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PubMed1984

Improved preferential tumor hyperthermia with regional heating and systemic blood cooling: a balanced heat transfer method.

Absorption of power in large body volumes can occur with some approaches used for hyperthermia treatment of cancer. A systemic heat absorption rate exceeding the heat dissipation rate can lead to systemic temperature elevation that limits the magnitude and duration of application of power and hence the degree of preferential tumor temperature rise. We describe a hyperthermia approach consisting of regional electromagnetic power absorption and extracorporeal blood cooling with regulation of both systemic heat absorption and dissipation rates ("balanced heat transfer"). A test of this approach in five dogs with nonperfused tumor models demonstrated intratumoral temperatures greater than 42 degrees C, while systemic temperature remained at 33 degrees C and visceral temperatures within the heated region equilibrated between 33 and 42 degrees C. Solutions of the bioheat transfer equation were obtained for a simplified model with a tumor perfusion rate lower than surrounding normal tissue perfusion rate. In this model, the use of arterial blood temperatures less than 37 degrees C allowed higher power densities to be used, for given normal tissue temperatures, than when arterial temperature was greater than or equal to 37 degrees C. As a result, higher intratumoral temperatures were predicted. Control of arterial blood temperature using extracorporeal cooling may thus (1) limit systemic temperature rise produced by regional heating devices and (2) offer a means of improving intratumoral temperature elevations.

Animals↗
PubMed1994

Demonstration of heat-labile and heat-stable epitopes of Rickettsia japonica on ultrathin sections.

BACKGROUND: Spotted fever group rickettsiae including Rickettsia japonica have two major polypeptides and lipopolysaccharide (LPS)-like antigen on the surface. The major part of the antibodies to these polypeptides generated by immunization with live rickettsiae are reactive with heat-labile and conformation-dependent epitopes. EXPERIMENTAL DESIGN: To demonstrate and precisely localize the heat-labile and heat-stable epitopes on the major surface polypeptides and LPS-like antigen of R. japonica, the immunocolloidal gold method was performed on ultrathin sections with polyclonal and monoclonal antibodies. The antigenicity and fine structure were preserved by using periodate-lysine-paraformaldehyde as fixative, followed by embedding with the resin Lowicryl K4M at a polymerization temperature of -35 degrees C. RESULTS: Heat-labile and heat-stable epitopes on the two major surface polypeptides together with LPS-like antigen of R. japonica were demonstrated at the same location. These antigens were rather broadly distributed on the cell wall apart from the slime layer of the organism. The number of gold particles corresponding to the LPS-like antigen was much larger than that corresponding to the polypeptide antigen. CONCLUSIONS: Heat-labile epitopes of rickettsiae could be preserved and demonstrated by using the procedure cited here. Moreover, the precise localization of the major surface polypeptides and LPS-like antigen could be achieved in the cell wall by using ultrathin sections of infected cells instead of whole rickettsial cells. The LPS-like antigen was quantitatively predominant as judged by immunoelectron microscopy.

Antibodies, Monoclonal↗
PubMed1998

[Analysis of the body heat condition during muscular work based on the heat physical model of the rabbit body].

Quantitative data on body weight, heat absorption and heat conduction, value of relative body surface, and other values reflecting the main heat-physical parameters of the rabbit body, were obtained for a heat-physical model. The model "body" revealed a comparatively great heat inertia capacity which explains a passive rise of the "body" temperature in light or moderate physical work. Conditions of increasing the heat-physical efficacy of thermoregulatory vascular responses in animals, were revealed.

Animals↗
PubMedDate not supplied

[Dynamics of changes in integral parameters of muscle tissue heat resistance after preliminary heating at the damaging temperature in various frog species].

The dynamics of mean heat resistance of the Rana temporaria m. sartorius against heating at 38 degrees C were studied. The following indices were used: heat resistance (HR), coefficient of correlation between the initial HR level of the muscle and the magnitude and direction of its change, and coefficient of correlation between the heat resistance of the paired muscle and HR variability under the influence of preliminary heating at 38 degrees C for 5-180 min. Almost all these indices showed a biphasic pattern of changes with reference to the dose of preliminary treatment. The dynamics of the coefficient of correlation between the initial HR of muscle and its change and the coefficient of correlation between the resistance of paired muscle and HR variability provides much more information about both the pattern of muscle reaction to preliminary heating and muscle functional state than the mean HR level does.

Adaptation, Physiological↗
PubMed1998

The C-terminal hydrophobic repeat of Schizosaccharomyces pombe heat shock factor is not required for heat-induced DNA-binding.

The C-terminal hydrophobic repeat (CTR) of heat shock transcription factor (HSF) has been proposed to regulate DNA binding by intramolecular interactions with the leucine zipper motifs present in the HSF trimerization domain. Schizosaccharomyces pombe provides a useful model organism for the study of the regulation of HSF DNA binding because, unlike Saccharomyces cerevisiae, S. pombe hsf is highly heat shock inducible for DNA binding and contains a clear homology to the CTR. We examined the role that the CTR plays in the regulation of S. pombe hsf by constructing isogenic strains bearing deletion and point mutations in the chromosomal copy of hsf. Surprisingly, we found that point mutation of key hydrophobic amino acids within the CTR, as well as full deletion of it, yielded factors that show normal binding at normal growth temperatures and full levels of heat-induced binding. Deletion of the CTR did, however, slightly lower the temperature required for maximal activation. In contrast, a large deletion of the C-terminus, which removes close to a third of the coding sequence, was deregulated and bound DNA at control temperature. Several of the deletion mutants were significantly reduced in their level of expression, yet they showed wild-type levels of DNA binding activity following heat shock. These experiments demonstrate that appropriate regulation of the DNA binding activity of S. pombe hsf is not solely dependent upon the CTR, and imply that a feedback mechanism exists that establishes proper levels of DNA binding following heat shock despite mutations that significantly alter levels of total hsf.

Amino Acid Sequence↗
PubMed1996

Effect of caloric restriction on the expression of heat shock protein 70 and the activation of heat shock transcription factor 1.

The regulation of heat shock protein 70 (hsp70) expression is an excellent example of a cellular mechanism that has evolved to protect all living organisms from various types of physiological stresses; therefore, the reported age-related alterations in the ability of cells to express hsp70 in response to stress could seriously compromise the ability of a senescent organism in respond to changes in its environment. Because caloric restriction (CR) is the only experimental manipulation known to retard aging and increase the survival of rodents, it was of interest to analyze the effect of CR on the age-related alteration in the induction of hsp70 expression in rat hepatocytes. The effect of CR on the nuclear transcription of hsp70 gene in rat hepatocytes in response to various levels of heat shock was determined, and it was found that the age-related decline in the transcription of hsp70 at all temperatures studied was reversed by CR. Because the heat shock transcription factor (HSF) mediates the heat-induced transcription of hsp70, the effect of CR on the induction of HSF binding activity by heat shock was studied and found to arise from HSF1, which has been shown to be involved in the induction of HSF binding activity in other cell types. The age-related decrease in the induction of HSF1 binding activity in rat hepatocytes was reversed by CR, and did not appear to be due to an accumulation of inhibitory molecules with age. Interestingly, the level of HSF1 protein was significantly higher in hepatocytes isolated from old rats fed ad libitum compared to hepatocytes obtained from rats fed the CR diet even though the levels of HSF1 binding activity were lower for hepatocytes isolated from the old rats fed ad libitum. The levels of the mRNA transcript for HSF1 was not significantly altered by age or CR. Thus, the changes in HSF1 binding activity with age and CR do not arise from changes in the level of HSF1 protein available for activation.

Age Factors↗
PubMed1995

Identification of members of the HSP30 small heat shock protein family and characterization of their developmental regulation in heat-shocked Xenopus laevis embryos.

In the present study we have characterized the synthesis of members of the HSP30 family during Xenopus laevis development using a polyclonal antipeptide antibody derived from the carboxyl end of HSP30C. Two-dimensional PAGE/immunoblot analysis was unable to detect any heat-inducible small HSPs in cleavage, blastula, gastrula, or neurula stage embryos. However, heat-inducible accumulation of a single protein was first detectable in early tailbud embryos with an additional 5 HSPs at the late tailbud stage and a total of 13 small HSPs at the early tadpole stage. In the Xenopus A6 kidney epithelial cell line, a total of eight heat-inducible small HSPs were detected by this antibody. Comparison of the pattern of protein synthesis in embryos and somatic cells revealed a number of common and unique heat inducible proteins in Xenopus embryos and cultured kidney epithelial cells. To specifically identify the protein product of the HSP30C gene, we made a chimeric gene construct with the Xenopus HSP30C coding sequence under the control of a constitutive promoter. This construct was microinjected into fertilized eggs and resulted in the premature and constitutive synthesis of the HSP30C protein in gastrula stage embryos. Through a series of mixing experiments, we were able to specifically identify the protein encoded by the HSP30C gene in embryos and somatic cells and to conclude that HSP30C synthesis was first head-inducible at the early tailbud stage of development. The differential pattern of heat-inducible accumulation of members of the HSP30 family during Xenopus development suggests that these proteins may have distinct functions at specific embryonic stages during a stress response.

Amino Acid Sequence↗
PubMed2001

Heat-stress induced synthesis of chloroplast protein synthesis elongation factor (EF-Tu) in a heat-tolerant maize line.

A heat-tolerant maize (Zea mays L.) line, ZPBL 1304, synthesizes a unique set of five heat-shock polypeptides of 45 kDa. Previous studies suggested that these polypeptides might play a role in the development of thermotolerance in maize (Ristic et al., 1996, J. Plant Physiol. 149:424-432; Ristic et al., 1998, J. Plant Physiol. 153:497-505). In the present study, we isolated these polypeptides, sequenced them, and investigated their subcellular distribution and origin. Of the five polypeptides of 45 kDa, three polypeptides, including the two most abundant ones, yielded amino acid sequences similar to the chloroplast and bacterial protein synthesis elongation factor (EF-Tu). This was further confirmed using an antibody raised against maize EF-Tu, which showed a very strong reaction with the 45-kDa heatshock protein(s). Studies on subcellular distribution and origin revealed that the 45-kDa polypeptides were localized to the chloroplasts, and were likely of nuclear origin. A full-length maize EF-Tu cDNA (Zmeftu1), previously isolated from the B73 line of maize, was used as a probe for northern blot analysis of RNA extracted from the ZPBL 1304 maize line (the nucleotide and deduced amino acid sequences of Zmeftu1 are 88% identical to the rice EF-Tu sequence). Northern blots showed a 1.85-fold increase in steady-state levels of EF-Tu mRNA during heat stress. An increase in EF-Tu transcript levels during heat stress was accompanied by increased levels of the EF-Tu protein. Isolated chloroplasts from heat-stressed plants also had higher levels of EF-Tu as compared to control chloroplasts. The maize EF-Tu polypeptides showed > 80% sequence similarity with the bacterial EF-Tu, which has recently been shown to function as a molecular chaperone and to play a role in the protection of other proteins from thermal denaturation (Caldas et al., 1998, J. Biol. Chem. 273:11478-11482). It is hypothesized that chloroplast EF-Tu of the ZPBL 1304 maize line plays an important role in the development of thermotolerance.

Amino Acid Sequence↗
PubMed1996

Interleukin-4 upregulates the heat shock protein Hsp90alpha and enhances transcription of a reporter gene coupled to a single heat shock element.

Transcription of the heat shock protein Hsp90alpha was strongly upregulated in human T-cells by interleukin-4 (IL-4) and to a lesser extent by IL-2, reaching peak levels after 2-3 days of stimulation. Heat shock proteins are induced within minutes under stress conditions, via heat shock factors (HSF), which activate heat shock elements (HSE). IL-4, IL-2 and IL-13 upregulated transcription of a reporter gene coupled to a single HSE site and a minimal promoter. HSE may therefore be involved in cytokine induced heat shock gene transcription in the absence of cellular stress.

Base Sequence↗
PubMed2004

Coactivator ASC-2 mediates heat shock factor 1-mediated transactivation dependent on heat shock.

Upon exposure to elevated temperatures, mammalian cells increase the expression of the heat shock proteins (HSP) through activation of the heat shock factor 1 (HSF1). Since most transcription factors require coactivators for efficient transcriptional activity, we tried to identify the coactivator(s) that interacts with and modulates the activities of HSF1. In vitro glutathione S-transferase (GST) pull-down assay revealed that HSF1 strongly interacts with activating signal cointegrator (ASC)-2 and weakly with cyclic adenosine monophosphate responsive element binding protein (CBP). We also show that cotransfection of ASC-2, but not CBP, potentiates HSF1-mediated transactivation based on its cognate element (heat shock element, HSE) linked to luciferase reporter. The molecular interaction of HSF1 and ASC-2 was stimulated by heat shock in cells and the overexpression of HSF1-interacting domain of ASC-2 inhibited the specific induced protein association and HSF1-mediated transactivation. Taking these results together, we suggest that ASC-2 in a novel coactivator for HSF1 and heat shock stress may contribute the strong active transcription complex through sequential recruitment of HSF1 and ASC-2.

Binding Sites↗
PubMed1999

Influence of polyamines on DNA binding of heat shock and activator protein 1 transcription factors induced by heat shock.

Polyamine depletion, obtained in FAO cells with specific inhibitors of biosynthetic enzymes, prevents or decreases the accumulation of hsp 70 mRNA following heat shock [Desiderio et al., Hepatology 24 (1996) 150-156]. The present study shows that under conditions of spermidine depletion caused by alpha-difluoromethylornithine, the DNA binding capacity of the transcription factor HSF induced by heat shock undergoes a severe and prompt deactivation. Replenishment of the spermidine pool before heat shock re-establishes the DNA binding activity of HSF and the inducibility of hsp 70 mRNA. Similar to HSF, but with a different time-course, the DNA binding of the transcription factor AP-1 activated by heat shock is also impaired in spermidine-depleted cells and reversed by exogenous spermidine. STAT3 provides an example of a transcription factor slightly activated by heat shock but insensitive to polyamine decrease.

Animals↗
PubMed1999

ATPase activity of the heat shock protein hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat-induced apoptosis.

A major inducible heat shock protein, Hsp72, has previously been found to stimulate dephosphorylation (inactivation) of stress kinase JNK in heat-shocked cells and protect them from apoptosis. Using Rat-1 fibroblasts with constitutive expression of a human Hsp72 or its deletion mutant lacking an ATPase domain (C-terminal fragment (CTF)), we tested whether ATPase activity of Hsp72 is necessary for these effects. We found that expression of CTF markedly increased, similarly to the intact protein, JNK dephosphorylation in heat-shocked cells. As a result, JNK inactivation following heat shock occurred much faster in cells expressing either full-length or mutant Hsp72 than in parental cells and this was accompanied by suppression of heat-induced apoptosis. Thus, protein refolding activity of Hsp72 appears to be dispensable for its effect on JNK inactivation and apoptosis.

Adenosine Triphosphatases↗
PubMed1995

Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis.

ATHSF1 is a heat shock transcription factor (HSF) of Arabidopsis that is constitutively expressed but its activity for DNA binding, trimer formation and transcriptional activation of heat shock (hs) genes is repressed at normal temperatures. In this study the functional properties of chimeric HSF-glucuronidase (GUS) fusion proteins were tested. Ectopic expression of HSF-GUS or GUS-HSF in transgenic Arabidopsis plants resulted in a derepression of HSF functions as shown by trimer formation, specific DNA binding, and the constitutive expression of heat shock proteins (HSPs) at normal temperature. A novel GUS activity-staining protocol was used to show the specific binding of trimeric HSF fusion proteins to DNA and following hs, an interaction between chimeric HSF-GUS and authentic HSF proteins. The chimeric HSFs were insensitive to the negative regulation that counteracts activation of the authentic HSF at normal temperature. Heterotrimer complexes were reconstituted in vitro from recombinant ATHSF1 and HSF-GUS proteins expressed in Escherichia coli and using this protocol, the temperature-dependent activation of wt HSF was monitored in vivo and in vitro. Transgenic plants expressing constitutively active HSF-GUS fusion proteins are also constitutive for HSPs. Approximately 20% of the maximum heat-inducible levels of HSP18 were already present at normal temperature. The level of basic thermotolerance was significantly enhanced in these plants. The results indicate that genetic engineering using protein fusion is a very effective means to derepress the activity of an important regulatory protein in plants, that consequently activates a constitutive hs response in the absence of heat stress and eventually alters the thermotolerance phenotype.

Acclimatization↗
PubMed1998

Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis.

Heat shock transcription factor 1 (HSF1) is a member of the vertebrate HSF family that regulates stress-inducible synthesis of heat shock proteins (HSPs). Although the synthesis of the constitutively expressed and inducible members of the heat shock family of stress proteins correlates with increased cellular protection, their relative contributions in acquired cellular resistance or "thermotolerance" in mammalian cells is presently unknown. We report here that constitutive expression of multiple HSPs in cultured embryonic cells was unaffected by disruption of the murine HSF1 gene. In contrast, thermotolerance was not attainable in hsf1(-/-) cells, and this response was required for protection against heat-induced apoptosis. We conclude that 1) constitutive and inducibly expressed HSPs exhibit distinct physiological functions for cellular maintenance and adaptation, respectively, and 2) other mammalian HSFs or distinct evolutionarily conserved stress response pathways do not compensate for HSF1 in the physiological response to heat shock.

Alleles↗
PubMed2006

Genome-wide analysis reveals new roles for the activation domains of the Saccharomyces cerevisiae heat shock transcription factor (Hsf1) during the transient heat shock response.

In response to elevated temperatures, cells from many organisms rapidly transcribe a number of mRNAs. In Saccharomyces cerevisiae, this protective response involves two regulatory systems: the heat shock transcription factor (Hsf1) and the Msn2 and Msn4 (Msn2/4) transcription factors. Both systems modulate the induction of specific heat shock genes. However, the contribution of Hsf1, independent of Msn2/4, is only beginning to emerge. To address this question, we constructed an msn2/4 double mutant and used microarrays to elucidate the genome-wide expression program of Hsf1. The data showed that 7.6% of the genome was heat-induced. The up-regulated genes belong to a wide range of functional categories, with a significant increase in the chaperone and metabolism genes. We then focused on the contribution of the activation domains of Hsf1 to the expression profile and extended our analysis to include msn2/4Delta strains deleted for the N-terminal or C-terminal activation domain of Hsf1. Cluster analysis of the heat-induced genes revealed activation domain-specific patterns of expression, with each cluster also showing distinct preferences for functional categories. Computational analysis of the promoters of the induced genes affected by the loss of an activation domain showed a distinct preference for positioning and topology of the Hsf1 binding site. This study provides insight into the important role that both activation domains play for the Hsf1 regulatory system to rapidly and effectively transcribe its regulon in response to heat shock.

DNA-Binding Proteins↗
PubMed1998

The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo.

Plants synthesize several classes of small (15- to 30-kD monomer) heat-shock proteins (sHSPs) in response to heat stress, including a nuclear-encoded, chloroplast-localized sHSP (HSP21). Cytosolic sHSPs exist as large oligomers (approximately 200-800 kD) composed solely or primarily of sHSPs. Phosphorylation of mammalian sHSPs causes oligomer dissociation, which appears to be important for regulation of sHSP function. We examined the native structure and phosphorylation of chloroplast HSP21 to understand this protein's basic properties and to compare it with cytosolic sHSPs. The apparent size of native HSP21 complexes was > 200 kD and they did not dissociate during heat stress. We found no evidence that HSP21 or the plant cytosolic sHSPs are phosphorylated in vivo. A partial HSP21 complex purified from heat-stressed pea (Pisum sativum L.) leaves contained no proteins other than HSP21. Mature recombinant pea and Arabidopsis thaliana HSP21 were expressed in Escherichia coli, and purified recombinant Arabidopsis HSP21 assembled into homo-oligomeric complexes with the same apparent molecular mass as HSP21 complexes observed in heat-stressed leaf tissue. We propose that the native, functional form of chloroplast HSP21 is a large, oligomeric complex containing nine or more HSP21 subunits, and that plant sHSPs are not regulated by phosphorylation-induced dissociation.

Arabidopsis↗
PubMed1998

Glycogen synthase kinase 3beta and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock.

Heat shock transcription factor 1 (HSF-1) activates the transcription of heat shock genes in eukaryotes. Under normal physiological growth conditions, HSF-1 is a monomer. Its transcriptional activity is repressed by constitutive phosphorylation. Upon activation, HSF-1 forms trimers, acquires DNA binding activity, increases transcriptional activity, and appears as punctate granules in the nucleus. In this study, using bromouridine incorporation and confocal laser microscopy, we demonstrated that newly synthesized pre-mRNAs colocalize to the HSF-1 punctate granules after heat shock, suggesting that these granules are sites of transcription. We further present evidence that glycogen synthase kinase 3beta (GSK-3beta) and extracellular signal-regulated kinase mitogen-activated protein kinase (ERK MAPK) participate in the down regulation of HSF-1 transcriptional activity. Transient increases in the expression of GSK-3beta facilitate the disappearance of HSF-1 punctate granules and reduce hsp-70 transcription after heat shock. We have also shown that ERK is the priming kinase for GSK-3beta. Taken together, these results indicate that GSK-3beta and ERK MAPK facilitate the inactivation of activated HSF-1 after heat shock by dispersing HSF-1 from the sites of transcription.

Calcium-Calmodulin-Dependent Protein Kinases↗
PubMed2006

Heat shock-independent induction of multidrug resistance by heat shock factor 1.

The screening of two different retroviral cDNA expression libraries to select genes that confer constitutive doxorubicin resistance has in both cases resulted in the isolation of the heat shock factor 1 (HSF1) transcription factor. We show that HSF1 induces a multidrug resistance phenotype that occurs in the absence of heat shock or cellular stress and is mediated at least in part through the constitutive activation of the multidrug resistance gene 1 (MDR-1). This drug resistance phenotype does not correlate with an increased expression of heat shock-responsive genes (heat shock protein genes, or HSPs). In addition, HSF1 mutants lacking HSP gene activation are also capable of conferring multidrug resistance, and only hypophosphorylated HSF1 complexes accumulate in transduced cells. Our results indicate that HSF1 can activate MDR-1 expression in a stress-independent manner that differs from the canonical heat shock-activated mechanism involved in HSP induction. We further provide evidence that the induction of MDR-1 expression occurs at a posttranscriptional level, revealing a novel undocumented role for hypophosphorylated HSF1 in posttranscriptional gene regulation.

ATP Binding Cassette Transporter, Subfamily B, Mem↗