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PubMed1992

Heat-induced transcription from RNA polymerases II and III and HSF binding activity are co-ordinately regulated by the products of the heat shock genes.

Heat shock leads to co-ordinate increases in transcription of a family of heat shock genes, including the mouse hsp70.1 and B2 genes. Activation of the heat shock transcription factor (HSF) by heat shock stimulates transcription of the murine hsp70.1 gene (by RNA polymerase II). B2 genes are short, repetitive sequences whose transcription (by RNA polymerase III) are also increased after heat shock. We have studied whether heat-induced transcription is auto-regulated by the products of the heat shock genes. The results indicate: (1) after an initial heat shock, transcription of the heat shock genes by RNA polymerases II and III becomes desensitized to further heat shock, and the heat-induced DNA binding activity of the HSF is lost, (2) if accumulation of heat shock gene products is inhibited, the desensitizing effect of a prior heat shock is removed, and (3) transcription of the hsp70.1 and B2 genes apparently involves different mechanisms, with hsp70.1 employing the HSF and the B2 gene using a separate, heat-activated transcriptional mechanism. However, the level of transcription from the hsp70.1 and B2 genes and the stability of their respective RNAs are co-ordinately regulated by the level of heat shock protein in the cell. The data indicate that auto-regulation of the level of mouse heat shock gene products is mediated by RNA polymerase II transcripts but that the regulatory mechanism can control transcription from RNA polymerase III genes as well.

Animals↗

PubMed1993

Characterization of two maize HSP90 heat shock protein genes: expression during heat shock, embryogenesis, and pollen development.

We have isolated two genes from Zea mays encoding proteins of 82 and 81 kD that are highly homologous to the Drosophila 83-kD heat shock protein gene and have analyzed the structure and pattern of expression of these two genes during heat shock and development. Southern blot analysis and hybrid select translations indicate that the highly homologous hsp82 and hsp81 genes are members of a small multigene family composed of at least two and perhaps three or more gene family members. The deduced amino acid sequence of these proteins based on the nucleotide sequence of the coding regions shows 64-88% amino acid homology to other hsp90 family genes from human, yeast, Drosophila, and Arabidopsis. The promoter regions of both the hsp82 and hsp81 genes contain several heat shock elements (HSEs), which are putative binding sites for heat shock transcription factor (HSF) commonly found in the promoters of other heat shock genes. Gene-specific oligonucleotide probes were synthesized and used to examine the mRNA expression patterns of the hsp81 and hsp82 genes during heat shock, embryogenesis, and pollen development. The hsp81 gene is only mildly heat inducible in leaf tissue, but is strongly expressed in the absence of heat shock during the pre-meiotic and meiotic prophase stages of pollen development and in embryos, as well as in heat-shocked embryos and tassels. The hsp82 gene shows strong heat inducibility at heat-shock temperatures (37-42 degrees C) and in heat shocked embryos and tassels but is only weakly expressed in the absence of heat shock. Promoter-GUS reporter gene fusions made and analyzed by transient expression assays in Black Mexican Sweet (BMS) Maize protoplasts also indicate that the hsp82 and hsp81 are regulated differentially. The hsp82 promoter confers strong heat-inducible expression of the GUS reporter gene in heat-treated cells (60- to 80-fold over control levels), whereas the hsp81 promoter is only weakly heat inducible (5- to 10-fold over control levels).

Amino Acid Sequence↗

PubMed1988

Evidence for a role of heat-shock proteins in proliferation after heat treatment of synchronized mouse neuroblastoma cells.

A role for heat-shock proteins (HSPs) in proliferation after heat treatment was considered in synchronized mouse neuroblastoma cells. For this purpose enhancement of HSP synthesis after heat treatment was inhibited by actinomycin D and the effect of this on cell cycle progression into mitosis and on cell survival was studied both in thermoresistant G1- and in thermosensitive late S/G2-phase cells. In G1-phase cells expression of basal and heat-induced HSP synthesis was the same as that in late S/G2-phase cells, which suggests that regulation of thermoresistance throughout the cell cycle is not directly linked with HSP synthesis. The synthesis of HSP36, HSP68, and HSP70 was enhanced after a 30-min treatment at 41-43 degrees C. Increase of HSP synthesis after heat shock was partly suppressed by the presence of 0.1 microgram/ml actinomycin D during heat treatment, while 0.2 micrograms/ml prevented enhancement of HSP synthesis completely. Suppression of heat-induced HSP synthesis by actinomycin D had the same concentration dependency in G1- and late S/G2-phase cells. Actinomycin D potentiated induction of mitotic delay by heat treatment (30 min, 42.5 degrees C) but only under conditions where it actually inhibited heat-induced enhancement of HSP synthesis. Heat-induced cell killing was also potentiated by actinomycin D. The potentiating effect of actinomycin D on heat-induced mitotic delay and on heat-induced cell killing was more pronounced in G1-phase cells than in late S/G2-phase cells. These results give evidence for a role of HSPs in the resumption of proliferation after heat treatment and suggest that heated G1-phase cells are more dependent on HSP synthesis for recovery of proliferation after heat treatment than heated late S/G2-phase cells.

Animals↗

PubMed1986

Influence of rate of heating on thermosensitivity of L1210 leukemia: membrane lipids and Mr 70,000 heat shock protein.

We examined the effect of rate of temperature rise on the thermosensitivity of a murine lymphoblastic leukemia. L1210 cells suspended in RPMI 1630 medium:5% fetal bovine serum at pH 7.4 were heated from 37 degrees C-42 degrees C, or 44 degrees C over variable times (immediately, 30, 60, 120, 180 min) in a circulating water bath controlled by an electronic temperature programmer. Survival of the cells using a soft agar clonogenic assay was plotted against the time at final temperature so that a Do (min of heat required to reduce survival by 63% on the exponential portion of the survival curve) could be calculated as an estimate of thermosensitivity. Cells heated from 37 degrees C-42 degrees C over a time period of 30 min (10 degrees C/h) were less thermosensitive (Do 62.7 +/- 12.5 min) as compared to those exposed immediately to 42 degrees C (Do 38.5 +/- 2.2 min). Cells heated over a period of 180 min (1.6 degrees C/h) showed almost no death even after 4 h at 42 degrees C. Thermosensitivity of cells heated to several other high temperatures was also a function of rate of heating. This relative thermal resistance induced by slow heating was not a result of a change in membrane cholesterol content or fatty acid composition. Similarly, there was no difference between cells heated at slow and fast rates in cell cycle distribution or in cellular protein concentration. The major heat shock protein of Mr 70,000, which was induced by immediate heating, was not synthesized at the same high rate 1-12 h after heat treatment by the cells made thermotolerant with slow heating. We conclude that the thermosensitivity of this neoplastic cell can be altered considerably by the rate of heating. This alteration is not due to a change in membrane lipids. Furthermore, the heat shock protein at Mr 70,000 which was synthesized after immediate heating could not be demonstrated in the gradually heated L1210 leukemia cells.

Animals↗

PubMed2001

Cold cardioplegic arrest enhances heat shock protein 70 in the heat-shocked rat heart.

BACKGROUND: Myocardial content of the 70-kd heat shock protein has been found to correlate with improved cardiac recovery after ischemia, but the mechanisms and conditions that regulate its level, particularly under clinical conditions, are unclear. The aim of this study was to assess the effect of hypothermic cardioplegic arrest and reperfusion on the expression of 70-kd heat shock protein in a protocol mimicking conditions of preservation for cardiac transplantation. METHODS: Heat-shocked and control hearts were subjected to 4 hours of cardioplegic arrest and global ischemia at 4 degrees C and then to 20 minutes of reperfusion. Hearts were freeze clamped at different time points-after 15 minutes of Langendorff perfusion, at the end of ischemia, and after 20 minutes of reperfusion, and analyzed for heat shock protein 70 content by Western blotting. Another set of hearts was subjected to 10 minutes of normothermic ischemia and 20 minutes of reperfusion followed by freeze clamping and analysis of heat shock protein 70 content as in cardioplegic arrest protocol. Cardiac function was measured by means of a left ventricular balloon at the end of reperfusion. RESULTS: Preischemic concentration of 70-kd heat shock protein was increased in heat-shocked hearts compared with control hearts. The content of 70-kd heat shock protein in heat-shocked hearts was further increased from 5.0 +/- 2.4 ng/microg at the end of ischemia to 11.0 +/- 4.9 ng/microg (n = 8, mean +/- SD; P <.05) at 20 minutes of reperfusion after cold cardioplegic arrest. No further rise in 70-kd heat shock protein of the heat-shocked hearts was observed after normothermic ischemia. Maximal developed pressure was 120.8 +/- 13.4 mm Hg in control hearts compared with 164.7 +/- 22.5 mm Hg in heat-shocked hearts (n = 5, mean +/- SD; P =.037) after cardioplegic arrest. By contrast, after normothermic ischemia, maximum developed pressure was 111.2 +/- 10.9 mm Hg in control hearts compared with 139.2 +/- 11.0 mm Hg in heat-shocked hearts (n = 4, mean +/- SD; P =.031). CONCLUSION: Hypothermic cardioplegic arrest but not short normothermic ischemia triggered a further increase in the level of 70-kd heat shock protein in heat-shocked rat hearts, which may enhance endogenous cardiac protection.

Analysis of Variance↗

PubMed2002

[The expression of heat shock protein 70 (HSP70) in the cells of rat liver and cardiac muscle in different heat exposure stages].

OBJECTIVE: To show the changes of heat shock protein 70(HSP70) expression at cellular level in different heat exposure stages and the significance of HSP70 expression in heat exposure organism. METHOD: The heat exposure model was established in rats with artificial hot climatic chamber[34 +/- 1) degree C, RH 60%]. SD rats were randomly divided into control groups(C) and heat exposure groups(A), and into subgroups including 2, 7, 14, 28 d stages from each one of the groups. The immuno-histochemistry was used to detect HSP70 expression in rat liver and cardiac muscle, and photography analytic software was used to analyze HSP70 expression in liver and cardiac cells. RESULTS: The expression intensity of HSP70 in heat exposure groups(gray values of liver were 137.0 +/- 5.1, 137.0 +/- 5.2, 137.8 +/- 7.1, 139.2 +/- 5.2 respectively; of cardiac muscle 156.1 +/- 4.4, 155.1 +/- 6.2, 155.4 +/- 4.5, 156.2 +/- 5.1 respectively) was stronger than that in control groups(P < 0.01 or P < 0.05) during all stages of the heat exposure; There was no significant difference in expression intensity of HSP70 among various stages of heat exposure; after 2 d of heat exposure, HSP70 expression in cell nuclei of the liver and cardiac muscle cells was stronger than that in cytoplasm in heat exposure group; HSP70 expression in Kupffer's cells of liver was also stronger than that of control(P < 0.05), but not on 7, 14 and 28 d; the activities of alanine aminotransferase(ALT), aspartate aminotransferase(AST), creatine kinase(CK) and hydroxybutyrate dehydrogenase(HBD) showed an increase on 2 d and 28 d of heat exposure. CONCLUSION: The vital organs would be damaged on 2 d of heat exposure. High expression of HSP70 at this stage may be a marker of cell damage; Increased HSP70 expression on 7-14 d of heat exposure may play an important role in adaptation to heat, while long term(28 d) heat exposure, the protection of HSP70 from tissue damage may not be enough.

Adaptation, Physiological↗

PubMed1995

Heat generation and heat protection in methylmethacrylate cementation of vertebral bodies. A cadaver study evaluating different clinical possibilities of dural protection from heat during cement curing.

For metastatic disease of the spine, anterior operations on the vertebral bodies often include methylmethacrylate cementation. The cement curing process may produce high temperatures in the surroundings, as demonstrated in joint replacement surgery, and there is a risk of thermal injury to the spinal nerves. In cadavers, we studied the heat arising during curing of cement on the dural sac, and the temperature of the cement surface was measured when the vertebral body was reconstructed using acrylic cement in the same way as in tumor surgery. The temperature increase on the surface of the dural sac during polymerization was between 4 degrees and 12 degrees C, depending on the amount of protection. Only a moderate temperature elevation was measured on the surface of the dural sac, provided that the posterior cortex of the vertebra was retained together with 0.5 cm of the spongious bone or a silicone membrane.

Bone Cements↗

PubMed1978

Heat stress upon undressed man due to different combinations of elevated environmental temperature, air humidity, and metabolic heat production: a critical comparison of heat stress indices.

In several 100 climatic chamber experiments young healthy acclimatized men were exposed successively to combinations of ambient temperature and air humidity that were varied systematically from day to day within the range of 15 to 57 degrees C and 8 to 97% relative humidity, with air speed kept constant at 0.3 m/s. The subjects who were nearly nude were exposed at rest and at different treadmill work levels (metabolic rates up to about 1350 kJ/h). Each exposure lasted between two and six h. It was found that body temperatures and heart rate, but not loss of sweat, were suitable criteria for indicating equal stress conditions. Equations were derived describing those climatic combinations which were equivalent at the various activity levels of each subject. The slope of the respective equivalence curves plotted in psychrometric charts varied systematically with work level. The curves obtained for various subjects at any given activity level showed similarities, so that the calculation of an equivalence system common to all subjects seemed to be justified. A detailed comparison of these results with previous indices is presented. The combinations of ambient temperatures and humidities that were found to be equivalent under the given conditions of physical activity corresponded particularly well with the Index of Physiological Effect (ROBINSON et al.). There was also good agreement with the P4SR Index (MCARDLE et al.). The combinations corresponded with other indices (Heat Stress Index of BELDING and HATCH, Index of Thermal Stress of GIVONI) and with Basic Effective Temperature and Wet-bulb Globe Temperature only within limited ranges of climate depending upon work level. A procedure is presented which allows one to evaluate in terms of physiological responses how far various indices describe equivalent stress conditions correctly.

Adult↗

PubMed1996

Astrocyte survival and HSP70 heat shock protein induction following heat shock and acidosis.

Although severe acidosis is an important mediator of brain infarction, recent evidence suggests that mild acidosis may protect ischemic cells. The HSP70 heat shock protein is induced by acidosis in cultured cells and in ischemic brain and protects cells against many types of injury. Therefore, this study determined whether induction of heat shock proteins protects cultured astrocytes against acidosis. Brief exposure of cultured cortical astrocytes to acid (pH 5.2 for 40 min) or heat shock (45 degrees C for 40 min) markedly induced hsp70 mRNA and HSP70 protein. HSP70 protein was detected with the C92 monoclonal antibody (Welch and Suhan: J Cell Biol 103:2035, 1986), which has been shown to recognize the protein product of the full-length rat hsp70 cDNA (Longo et al: J Neurosci Res 36:325, 1993). Heat shock of the cultured cortical astrocytes completely protected the astrocytes from an otherwise lethal heat exposure 24 h later (45 degrees C for 4 h). In contrast, heat pretreatment sensitized the astrocytes to injury from acidosis 24 h later. Acid pretreatment, which markedly induced the HSP70 protein without producing astrocytic cell death, similarly sensitized the cells to injury from acidosis 24 h later (60% survival following pH 5.2 for 3 h versus 90% survival in controls; P < 0.0001). Surprisingly, heat shock pretreatment protected astrocytes against exposure to acid 48 h later (P < 0.05, 1.5-3 h), whereas acid pretreatment had no effect on astrocyte survival 48 h later. Since heat shock did not protect against acidosis at 24 h when HSP70 induction was maximal but did protect at 48 h when HSP70 was markedly diminished, the protective effect of heat shock at 48 h may be related to stress proteins present at 48 h. It is concluded that induction of HSP70 and other heat shock proteins by heat shock protects astrocytes against subsequent lethal heat shock. However, heat shock and acid treatment increase the vulnerability of astrocytes to acidosis 24 h later in spite of the induction of HSP70 heat shock proteins. The finding that heat shock protected astrocytes against acidosis 2 days later may suggest that delayed induction of stress proteins partially protects the astrocytes against damage produced by high concentrations of hydrogen ions.

Acidosis↗

PubMed1985

Heat-resistant variants of Chinese hamster fibroblasts altered in expression of heat shock protein.

Heat-resistant variants of the Chinese hamster HA-1 line have been isolated after repeated heat treatments. The heat-resistant phenotype has been stable for over 70 passages. One of the members of the 70-kDa heat shock protein family was found to be synthesized at greater levels in the heat-resistant variants under normal growth conditions. Mild heat treatment of the variant lines induced a transient thermotolerance that was accompanied by additional increase in the synthesis of the 70-kDa heat shock proteins. Cell-free translation of total cellular RNA revealed greater amounts of 70-kDa heat shock protein mRNA in both control and heated variant cells. The greater levels of 70-kDa heat shock protein synthesized in the variant cells presumably are a reflection of altered levels of its messenger mRNA. In addition, we found that translational control plays a role in the elevated expression of heat shock proteins in heat-shocked HA-1 cells and their heat-resistant variants. The association of the heat-resistant phenotype with increased levels of a 70-kDa heat shock protein suggests strongly that this gene product plays a role in protecting cells from damage inflicted by elevated temperatures.

Animals↗

PubMed1991

Loss of the intrinsic heat resistance of human cells and changes in Mr 70,000 heat shock protein expression in human x hamster hybrids.

Since mammalian cells vary widely in their intrinsic thermoresistance, we have investigated the genetic basis underlying this phenomenon in human and rodent cell lines. Typically, human cells are considerably more resistant to killing by heat than rodent cell lines. To determine whether the heat-resistant phenotype is dominant or recessive and to locate the chromosome(s) bearing determinants for heat resistance, we have prepared hybrids of heat-resistant human HT1080 cells and heat-sensitive Chinese hamster ovary (CHO) cells to test their response to heat. For both mass hybrid cultures and individual clones, the heat response of the hybrids was similar to that of the CHO parent. Analysis by in situ hybridization revealed the presence of five to 20 human chromosomes per cell in the mass hybrids and four to eight intact chromosomes plus some fragments in individual clones isolated from the hybrid cell population. A similar result was obtained using a different human cell line, AG1522. These data suggest that heat resistance is a recessive trait. Consistent with this conclusion are the results from a study of a fusion of HT1080 to a CHO mutant, BL-10, which was found to be hypersensitive to heat-induced killing. These hybrids had a normal CHO heat response and not the more heat-resistant phenotype of HT1080 cells. Two hybrid clones, H2 and H4, from the HT1080/BL-10 fusion were studied in more detail. Both clones possess similar amounts of Mr 70,000 heat shock protein (HSP70), despite the fact that H4 contains three human chromosomes (Nos. 6, 14, and 21) which carry HSP70 genes while H2 contains only one (chromosome 6). Both hybrid cell lines have the same response to heat. Although we found a wide range of sensitivities to heat, all cell lines contained a similar amount of constitutive HSP70, suggesting that HSP70 levels per se are not the critical determinant of intrinsic heat resistance.

Animals↗

PubMed1996

[Is reduction of intraoperative heat loss and management of hypothermic patients with anesthetic gas climate control advisable? Heat and humidity exchangers vs. active humidifiers ina functional lung model].

UNLABELLED: Heated humidifiers (HH) as well as heat and moisture exchangers (HME) are commonly used in intubated patients as air-conditioning devices to raise the moisture content of the air, thus preventing mucosal damage and heat loss resulting from ventilation with dry inspired gases. In contrary to HME, HH are able to add heat and moisture to the inspired air in surplus, which is often stressed as an advantage in warming hypothermic patients or reducing major heat losses, e.g., during long operations. The impact of air conditioning on the energy balance of man was calculated comparing HME and HH. METHODS: The efficiency of a HME (Medisize Hygrovent) and a HH (Fisher & Paykel MR 730) was evaluated in a mechanically ventilated lung model simulating the physiological heat and humidity conditions of the upper airways. The gas flow from the central supply was dry; the model temperature varied between 32 and 40 degrees C. By using a HH in the inspiratory limb, a circle system was simulated with water-saturated inspired air at room temperature. The water content of the ventilated air was determined at the tracheal tube connection using a fast, high-resolution humidity meter and was compared with the moisture return of the HME. The energy balance was calculated according to thermodynamic laws. RESULTS: Both HME and HH were able to create physiological heat and humidity conditions in the airways. With the normothermic patient model, the moisture return of the HME was equal to that of the HH set at 34 degrees C. Increasing the heating temperature resulted only in reduced water loss from the lung; heat and water input in the normothermic model was not possible. This was only effective with almost negligible amounts under hypothermic patient model conditions. DISCUSSION: The water content in the inspired and expired air is the most important parameter for estimating pulmonary heat loss in mechanically ventilated patients. In adults (minute volume approximately 71/min) the main fraction of pulmonary heat loss results from water evaporation from the airways (approximately 6 kcal/h), whereas the heat loss due to convection is negligible (approximately 1.2 kcal/h). In intubated patients ventilated with dry air, the heat loss increases to approximately 8 kcal/h due to greater water evaporation from the airways. Both HME and HH are able to reduce the pulmonary heat loss to 1-2 kcal/h. In normothermic as well as hypothermic patients, HH do not offer significant advantages in heat balance compared to effective HME. In conclusion, air conditioning in intubated patients is neither a powerful too for maintaining body temperature during long-lasting anaesthesia nor a sufficient method of warming hypothermic patients in intensive care units.

Air Conditioning↗

PubMed1994

Role of blood as heat source or sink in human limbs during local cooling and heating.

The objective of the present study was to investigate the relative contribution of the convective heat transfer in the forearm and hand to 1) the total heat loss during partial immersion in cold water [water temperature (Tw) = 20 degrees C] and 2) the heat gained during partial immersion in warm water (Tw = 38 degrees C). The heat fluxes from the skin of the forearm and finger were continuously monitored during the 3.5-h immersion of the upper limb (forearm and hand) with 23 recalibrated heat flux transducers. The last 30 min of the partial immersion were conducted with an arterial occlusion of the forearm. The heat flux values decreased during the occlusion period at Tw = 20 degrees C and increased at Tw = 38 degrees C for all sites, plateauing only for the finger to the value of the tissue metabolic rate (124.8 +/- 29.0 W/m3 at Tw = 20 degrees C and 287.7 +/- 41.8 W/m3 at Tw = 38 degrees C). The present study shows that, at thermal steady state during partial immersion in water at 20 degrees C, the convective heat transfer between the blood and the forearm tissue is the major heat source of the tissue and accounts for 85% of the total heat loss to the environment. For the finger, however, the heat produced by the tissue metabolism and that liberated by the convective heat transfer are equivalent. At thermal steady state during partial immersion in water at 38 degrees C, the blood has the role of a heat sink, carrying away from the limb the heat gained from the environment and, to a lesser extent (25%), the metabolic and conductive heats. These results suggest that during local cold stress the convective heat transfer by the blood has a greater role than that suggested by previous studies for the forearm but a lesser role for the hand.

Adolescent↗

PubMed1999

Heat stress preconditioning does not protect renal epithelial Na(+),K(+),Cl(-) and Na(+),P(i) cotransporters from their modulation by severe heat stress.

This study compares the effects of heat and osmotic stress on heat stress protein (HSP) production while examining the putative protective action of HSPs on modulation of Na(+),K(+),Cl(-) and Na(+),P(i) cotransporters in Madin-Darby canine kidney (MDCK) epithelial cells by severe heat stress (46 degrees C, 15 min). Preconditioning heat stress (43 degrees C, 20 min) followed by 4 h recovery at 37 degrees C led to a 35-fold increase of HSP70 mRNA expression measured by Northern blot analysis. The protein content of HSP70 and HSP27, assessed by Western blots, was augmented by 5- and 2-fold, respectively, after 6 h of recovery. In contrast to preconditioning heat stress, hyperosmotic stress (520 vs. 320 mosm) elevated HSP70 mRNA content only by 7-fold and did not significantly affect the protein content of HSP70 or HSP27. Neither cell survival, assessed as lactate dehydrogenase (LDH) release, nor the basal activities of the ion transporters and their modulation by protein kinase C, P(2)-purinoceptor and cell volume were altered by preconditioning heat stress. Severe heat stress increased extracellular LDH content from 3+/-2 to 23+/-5% and enhanced Na(+),K(+),Cl(-) and Na(+),P(i) cotransport activity by 2-3-fold. The volume- and protein kinase C-dependent regulation of these carriers was abolished by severe heat stress while regulation by P(2)-purinoceptors was preserved. Preconditioning heat stress diminished severe heat stress-induced LDH release to 11+/-4% but did not protect Na(+),K(+),Cl(-) and Na(+),P(i) cotransporters from activation by severe heat stress and did not prevent severe heat stress-induced inactivation of protein kinase C- and volume-dependent signaling pathways. These results show that in MDCK cells, preconditioning heat stress-induced HSPs are not involved in the regulation of Na(+),K(+),Cl(-) and Na(+),P(i) cotransporters and do not protect them from modulation by severe heat stress.

Animals↗

PubMed1998

Cytoprotection and regulation of heat shock proteins induced by heat shock in human breast cancer T47-D cells: role of [Ca2+]i and protein kinases.

Overexpression of heat shock protein 70 kDa alters the susceptibility of tumor cells to chemotherapeutic agents. We conducted experiments to study the regulation of expression of heat shock proteins (HSPs) in heat shock-treated T47-D cells, a human breast cancer cell line that expresses estrogen receptors. Cells exposed to heat shock at 44 degreesC displayed increased expression of heat shock protein 72 kDa (HSP-72), glucose-regulated protein 78 kDa (GRP-78), and GRP-94 in a time-dependent manner, as shown by [35S]methionine incorporation and Western blotting experiments. The maximal rate of synthesis occurred between 2 and 4 h after heat shock. Removal of external Ca2+ inhibited the synthesis of the heat shock-induced GRP-78 but not of HSP-72 and GRP-94, whereas treatment of cells with BAPTA (a Ca2+ chelator) inhibited HSP-72 and GRP-78. Treatment with H89 (a protein kinase A inhibitor) blocked the heat shock-induced GRP-78 synthesis, whereas GF-109203X (a protein kinase C inhibitor) attenuated the heat shock-induced HSP-72 synthesis and completely blocked synthesis of GRP-78 but not of GRP-94. These results indicate that protein kinase C is involved in regulation of the heat shock-induced synthesis of HSP-72, whereas PKA and PKC are involved in the regulation of GRP-78 synthesis. Cells overexpressing HSP-72 and GRPs after heat shock displayed resistance against lethal temperature (47 degreesC for 50 min) -induced death, which was diminished after removal of external Ca2+ and treatment with GF-109203X. Heat shock increased intracellular free Ca2+ concentration ([Ca2+]i) in a temperature- and heating duration-dependent fashion, and the increase was inhibited in the absence of external [Ca2+]i and significantly reduced by pretreatment with H89 and GF-109203X. The results suggest that different pathways are involved in the induction of synthesis of HSP-72, GRP-78, and GRP-94 by heat shock. It is highly likely that only HSP-72 and GRP-78 are involved in the process of cytoprotection from the thermal injury.

Calcium↗

PubMed2000

Heat transfer in a microvascular network: the effect of heart rate on heating and cooling in reptiles (Pogona barbata and Varanus varius).

Thermally-induced changes in heart rate and blood flow in reptiles are believed to be of selective advantage by allowing animal to exert some control over rates of heating and cooling. This notion has become one of the principal paradigms in reptilian thermal physiology. However, the functional significance of changes in heart rate is unclear, because the effect of heart rate and blood flow on total animal heat transfer is not known. I used heat transfer theory to determine the importance of heat transfer by blood flow relative to conduction. I validated theoretical predictions by comparing them with field data from two species of lizard, bearded dragons (Pogona barbata) and lace monitors (Varanus varius). Heart rates measured in free-ranging lizards in the field were significantly higher during heating than during cooling, and heart rates decreased with body mass. Convective heat transfer by blood flow increased with heart rate. Rates of heat transfer by both blood flow and conduction decreased with mass, but the mass scaling exponents were different. Hence, rate of conductive heat transfer decreased more rapidly with increasing mass than did heat transfer by blood flow, so that the relative importance of blood flow in total animal heat transfer increased with mass. The functional significance of changes in heart rate and, hence, rates of heat transfer, in response to heating and cooling in lizards was quantified. For example, by increasing heart rate when entering a heating environment in the morning, and decreasing heart rate when the environment cools in the evening a Pogona can spend up to 44 min longer per day with body temperature within its preferred range. It was concluded that changes in heart rate in response to heating and cooling confer a selective advantage at least on reptiles of mass similar to that of the study animals (0. 21-5.6 kg).

Animals↗

PubMed1991

Sodium dodecyl sulfate and heat induce two distinct forms of lobster muscle multicatalytic proteinase: the heat-activated form degrades myofibrillar proteins.

A multicatalytic proteinase (MCP) purified from lobster claw and abdominal muscles degrades a variety of peptide and protein substrates. The enzyme is activated by low concentrations (0.03%) of sodium dodecyl sulfate (SDS) and brief (1 min) heating at 60 degrees C. The lobster MCP can assume three stable and functionally distinct states in vitro; these are classified as the basal, heat-activated, and SDS-activated forms. The basal MCP possessed high trypsin-like peptidase activity and low chymotrypsin-like peptidase, peptidylglutamyl-peptide hydrolase, and caseinolytic activities; incubation of the basal form with SDS stimulated the peptidylglutamyl-hydrolase activity about 30-fold and inhibited the other three activities 80% to 100%. Heating the basal form stimulated caseinolytic activity about 6-fold with little effect on the peptidase activities. The heat-activated enzyme also degraded myosin, tropomyosin, troponin, and actin depolymerizing factor; alpha-actinin was resistant to proteolysis. Incubation of the heat-activated MCP with SDS inhibited the trypsin-like, chymotrypsin-like, and proteinase activities 95 to 100% and stimulated the peptidylglutamyl-hydrolase activity about 16-fold. Incubation of myosin with either the basal or the heat-activated forms in the presence of SDS generated identical proteolytic fragments of the myosin heavy chain, suggesting that SDS induced a third form that can be produced from either the basal or the heat-activated forms. The heat-activated form produced proteolytic fragments of myosin heavy chain different from those generated by either basal or heat-activated enzymes in the presence of SDS. Furthermore, 100 mM KCl stimulated the caseinolytic activity of the heat-activated form 24% and inhibited the trypsin-like and peptidylglutamyl-hydrolase activities 56 and 20%, respectively. These results, though indirect, suggest that heating induced a proteinase activity that was distinct from the three peptidase activities. Activation of the basal form with SDS was reversible, since precipitation of dodecyl sulfate with 100 mM KCl restored trypsin-like activity and inhibited peptidylglutamyl-hydrolase activity. In contrast, removal of dodecyl sulfate from the SDS-activated form that was derived from the heat-activated MCP induced its conversion to the basal form. Thus, although heat-activation was irreversible, the heat-activated form was converted back to the basal form via the SDS-activated form.

Amino Acid Sequence↗

PubMed1983

Influence of heating rate on control of heat loss from the tail in mice.

Although heating rate is important for stimulating thermoregulatory reflexes, it is not known if the control system differentiates between total heat gain and rate of heat gain. Exposing animals to microwaves inside a waveguide permits continuous monitoring of whole-body heat absorption. Tail skin temperature of restrained mice was recorded during whole-body exposure to 2,450-MHz microwave radiation at specific absorption rates (SAR) of either 11.5, 21.7, or 43.5 W . kg-1 and whole-body heat loads of 0.3-14 J . g-1. The integration of tail skin temperature with time, defined as the skin temperature index (STI), was measured as a function of absorbed heat load. At ambient temperatures of 20 and 25 degrees C the STI, averaged with respect to heat load, increased significantly with SAR. Depending on SAR, the sensitivity of heat loss from the tail to microwave exposure increased 32-71% per 1 degree C elevation in ambient temperature. The data indicate that heat loss from the tail increases with the whole-body heat load accrued from microwave exposure. When heat loss is averaged with respect to heat load, the rate of heat absorption and ambient temperature increase the sensitivity of thermoregulatory centers that control peripheral heat loss from the tail of mice.

Animals↗