air exchange in preterm infants in conventional incubators, we measured insensible water loss and total heat loss in preterm infants in a conventional forced convection incubator (air velocity 15 to 25 cm/second) and in a specially constructed still-air incubator (air velocity 0 to 2 cm/second) at equal operative temperature and humidity. Under the forced conditions, insensible water loss in the preterm infants increased by a mean 52% from 1.04 +/- 0.24 (mean +/- SD) to 1.58 +/- 0.51 ml/kg/hour (P less than 0.001). The ensuing increase in evaporative heat loss was partly reflected in the small but significant increase in total heat loss from 1.65 +/- 0.47 to 1.80 +/- 0.44 kcal/kg/hour (P less than 0.02). In the forced convection incubator, the increased evaporative heat loss in preterm infants was apparently partly compensated by a decreased nonevaporative heat loss. If reduction of insensible water loss is required, preterm infants should not be subjected to forced convection in incubators.

Air↗
PubMed1995

Protective effect of heat shock pretreatment with heat shock protein induction before hepatic warm ischemic injury caused by Pringle's maneuver.

BACKGROUND: Induction of heat shock proteins is thought to have a > cytoprotective effect against environmental stress and to result in a better ischemic tolerance. The protective ability of heat exposure and heat shock protein 72 (HSP 72) induction before warm ischemia caused by Pringle's maneuver was evaluated in rats. METHODS: Heat exposed rats (HS) were compared with control animals (C). The gene expression (messenger RNA) of HSP 72 and HSP 72 were detected by Northern and Western blot analyses. During 40 minutes of in situ reperfusion, liver energy metabolism and levels of standard liver enzymes were evaluated. The survival rate was determined after postoperative day 7. RESULTS: After heat exposure and recovery, messenger RNA of HSP 72 and HSP 72 can be detected strongly in HS group but not in C group. During reperfusion HS group exhibited a significantly (p < 0.01) improved energy metabolism, and the release of liver enzymes was significantly (p < 0.001) reduced compared with C group. Seven-day survival rate was 100% in HS group but at 50% was significantly impaired (p < 0.05) in C group. CONCLUSIONS: Heat exposure associated with HSP induction has a significant protective effect against warm ischemic liver injury, which results in a relevant improvement of survival rate.

Adenosine Triphosphate↗
PubMed1998

Isolation and characterization of a heat-induced gene, hcit2, encoding a novel 16.5 kDa protein: expression coincides with heat-induced tolerance to chilling stress.

Heat treatment of tomato fruits induces tolerance to chilling injury. We have previously shown that specific heat-shock proteins (HSPs) are expressed in heated tomato fruits after cold storage. To search for heat-induced genes that are expressed at low temperatures, a cDNA library prepared from pre-heated chilled tomato fruits was differentially screened. A novel cDNA clone, hcit2, encoding a protein of ca. 16.5 kDa, was isolated. The predicted protein contains three putative trans-membrane hydrophobic sequences, suggesting that the protein is membrane-localized. The expression of hcit2 in fruits was induced by high temperature, but not by other stresses such as low temperature, drought or anaerobic conditions, and not during fruit ripening. A high level of hcit2 transcript was found in heated fruits after 2 weeks at 2 degrees C. High temperatures also induced hcit2 expression in tomato leaves, flowers and stems. The HCIT2 protein may be involved in the acquisition of tolerance to chilling injury.

Amino Acid Sequence↗
PubMed1999

The rate and risk of heat-related illness in hospital emergency departments during the 1995 Chicago heat disaster.

OBJECTIVES: To conduct an Emergency Department (ED)-based treated prevalence study of heat morbidity and to estimate the rate and risk of heat morbid events for all Chicago MSA EDs (N = 95; 2.7 million visits per year). METHODS: ED patient log data were compiled from 13 randomly selected hospitals located throughout the Chicago MSA during the 2 weeks of the 1995 heat disaster and from the same 2-week period in 1994 (controls). Measurements included: age, sex, date, and time of ED service, up to three ICD-9 diagnoses, and disposition. RESULTS: Heat morbidity for Chicago MSA hospital EDs was calculated at 4,224 (95% CI = 2964-5488) cases. ED heat morbidity increased significantly 5 days prior to the first heat-related death. In 1995, there was an increase in the estimated relative risk for the city = 3.85 and suburbs = 1.89 over the control year of 1994. CONCLUSIONS: Real time ED-based computer automated databanks should be constructed to improve public health response to infectious or noninfectious outbreaks. Rapid area-wide M&M tabulations can be used for advancing the effectiveness of community-based prevention programs, and anticipating hospital ED resource allocation.

Adolescent↗
PubMed2001

Heat shock stimulation of a tilapia heat shock protein 70 promoter is mediated by a distal element.

We reported previously that a tilapia (Oreochromis mossambicus) heat shock protein 70 (HSP70) promoter is able to confer heat shock response on a reporter gene after transient expression both in cell culture and in microinjected zebrafish embryos. Here we present the first functional analysis of a fish HSP70 promoter, the tiHSP70 promoter. Using transient expression experiments in carp EPC (epithelioma papulosum cyprini) cells and in microinjected zebrafish embryos, we show that a distal heat shock response element (HSE1) at approx. -800 is predominantly responsible for the heat shock response of the tiHSP70 promoter. This element specifically binds an inducible transcription factor, most probably heat shock factor, and a constitutive factor. The constitutive complex is not observed with the non-functional, proximal HSE3 sequence, suggesting that both factors are required for the heat shock response mediated by HSE1.

Animals↗
PubMed1994

Isolation of a novel inducible rat heat-shock protein (HSP70) gene and its expression during ischaemia/hypoxia and heat shock.

Most of the members of the mammalian heat-shock protein (HSP) gene family have been studied and isolated from human and mouse cells. Few studies have concentrated on the HSPs of rat, a commonly used experimental animal. We have isolated and characterized a novel inducible rat HSP70 gene using an HSP70 cDNA sequence obtained from an ischaemic rat heart cDNA library. The isolated rat HSP70 gene was found to be a functional gene, as indicated by RNAase-protection and Northern-blot analysis. The deduced amino acid sequence of the inducible rat HSP70 exhibits a high degree of similarity to previously isolated mammalian inducible HSP70 gene products. Expression of the inducible HSP70 gene in rat myogenic cells (H9c2) is markedly increased after relatively short periods of hypoxia as well as by heat shock. Two heat-shock elements (HSE) are present in the rat HSP70 promoter. Transient transfection of rat HSP70 promoter/chloramphenicol acetyltransferase constructs into H9c2 cells shows that the presence of either of the two HSEs is sufficient for heat-shock inducibility. In contrast, induction of the rat HSP70/chloramphenicol acetyltransferase constructs by hypoxia is only detectable when both HSEs are present. This leads us to conclude that the induction of HSP70 by hypoxia and heat shock occurs through the same regulatory HSEs but the activation of the inducible HSP70 gene by heat shock is several-fold higher than by hypoxia.

Amino Acid Sequence↗
PubMed2000

Transient expression and heat-stress-induced co-aggregation of endogenous and heterologous small heat-stress proteins in tobacco protoplasts.

Heat-stress granules (HSG) are highly ordered, cytoplasmic chaperone complexes found in all heat-stressed plant cells. We have developed an experimental system involving expression of cytosolic class I and class II small heat-stress proteins (Hsps) of pea, Arabidopsis and tomato in tobacco protoplasts to study the structural prerequisites for the assembly of HSG or HSG-like complexes. Class I and class II small Hsps formed class-specific dodecamers of 210-280 kDa, which, upon heat stress, were incorporated into HSG complexes. Interestingly, class II dodecamers alone could form HSG-like complexes (auto-aggregation), whereas class I dodecamers could do so only in the presence of class II proteins (recruitment). By analysing C-terminal deletion forms of Hsp17 class II, we obtained evidence that the intact C-terminus is critical for the oligomerization state, for the heat-stress-induced auto-aggregation and for recruitment of class I proteins. The class-specific formation of dimers as a prerequisite for oligomerization was analysed by the yeast two-hybrid system. In the presence of the endogenous (tobacco) set of heat-stress-induced proteins, all heterologous class I and class II proteins were incorporated into HSG complexes, whose ultrastructure was different from that of complexes formed by class I and class II proteins alone. Although other, more distantly related, members of the Hsp20 family, i.e. the plastidic pea Hsp21, the Drosophila Hsp23 and the mouse Hsp25, were well expressed in tobacco protoplasts and formed homo-oligomers of 200-700 kDa, none of them could be recruited to HSG complexes.

Amino Acid Sequence↗
PubMed2002

Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants.

To examine functions of two small heat shock proteins of Escherichia coli, IbpA and IbpB, we constructed His-IbpA and His-IbpB, in which a polyhistidine tag was fused to the N-terminals. Both purified His-IbpA and His-IbpB formed multimers, which have molecular masses of about 2.0-3.0 MDa and consist of about 100-150 subunits. They suppressed the inactivation of several enzymes including citrate synthase and 6-phosphogluconate dehydrogenase by heat, potassium superoxide, hydrogen peroxide and freeze-thawing, but not the inactivation of glyceraldehyde-3-phosphate dehydrogenase by hydrogen peroxide. Both His-IbpA and His-IbpB suppressed enzyme inactivation by various treatments and were also found to be associated with their non-native forms. However, both His-IbpA and His-IbpB were not able to reactivate enzymes inactivated by heat, oxidants or guanidine hydrochloride. When heated to 50 degrees C, each multimeric form of His-IbpA or His-IbpB was dissociated to form a monomer for His-IbpA, and an oligomer of about one-quarter size for His-IbpB. These structural changes were reversible, as both heated proteins regained the multimeric structures after incubation at 25 degrees C. However, when exposed to hydrogen peroxide or potassium superoxide, the large multimeric forms of His-IbpA and His-IbpB were maintained. The results suggest that His-IbpA and His-IbpB suppress the inactivation of enzymes and bind non-native proteins to protect their structures from heat and oxidants.

Citrate (si)-Synthase↗
PubMed1982

Transcription of a Drosophila heat shock gene is heat-induced in Xenopus oocytes.

Xenopus cells, like many other eukaryotic cells, respond to heat treatments by increasing the rate of synthesis of a few characteristic proteins, the heat shock proteins. Because of the generality of this response, it seemed possible to examine the expression of isolated heat shock genes in a heterologous system. Phage 122 DNA, containing two identical genes coding for the Drosophila 70,000-dalton heat shock protein (hsp70 genes), was microinjected into Xenopus oocyte nuclei. The Drosophila hsp70 genes are transcribed efficiently in heat-treated oocytes (35-37 degrees C) to give RNA of the correct size and sequence content. Transcription is sensitive to low levels of alpha-amanitin and therefore is carried out by RNA polymerase II. At normal temperatures (20-28 degrees C) essentially no Drosophila-specific RNA is formed. The isolated insert fragment of phage 122 also gives RNA of correct length in heat-treated oocytes which hybridizes to the coding segment of Drosophila hsp70 genes only. At normal temperatures, however, its rate of transcription is variable and only RNA heterogeneous in size is formed.

Animals↗
PubMed1991

Selective activation of human heat shock gene transcription by nitrosourea antitumor drugs mediated by isocyanate-induced damage and activation of heat shock transcription factor.

Treatment of cultured human tumor cells with the chloroethylnitrosourea antitumor drug 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) selectively induces transcription and protein synthesis of a subset of the human heat shock or stress-induced genes (HSP90 and HSP70) with little effect on other stress genes or on expression of the c-fos, c-myc, or beta-actin genes. The active component of BCNU and related compounds appears to be the isocyanate moiety that causes carbamoylation of proteins and nucleic acids. Transcriptional activation of the human HSP70 gene by BCNU is dependent on the heat shock element and correlates with the level of heat shock transcription factor and its binding to the heat shock element in vivo. Unlike activation by heat or heavy metals, BCNU-mediated activation is strongly dependent upon new protein synthesis. This suggests that BCNU-induced, isocyanate-mediated damage to newly synthesized protein(s) may be responsible for activation of the heat shock transcription factor and increased transcription of the HSP90 and HSP70 genes.

Actins↗
PubMed1999

The activation of the rat copper/zinc superoxide dismutase gene by hydrogen peroxide through the hydrogen peroxide-responsive element and by paraquat and heat shock through the same heat shock element.

Copper/zinc superoxide dismutase (SOD1) protects cells against oxidative hazards by the dismutation of superoxide radicals. The promoter activity of the SOD1 gene was increased 3-5-fold by hydrogen peroxide, paraquat (PQ) and heat shock. Functional analyses of the regulatory region of the SOD1 gene by deletions, mutations, and heterologous promoter systems confirmed the induction of the SOD1 gene by H(2)O(2) through the hydrogen peroxide-responsive element (HRE) (between nucleotides -533 and -520). Gel mobility shift assays showed that the existence of an H(2)O(2)-inducible protein bound to the oligonucleotide of the HRE. Similar analyses showed that the heat shock activated the SOD1 promoter through the heat shock element (HSE) (between nucleotides -185 and -171). A strong specific far-shifted complex with the oligonucleotide of the HSE was observed by the treatment of heat shock. When cells were treated with PQ, a strong far-shifted complex with the HSE was observed and was competed out by the cold HSE probe, indicating that PQ also activated the SOD1 promoter through the same HSE site. It is very interesting to note that chemical and physical stresses, such as PQ and heat shock, respectively, activated the SOD1 promoter through the same cis-element HSE. These results indicate that the SOD1 was inducible by H(2)O(2) through the HRE and by PQ and heat shock through the same HSE to protect cells from oxidative hazards.

Animals↗