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PubMed1994

Heat-shock protein induction in rat hearts. A direct correlation between the amount of heat-shock protein induced and the degree of myocardial protection.

BACKGROUND: Previous studies have demonstrated that heat-shock treatment results in the induction of 72-kD heat-shock protein (HSP72) and a reduction of infarct size after subsequent ischemia and reperfusion. METHODS AND RESULTS: To test the hypothesis that the degree of protection from ischemic injury in heat-shocked rats correlates with the degree of prior HSP72 induction, rats pretreated with 40 degrees C, 41 degrees C, or 42 degrees C of whole-body hyperthermia followed by 24 hours of recovery and control rats (n = 6 in each group) were quantitatively assessed for the presence of myocardial HPS72 by optical densitometry of Western blots and a primary antibody that is specific for HSP72 and a tertiary antibody labeled with 125I. Although rats heat-shocked to 40 degrees C had no significant induction of myocardial HSP72, rats heat-shocked to 41 degrees C and 42 degrees C demonstrated progressively increased amounts of myocardial HSP72 compared with controls. Separate groups of rats heat-shocked to 40 degrees C (n = 16), 41 degrees C (n = 37), and 42 degrees C (n = 36) with 24 hours of recovery and controls (n = 26) were subjected to 35 minutes of left coronary artery occlusion and 120 minutes of reperfusion. Compared with control and 40 degrees C rats, there was progressive infarct size reduction, assessed by triphenyltetrazolium chloride staining, in rats that were heat-shocked to 41 degrees C and 42 degrees C. Furthermore, there was a direct correlation between the amount of HSP72 induced and the reduction in infarct size (r = .97, P = .037). CONCLUSIONS: These results suggest that the improved salvage after heat-shock pretreatment may be related to the amount of HSP72 induced before prolonged ischemia and reperfusion.

Animals↗
PubMed2000

Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL.

Heat shock or transfection with heat shock protein 70 (Hsp70) genes has been shown to protect tumor cell lines against immune mechanisms of cytotoxicity. We have reported previously that heat shock confers resistance to CTL in the rat myeloma cell line Y3 that is Hsp70 defective. Evidence is now presented that Hsp70 is able to prevent the induction of the resistant phenotype. In Con A-stimulated lymphocytes and in lymphocyte x Y3 somatic cell hybrid clones a severe, non-Hsp70-inducing heat shock elicits resistance to CTL in contrast to a heat shock that results in Hsp70 expression. Thus, Hsp70 expression appears to be negatively associated with the development of resistance. Furthermore, loading of Y3 cells with recombinant Hsp70 protein before heat shock is able to prevent resistance. Because apoptosis induced in Y3 cells by heat shock is not affected, Hsp70 appears to interfere selectively with the CTL-induced lethal pathway that is found to be calcium but not caspase dependent. It is suggested that after heat shock Hsp70 enhances the CTL-induced apoptotic pathway by chaperoning certain proteins in the target cell that are involved in the execution of cell death. Thus, although shown to confer protection against many cytotoxic mechanisms, Hsp70 does not appear to be generally cytoprotective. This observation could also be of relevance when interpreting the effectiveness of tumor immunity.

Animals↗
PubMed1990

Use of polymerase chain reaction to detect the expression of the Mr 70,000 heat shock genes in control or heat shock leukemic cells as correlated to their heat response.

The expression of the Mr 70,000 heat shock protein (HSP-70) in heat-resistant variants or heat-shocked cells has been correlated with development of thermal resistance. In these studies polymerase chain reaction (PCR) was used to detect low levels of HSP-70 mRNA present in control, unheated cells to investigate the possibility of predicting the intrinsic heat response in various leukemic cells. The expression of two human heat shock genes in control or heat-shocked cells was investigated. Synthetic primers and probes from the untranslated region of the two HSP-70 genes sequenced by Hunt and Morimoto (HSP-70A)(C. Hunt and R. I. Morimoto, Proc. Natl. Acad. Sci. USA, 82: 6455-6459, 1985) and Voellmy et al. (HSP-70B)(R. Voellmy et al., Proc. Natl. Acad. Sci. USA, 82: 4949-4953, 1985) were used in PCR reactions to follow expression in control or heat-shocked leukemic K562, KG-1, and HL-60 cells. The PCR results were correlated with heat response and patterns of protein synthesis in these cells. Results indicate that, among leukemic cells, K562 was much more resistant to killing by heat shock than either KG-1 or HL-60 cells. All control cells, however, expressed the HSP-70B gene. Of the three leukemic cells tested, K562 was the most heat resistant and constitutively expressed the HSP-70A mRNA and the heat-inducible HSP-70 protein. KG-1 and HL-60 cells did not express this gene in unheated cells. All heat-shocked cells expressed the HSP-70A mRNA and the heat-inducible HSP-70 protein. However, there was no significant increase in the mRNA level of the HSP-70B in heat-shocked leukemic cells as measured by PCR or the S1-nuclease protection assay. Other cells including normal human bone marrow and normal and tumorous tissues of the colon and breast all expressed both genes in control cells. Normal breast tissue expressed less mRNA for HSP-70B gene than the tumor tissue obtained from the same patient. In all studies the amplified beta-actin mRNA expression was used as an internal standard. These studies indicate that HSP-70B gene is expressed in all control leukemic cells. The expression of this gene did not seem to correlate with intrinsic heat resistance. The HSP-70A expression correlated with intrinsic and transient heat resistance. These studies also indicate that both HSP-70 genes in humans may be expressed in a variety of unheated normal and tumorous tissues more so than previously reported.

Base Sequence↗
PubMed1987

Detection of mRNAs coding for translationally regulated heat-shock proteins in non-heat-shocked thymic lymphocytes.

Heat shock induces 31 proteins in thymic lymphocytes in 1 h, 11 of which are not blocked by cordycepin, suggesting that their induction may be regulated at the level of translation (Maytin, E.V., Colbert, R.A., and Young, D.A. (1985) J. Biol. Chem. 260, 2384-2392). The possibility that mRNAs coding for these 11 cordycepin-insensitive heat-shock proteins would be found in non-heat-shocked thymus cells was investigated. Analysis of 1500 in vitro translation products separated by giant two-dimensional gel electrophoresis revealed that poly(A)+ RNA isolated from non-heat-shocked thymus cells coded for proteins corresponding to 10 of the 11 non-cordycepin-inhibitable heat-shock proteins. Comparison of the relative rates of synthesis of these 10 proteins in whole cells incubated at 37 and 42 degrees C, with their synthesis in vitro directed by poly(A)+ RNA isolated from cells incubated at 37 degrees C, suggests that mRNAs for 7 of them are present in sufficient amounts in non-heat-shocked cells to account for their increased synthesis during heat shock. These results indicate that part of the response of thymic lymphocytes to heat shock involves a rapid increase in the translation of a group of pre-existing mRNAs that are normally translated at very low rates or not at all.

Animals↗
PubMed1993

A distal heat shock element promotes the rapid response to heat shock of the HSP26 gene in the yeast Saccharomyces cerevisiae.

Induction of heat shock genes is mediated by heat shock factor (HSF). Our recent genomic footprinting experiments demonstrate that HSF binds constitutively to perfect and imperfect heat shock elements (HSEs) in the HSP26 gene in yeast. Site-directed mutagenesis of the single perfect HSE, previously reported to not be involved in regulating gene expression, significantly reduces the rate of response of the gene to heat shock. However, the same mutation only slightly reduced the rate of accumulation of HSP26 mRNA during heat shock. Genomic footprinting experiments indicate that this lag in response to heat shock is due to the failure of HSF to bind efficiently to the mutated HSE. The rate of response to heat shock of synthetic promoters containing one, two, three, or seven perfect HSEs was similar to that observed for the wild-type HSP26 gene. These results suggest that the rate of response to heat shock is correlated with HSF occupancy of HSEs, rather than the number of HSEs in a promoter. As with the wild-type and mutant HSP26 genes, the rate of accumulation of mRNA from synthetic promoters increased only moderately with an increase in the number of HSEs. These results suggest that as few as two HSE-HSF complexes are sufficient to saturate HSF's target in the basal transcription apparatus.

Base Sequence↗
PubMed1995

Activation of heat shock factor 1 in rat brain during cerebral ischemia or after heat shock.

Recently, many studies have demonstrated the induction of stress proteins in the mammalian nervous system under various pathological conditions. These altered genetic programs may function to protect individual cells against stressful conditions. However, little is known about the molecular mechanisms regulating these stress responses in animals. We report here the activation of a heat shock factor (HSF) in the rat brain during cerebral ischemia or after heat shock. Gel mobility shift assays revealed an increase in DNA binding activity to the heat shock element (HSE) during the early phases of ischemia. Supershift experiments using specific antisera against HSF1 and HSF2 showed that the ischemia-induced HSE-binding activity was mainly due to HSF1. In the heat-shocked brain, HSF1 was also activated, and the HSE-binding activity was higher in the cerebellum than in the cerebral cortex or hippocampus; Western blot analysis also showed that HSF1 was more abundant in the cerebellum than in the other two brain regions. Our results indicate that heat shock gene transcription is regulated by the activation of HSF1 in both cerebral ischemia and heat shock, and that different brain regions display differential sensitivities in their stress response. The cellular signals for heat shock gene transcription under in vivo pathological conditions will also be discussed.

Animals↗
PubMed1998

Expression levels of heat shock factors are not functionally coupled to the rate of expression of heat shock genes.

The expression patterns of two mammalian heat shock factors (HSFs) were analysed in cell systems known to reflect an altered heat shock response. For being able to discriminate between the two closely related factors HSF 1 and HSF 2, specific cDNA sequences were cloned and used to generate antisense RNAs as hybridization probes. In general, in various cell lines expression of the two heat shock factors was clearly different. These expression patterns of the HSF genes were not influenced by retinoic acid-induced differentiation of human NT2 and mouse F9 teratocarcinoma cells. Generally, HSF 2 expression was extremely low, whereas the significantly higher expression of HSF 1 revealed cell specific differences. The highest expression rates of both HSFs were observed in 293 cells. To examine whether these high levels are involved in the constitutive expression of heat shock genes in these cells, we analysed the binding pattern of 293 cell proteins to the heat shock elements (HSEs). As with other cells, HSE-binding activity in 293 cells was only observed after heat shock treatment. This points to an HSE-independent way for high level expression of heat shock genes in these cells.

Animals↗
PubMed2003

The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response.

Previous work has implicated heat shock transcription factor 1 (HSF1) as the primary transcription factor responsible for the transcriptional response to heat stress in mammalian cells. We characterized the heat shock response of mammalian cells by measuring changes in transcript levels and assaying binding of HSF1 to promoter regions for candidate heat shock genes chosen by a combination of genome-wide computational and experimental methods. We found that many heat-inducible genes have HSF1 binding sites (heat shock elements, HSEs) in their promoters that are bound by HSF1. Surprisingly, for 24 heat-inducible genes, we detected no HSEs and no HSF1 binding. Furthermore, of 182 promoters with likely HSE sequences, we detected HSF1 binding at only 94 of these promoters. Also unexpectedly, we found 48 genes with HSEs in their promoters that are bound by HSF1 but that nevertheless did not show induction after heat shock in the cell types we examined. We also studied the transcriptional response to heat shock in fibroblasts from mice lacking the HSF1 gene. We found 36 genes in these cells that are induced by heat as well as they are in wild-type cells. These results provide evidence that HSF1 does not regulate the induction of every transcript that accumulates after heat shock, and our results suggest that an independent posttranscriptional mechanism regulates the accumulation of a significant number of transcripts.

Animals↗
PubMed1995

Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock.

Hsc66 is the second identified Hsp70 protein in Escherichia coli. Mutations in hscA, the gene encoding Hsc66, compensate for some phenotypic effects of a mutation in hns, a gene encoding the cold-inducible, nucleoid-associated protein H-NS. Expression of hscA was not induced upon heat shock but was induced approximately 11-fold 3 h after a shift from 37 to 10 degrees C. Furthermore, hscA was induced upon chloramphenicol addition, which induces the synthesis of other cold-inducible genes. Mapping of the transcription initiation site showed that hscA was cotranscribed with an upstream dnaJ-like gene, hscB; thus, hscB was also cold inducible. The hscBA promoter did not contain a Y-box element found in some cold-inducible promoters. Using two-dimensional electrophoresis, we identified Hsc66 under static 37 degrees C growth conditions and showed that Hsc66 was induced, as well as hscA, 3 h after a cold shock. Growth of an hscA mutant following cold shock was monitored relative to that of an isogenic wild-type strain. While cold shock adaptation as a function of growth rate was not significantly impaired in an hscA mutant, the expression of at least five other proteins was altered in this mutant following cold shock. On the basis of the homology to Hsp70 proteins and the induction following cold shock, we speculate that Hsc66 functions as a cold shock molecular chaperone.

Bacterial Proteins↗
PubMed1988

Evidence for protection by heat-shock proteins against photoinhibition during heat-shock.

The nuclear-coded 22 kd heat-shock protein (HSP-22) which is transported into the chloroplast and localized in the thylakoids was further characterized and found to be located in the grana lamellae (stacked thylakoids) as an extrinsic protein in the green alga Chlamydomonas reinhardtii. Inhibition of photosynthetic electron flow during heat-shock of Chlamydomonas cells was light-dependent, occurring at low-light intensities (<100 W/m) as compared with photoinhibition at 25 degrees C (>1000 W/m). The site of the damage was localized at the photosystem II (PS II) reaction center. The damage was drastically increased when heat-shock treatment was carried out in the presence of the 80S ribosomal translation inhibitor, cycloheximide (CHI). Pre-incubation of Chlamydomonas cells at 42 degrees C resulted in partial protection against photoinhibition during heat-shock, as compared with cells pre-incubated at 42 degrees C in the presence of CHI which, therefore, did not translate the heat-shock proteins. Analysis of the thylakoid polypeptides' pattern by SDS-PAGE revealed that during heat-shock in the light, thylakoid proteins became aggregated proportionally to the light intensity. Heat-shock in the presence of CHI enhanced the aggregation process which, at low light intensities, was specific to the PS II reaction center D1-protein. The results suggest that the chloroplasts HSPs prevent damage to the PS II reaction center during heat-shock in the light.

Journal Article↗
PubMed1990

Biological effects of shock waves: effect of shock waves on the liver and gallbladder wall of dogs--administration rate dependence.

The effect of extracoporeal shock waves on the liver and the gallbladder wall was compared in two groups of dogs exposed to 1500 shock waves generated in an electrohydraulic lithotripter with 15 kV and 80 nF. The waves were focused on the gallbladder wall. In the experimental group, a shock wave burst of 10 consecutive waves with an interval of 10 ms between the waves was administered each second; in the control group, single shocks were released each second. The day following shock wave exposure, the dogs were anaesthetized, killed and then dissected. In the liver, subcapsular and intraparenchymal focal haemorrhages occurred in the high pressure field and venous thrombi in portal veins. There was a nonsignificant trend towards an increased number of venous thrombi after burst application. The gallbladder wall was haemorrhagic and oedematous, the mucosa was ulcerated in the focal area; blood clots were found in nearly all gallbladders. No differences were detected between the groups. The free plasma haemoglobin was only increased after fast shock wave administration. Increased haemolysis and the trend towards an increased number of thrombi favour cavitation as a mechanism of shock wave damage. The similar extent of tissue damage suggests that shock wave bursts can be applied for gallstone destruction in humans if the major liver vessels are kept out of the high pressure field.

Animals↗
PubMed1988

Anaphylactic shock-induced conditioned taste aversion. II. Correlation between taste aversion and indicators of anaphylactic shock.

Previous studies (V. J. Djurić, B. M. Marković, M. Lazarević, & B. D. Janković, 1987, in B. D. Janković, B. M. Marković, & N. H. Spector (Eds.), Neuroimmune interactions, pp. 561-568, New York: New York Acad. Sci.; B. M. Marković, V. J. Djurić, M. Lazarević, & B. D. Janković, 1988, Brain Behav. Immun. 2, 11-23) have shown that rats learn to associate the taste of saccharin with the induction of anaphylactic shock, thus exhibiting conditioned taste aversion (CTA) toward an otherwise preferred saccharin solution. The present experiment investigates the effect of unconditioned stimulus intensity (the amount of antigen used for the induction of shock) on CTA. Rats were sensitized to ovalbumin and subjected to a conditioning trial in which the conditioned stimulus (CS; saccharin solution given orally) signaled the presentation of the unconditioned stimulus (US; shocking doses of ovalbumin ranging from 0.5 to 3 mg given intraperitoneally). Behavioral signs, hematocrit, and rectal temperature were used for evaluation of anaphylactic shock. Twenty-four hours after the conditioning trial, rats were subjected to a two-bottle preference test between saccharin solution and water. Multiple regression statistical analysis revealed significant correlations among saccharin preference ratio, dose of antigen used for the induction of shock, behavioral signs of shock, rise in hematocrit, and fall in rectal temperature. A dose-dependent relation among saccharin preference ratio and physiological indicators of shock suggests that conditioned anaphylactic shock-induced avoidance behavior is functionally related to homeostatic factors involved in immune reactivity.

Anaphylaxis↗
PubMed2004

Attenuated adult biphasic shocks compared with weight-based monophasic shocks in a swine model of prolonged pediatric ventricular fibrillation.

AIM: To compare the safety and efficacy of attenuated adult biphasic shocks with standard monophasic weight-based shocks in a piglet model of prolonged prehospital ventricular fibrillation (VF). BACKGROUND: If attenuated adult shocks are safe and effective for prehospital pediatric VF, automated external defibrillators (AEDs) can be easily adapted for pediatric use. METHODS: After 7 min of untreated VF, piglets were randomized to treatment with attenuated adult biphasic shocks or weight-based monophasic shocks. The attenuated adult biphasic group received 200/300/360 J shocks, attenuated by specialized pediatric electrodes to 51/78/81 J and the monophasic weight-based control group received 2/4/4 J/kg shocks. Forty-eight female piglets were studied, 16 in each of three weight categories: 4 kg (neonatal), 14 kg (younger child) and 24 kg (older child). The primary outcome measures of efficacy and safety were 24h survival with good neurological outcome and post-resuscitation left ventricular ejection fraction (LVEF), respectively. RESULTS: For the 24 kg piglets, attenuated adult biphasic shocks resulted in superior 24 h survival with good neurological outcome (6/8 versus 0/8, P < 0.001) and greater LVEF 4 h post-resuscitation (34 +/- 4% versus 18 +/- 5%, P < 0.05). For the 14 and 4 kg piglets, 24 h survival with good neurological outcome occurred in 7/8 versus 5/8 and 7/8 versus 3/8, respectively, and LVEF 4 h post-resuscitation was 30 +/- 3% versus 36 +/- 6% and 30 +/- 3% versus 22 +/- 4%, respectively. CONCLUSIONS: The escalating attenuated adult biphasic dosage strategy was at least as safe and effective as the standard weight-based monophasic dose over a wide range of weights in this piglet model of prehospital VF. This work supports the concept of using an attenuated adult biphasic dosage in children.

Animals↗
PubMed2000

Improvement of stone fragmentation during shock-wave lithotripsy using a combined EH/PEAA shock-wave generator-in vitro experiments.

To control the collapse of cavitation bubbles induced during shock-wave lithotripsy (SWL), a piezoelectric annular array (PEAA) shock-wave generator was fabricated and combined with an experimental electrohydraulic (EH) shock-wave lithotripter with a truncated HM-3 reflector. The PEAA generator consists of eight individual transducers of 200-kHz resonant frequency. At a discharge voltage of 15 kV, the PEAA generator produces a shock wave with a peak positive pressure of 8.2 MPa, a positive half cycle duration of 2.9 micros, and a -6-dB beam width of 5 mm. The trigger of the PEAA generator was controlled via fiberoptic link with reference to the spark discharge of the EH generator. Hence, the PEAA-generated shock wave could be used to interact with cavitation bubbles induced by the EH source at various stages of their oscillation. The duration of bubble oscillation during SWL was monitored by a 2.25-MHz focused hydrophone, and this information was used to control the release timing of the PEAA generator. Stone fragmentation tests in vitro were carried out, and demonstrated that stone comminution could be significantly enhanced when the shock wave-bubble interaction occurred during the collapsing phase of the bubbles. A maximum increment of 60% to 80% in stone fragmentation was achieved when the PEAA-generated shock wave arrives near the collapse of the bubbles. Under these conditions, much intensified collapse of the bubbles near the surface of the stone, with strong secondary shock-wave emission and increased stress concentration at the impact site of the solid boundary, was observed using high-speed shadowgraph and photoelastic imaging.

Calculi↗
PubMed1996

RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose absence triggers the cold-shock response.

The cold-shock response, characterized by a specific pattern of gene expression, is induced upon a downshift in temperature and in the presence of inhibitors of ribosomal function. Here, we demonstrate that RbfA of Escherichia coli, considered to be involved in ribosomal maturation and/or initiation of translation, is a cold-shock protein. Shifting the rbfA mutant to a lower temperature resulted in a constitutive induction of the cold-shock response accompanied by slower growth at low temperatures, while shifting the rbfA mutant that overproduces wild-type RbfA resulted in an increase in total protein synthesis accompanied by faster growth adaptation to the lower temperature. Furthermore, the cold-shock response was also constitutively induced in a cold-sensitive 16S rRNA mutant at low temperatures. Accompanying the transient induction of the cold-shock response, we also report that shifting E. coli from 37 degrees C to 15 degrees C resulted in a temporary inhibition of initiation of translation, as evidenced by the transient decrease in polysomes accompanied by the transient increase in 70S monosomes. The accumulative data indicate that the inducing signal for the cold-unadapted non-translatable ribosomes which are converted to cold-adapted translatable ribosomes by the association of cold-shock proteins such as RbfA. Therefore, the expression of the cold-shock response, and thus cellular adaptation to low temperature, is regulated at the level of translation. The data also indicate that cold-shock proteins can be translated by ribosomes under conditions that are not translatable for most mRNAs.

Bacterial Proteins↗
PubMed2005

Heat shock protein and heat shock factor 1 expression and localization in vaccinia virus infected human monocyte derived macrophages.

BACKGROUND: Viruses remain one of the inducers of the stress response in the infected cells. Heat shock response induced by vaccinia virus (VV) infection was studied in vitro in human blood monocyte derived macrophages (MDMs) as blood cells usually constitute the primary site of the infection. METHODS: Human blood monocytes were cultured for 12-14 days. The transcripts of heat shock factor 1 (HSF1), heat shock protein 70 (HSP70), heat shock protein 90 (HSP90) and two viral genes (E3L and F17R) were assayed by reverse transcriptase-polymerase chain reaction (RT-PCR), and the corresponding proteins measured by Western blot. Heat shock factor 1 DNA binding activities were estimated by electrophoretic mobility shift assay (EMSA) and its subcellular localization analyzed by immunocytofluorescence. RESULTS: It appeared that infection with vaccinia virus leads to activation of the heat shock factor 1. Activation of HSF1 causes increased synthesis of an inducible form of the HSP70 both at the mRNA and the protein level. Although HSP90 mRNA was enhanced in vaccinia virus infected cells, the HSP90 protein content remained unchanged. At the time of maximum vaccinia virus gene expression, an inhibitory effect of the infection on the heat shock protein and the heat shock factor 1 was most pronounced. Moreover, at the early phase of the infection translocation of HSP70 and HSP90 from the cytoplasm to the nucleus of the infected cells was observed. CONCLUSION: Preferential nuclear accumulation of HSP70, the major stress-inducible chaperone protein, suggests that VV employs this particular mechanism of cytoprotection to protect the infected cell rather than to help viral replication. The results taken together with our previous data on monocytes or MDMs infected with VV or S. aureus strongly argue that VV employs multiple cellular antiapoptotic/cytoprotective mechanisms to prolong viability and proinflammatory activity of the cells of monocytic-macrophage lineage.

Journal Article↗
PubMed1970

The effect of stimuli followed by response-independent shock on shock-avoidance behavior.

Four rhesus monkeys were trained on a non-discriminated shock-avoidance schedule (baseline). Stimuli followed by response-independent shock were then presented with the avoidance baseline no longer in effect. The main portion of the experiment consisted of superimposing (independently of responding) the stimuli followed by response-independent shock on the avoidance baseline. Different temporal values of stimulus duration and delay of shock (produced by an avoidance response) were presented successively, using each subject as his own control. When the stimulus duration was short or the delay of shock was long, so that avoidance rate during the stimulus could assume any value without resulting in baseline (avoidable) shocks during the stimulus, a lowered or "suppressed" rate of responding developed during the stimulus. When the stimulus duration was long or the delay of shock was brief, so that avoidable shocks resulted from a response decrement during the stimulus, high or "facilitated" rates of responding developed for a large proportion of the time that the stimulus was present.

Animals↗
PubMed2005

The maize heat shock factor-binding protein paralogs EMP2 and HSBP2 interact non-redundantly with specific heat shock factors.

The heat shock response (HSR) is a conserved mechanism by which transcripts of heat shock protein (hsp) genes accumulate following mobilization of heat shock transcription factors (HSFs) in response to thermal stress. Studies in animals identified the heat shock factor-binding protein1 (HSBP1) that interacts with heat shock transcription factor1 (HSF1) during heat shock attenuation; overexpression analyses revealed that the coiled-coil protein HSBP1 functions as a negative regulator of the HSR. Zea mays contains two HSBP paralogs, EMP2 and HSBP2, which exhibit differential accumulation during the HSR and plant development. Embryo-lethal recessive emp2 mutations revealed that EMP2 is required for the down-regulation of hsp transcription during embryogenesis, whereas accumulation of HSBP2 is induced in seedlings following heat shock. Notwithstanding, no interaction has yet been demonstrated between a plant HSBP and a plant HSF. In this report 22 maize HSF isoforms are identified comprising three structural classes: HSF-A, HSF-B and HSF-C. Phylogenetic analysis of Arabidopsis, maize and rice HSFs reveals that at least nine ancestral HSF isoforms were present prior to the separation of monocot and eudicots, followed by differential amplification of HSF members in these lineages. Yeast two-hybrid analyses show that EMP2 and HSBP2 interact non-redundantly with specific HSF-A isoforms. Site-specific mutagenesis of HSBP2 reveals that interactions between hydrophobic residues within the coiled coil are required for HSF::HSBP2 binding; domain swapping demonstrate that the isoform specificity of HSF::HSBP interaction is conferred by residues outside of the coiled coil. These data suggest that the non-redundant functions of the maize HSBPs may be explained, at least in part, by the specificity of HSBP::HSF interactions during plant development.

Amino Acid Motifs↗