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PubMed1992

Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: multiple pathways to induce tolerance?

Recent data indicate that cells may acquire thermotolerance via more than one route. In this study, we observed differences in thermotolerance development in HeLa S3 cells induced by prior heating (15 minutes at 44 degrees C) or pretreatment with sodium-arsenite (1 hour at 37 degrees C, 100 microM). Inhibition of overall protein and heat shock protein (HSP) synthesis (greater than 95%) by cycloheximide (25 micrograms/ml) during tolerance development nearly completely abolished thermotolerance induced by arsenite, while significant levels of heat-induced thermotolerance were still apparent. The same dependence of protein synthesis was found for resistance against sodium-arsenite toxicity. Toxic heat, but not toxic arsenite treatments caused heat damage in the cell nucleus, measured as an increase in the protein mass of nuclei isolated from treated cells (intranuclear protein aggregation). Recovery from this intranuclear protein aggregation was observed during post-heat incubations of the cells at 37 degrees C. The rate of recovery was faster in heat-induced tolerant cells than in nontolerant cells. Arsenite-induced tolerant cells did not show an enhanced rate of recovery from the heat-induced intranuclear protein aggregation. In parallel, hyperthermic inhibition of RNA synthesis was the same in tolerant and nontolerant cells, whereas post-heat recovery was enhanced in heat-induced, but not arsenite-induced thermotolerant cells. The more rapid recovery from heat damage in the nucleus (protein aggregation and RNA synthesis) in cells made tolerant by a prior heat treatment seemed related to the ability of heat (but not arsenite) to induce HSP translocations to the nucleus.

Arsenic↗
PubMed1992

Inhibition of heat shock gene expression does not block the development of thermotolerance.

After cells have been exposed to a nonlethal heat shock, they develop an enhanced resistance to subsequent prolonged heat shock. This process, termed thermotolerance, correlates with the expression of a group of proteins called the heat shock proteins. When cells are exposed to heat, protein synthesis is rapidly turned off and takes 5-6 hr to recover. In thermotolerant cells, protein synthesis is not blocked by heat. The heat shock proteins are thought to be responsible for the development of thermotolerance and the protection of the protein synthesis machinery from heat inactivation. To test the hypothesis that the heat shock proteins are involved in the heat shock response, we used two inhibitors to block their transcription and expression during heating and then monitored the effect on the development of thermotolerance and on protein synthesis. Camptothecin inhibits DNA topoisomerase I and blocks transcription of all actively transcribed genes, whereas dichloro-D-ribofuranosylbenzimidazole (DRB) inhibits only those genes transcribed by RNA polymerase II. Both DRB and camptothecin blocked the heat-induced expression of the heat shock proteins, but the absence of these proteins did not block either the development of thermotolerance or the protection of protein synthesis after heating. The data indicate that thermotolerance can develop in the absence of new protein synthesis.

3T3 Cells↗
PubMed1987

Protein synthesis patterns following stage-specific heat shock in early Drosophila embryos.

Very short heat shocks are administered to carefully staged early embryos of Drosophila melanogaster, and the effects on protein synthesis pattern investigated. A shock as short as 2 min will induce the heat shock response (reduction of normal protein synthesis, increased synthesis of the heat shock proteins) in syncytial blastoderm or later stages. Thus the initial events of the heat shock response must occur within 2 min, and not reverse upon rapid return to 22 degrees C. A low level of synthesis of the 70 kDA heat shock protein is sometimes visible in unshocked animals, but may be induced by the labeling procedure. Survival following a short shock is not strictly correlated with a high level of heat shock response. Pre-blastoderm embryos do not produce significant heat shock protein, but survive a 2 min 43 degrees C heat shock better than do heat shock response competent blastoderm embryos. The protein synthesis pattern prior to the blastoderm stage is very stable, possibly enhancing survival following a short shock. Shocks of 3 min or longer are more detrimental to pre-blastoderm embryos than to later stages, confirming the role of the heat shock response in survival following a longer shock. Stage-specific developmental defects (phenocopies) may be induced by heat shock at the blastoderm or later stages. Induction of these defects may require disruption of the normal protein synthesis pattern. Use of very short heat shocks to induce the heat shock response will be valuable in identifying the precise time at which a specific defect can be induced.

Age Factors↗
PubMed1993

Transcriptional regulation in Drosophila during heat shock: a nuclear run-on analysis.

We used a nuclear run-on assay as a novel approach to study the changes in transcriptional activity that take place in Drosophila melanogaster during heat shock. In response to a rapid temperature upshift, total transcriptional activity in cultured KC161 cells decreased proportionally to the severity of the shock. After extended stress at 37 degrees C (15 min or more), transcription was severely reduced, and at 39 degrees C most transcription was instantaneously arrested. However, strikingly different responses were observed for individual genes. Transcription of histone H1 genes was severely inhibited even under mild heat shock conditions. Transcription of the actin 5C gene decreased progressively with increasing temperature, while transcription of the core histone genes or of the heat shock cognate genes was repressed only under severe heat shock conditions. Transcriptional activation of the D. melanogaster heat shock genes was also investigated. In unshocked cells, hsp84 was moderately transcribed, while transcriptional activity at the other protein-coding heat shock genes was undetectable (less than 0.2 polymerases per gene). Engaged but paused RNA polymerase molecules were found at the hsp70 and hsp26 genes, but not at the other heat shock genes. The rates of transcription increased with increasing temperature with a peak of expression at around 35 degrees C. At 37 degrees C, induction was less efficient, and no induction was achieved after a rapid shift to 39 degrees C. Increased transcription of the heat shock genes was observed within 1-2 min of heat shock, and maximal rates were reached within 2-5 min. Despite very similar profiles of response, different heat shock genes were transcribed at strikingly different rates, which varied over a 20-fold range. The noncoding heat shock locus 93D was transcribed at a very high rate under non-heat shock conditions, and showed a transcriptional response to elevated temperatures different from that of protein-coding heat shock genes. An estimation of the absolute rates of transcription at different temperatures was obtained.

Animals↗
PubMed2001

Heat stress induces the synthesis of a new form of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in cotton leaves.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) activase mRNA and protein synthesis were measured in the leaves of cotton (Gossypium hirsutum L.) plants under control (28 degrees C) or heat-stress (41 degrees C) conditions. A decline in activase transcript abundance occurred rapidly during the photoperiod and was unaffected by heat stress. In response to high temperature, de novo protein synthesis rapidly shifted from mainly expression of Rubisco large and small subunits to the major heat-shock proteins, while de novo synthesis of the constitutively expressed 47- and 43-kDa activase polypeptides was not appreciably altered. However, heat stress induced the synthesis of a 46-kDa polypeptide that immunoprecipitated with antibodies monospecific to activase. Expression of the 46-kDa polypeptide ceased within 1 h of the return of heat-stressed plants to control conditions. Activase precursors of 55 and 51 kDa were detected among the in vitro translation products of RNA from control and heat-stressed plants. In addition, a 53-kDa polypeptide that also immunoprecipitated with anti-activase IgG was among the in vitro translation products of RNA from heat-stressed plants. This putative activase precursor did not occur among the in vitro translation products of RNA from plants that had recovered from heat stress. The levels of the constitutive 47- and 43-kDa activase polypeptides were similar in control and heat-stressed plants, based on immunoblotting with antibodies to activase. However, a 46-kDa cross-reacting polypeptide was also present in heat-stressed plants and constituted about 5% of the total activase after 48 h at high temperature. The identity of the heat-induced 46-kDa polypeptide as activase was confirmed by protein sequencing, which showed that its N-terminal sequence was identical to that of the constitutive 47-kDa activase polypeptide. The presence of multiple isoforms for both the 47- and 43-kDa activase polypeptides on immunoblots of two-dimensional gels and the complex banding pattern on Southern blots together suggest the existence of more than one activase gene and the possibility that the synthesis of the heat-induced activase polypeptide may be regulated transcriptionally. Induction of a new form of activase may constitute a mechanism of photosynthetic acclimation to heat stress in cotton.

Antibodies↗
PubMed2006

Heat wave impacts on mortality in Shanghai, 1998 and 2003.

A variety of research has linked extreme heat to heightened levels of daily mortality and, not surprisingly, heat waves both in 1998 and in 2003 all led to elevated mortality in Shanghai, China. While the heat waves in the two years were similar in meteorological character, elevated mortality was much more pronounced during the 1998 event, but it remains unclear why the human response was so varied. In order to explain the differences in human mortality between the two years' heat waves, and to better understand how heat impacts human health, we examine a wide range of meteorological, pollution, and social variables in Shanghai during the summers (15 June to 15 September) of 1998 and 2003. Thus, the goal of this study is to determine what was responsible for the varying human health response during the two heat events. A multivariate analysis is used to investigate the relationships between mortality and heat wave intensity, duration, and timing within the summer season, along with levels of air pollution. It was found that for heat waves in both summers, mortality was strongly associated with the duration of the heat wave. In addition, while slightly higher than average, the air pollution levels for the two heat waves were similar and cannot fully explain the observed differences in human mortality. Finally, since the meteorological conditions and pollution levels for the two heat waves were alike, we conclude that improvements in living conditions in Shanghai, such as increased use of air conditioning, larger living areas, and increased urban green space, along with higher levels of heat awareness and the implementation of a heat warning system, were responsible for the lower levels of human mortality in 2003 compared to 1998.

Aged↗
PubMed1996

Heat shock inhibits the hypoxia-induced effects on iodide uptake and signal transduction and enhances cell survival in rat thyroid FRTL-5 cells.

Chronic hypoxia inhibits rat thyroid function in vivo. To determine possible mechanisms, we studied the effect of hypoxia on iodide uptake, the involvement of second messengers, and cell membrane permeability in rat thyroid FRTL-5 cells. Since sublethal heat stress protects tissues from ischemia, we also determined effects of heat stress. The initial rate of iodide uptake in untreated cells was between 12.98 and 15.28 pmol/micrograms DNA/min. Hypoxia (5% O2) increased the rate of uptake in a time-dependent manner. Heating cells at 45 degrees C for 15 min (heat shock) prior to exposure to hypoxia for 3 days inhibited the increase in the initial rate of I-uptake. Using fura-2, we found that the resting [Ca2+]i in suspended FRTL-5 cells was 65 +/- 7 nM (n = 16). [Ca2+]i was not increased in cells exposed to hypoxia for 1 day, while a 3-day exposure increased [Ca2+]i by 43 +/- 4% (p < 0.05); no additional increase occurred after 7 days of exposure. When cells were heated prior to hypoxia exposure for 3 days, the hypoxia-induced increase in [Ca2+]i did not occur. Similar observations were found with inositol trisphosphates (InsP3). Exposure of cells to hypoxia for 3 days increased InsP3 from 0.08 +/- 0.02 (n = 5) to 0.32 +/- 0.04% total cpm (n = 5, p < 0.05), but sublethal heating of cells prior to hypoxia exposure prevented the increase. Three-day hypoxia increased PKC activity in the membrane fraction (from 67 +/- 7 to 86 +/- 4% of total activity, p < 0.05), and heat shock inhibited these changes also. Immunoblots showed that hypoxia treatment alone and heat shock plus hypoxia resulted in the translocation of PKC-alpha, -delta, -epsilon, and -zeta isoforms, whereas heat shock alone translocated only PKC-beta I, -beta II, and -zeta. Cell membrane integrity was assayed by trypan blue exclusion. Hypoxia alone for 3 days did not affect membrane permeability, but only 49 +/- 3% of cells excluded trypan blue when a 3-day hypoxia exposure was followed by a 6 h reoxygenation. Heat shock prior to hypoxia and reoxygenation protected cell membrane function. Heat shock also induced heat shock protein 70 kDa (HSP-70) synthesis at the transcriptional level. Results suggest that heat shock protects FRTL-5 cells from hypoxic injury, perhaps by inhibiting the initial rate of iodide uptake and second messengers. It is likely that HSP-70 plays an essential role in the process of protection.

Animals↗
PubMed2001

Heat-related mortality in selected United States cities, summer 1999.

As part of a public health response to severe heat waves in the midwestern and northeastern United States in the summer of 1999, the authors actively solicited the number of heat-related deaths from 38 medical examiner and coroner jurisdictions comprising 35 metropolitan areas to enumerate heat-related deaths in areas affected by heat waves. They also determined the usefulness of these data for surveillance and rapid investigation of heat-related deaths. A total of 334 heat-related deaths were reported during the study period of July 1 - August 31. Minor changes in data collection and diagnostic criteria in some medical examiner and coroner jurisdictions would allow for greater comparability among jurisdictions. The National Association of Medical Examiners' position paper on heat-related mortality diagnosis provides important guidance to medical examiners and coroners regarding the certification of heat-related deaths and may require some refinement to address certain issues. Among these are certifying manner of death and classifying potential causes of heat-related death not involving hyperthermia or heat stroke, but where heat is a potential contributing factor to death. Medical examiners and coroners are an important resource for heat-related mortality research, and improvements in data collection and reporting could yield tremendous benefits to our understanding of and interventions for heat-related deaths.

Cause of Death↗
PubMed1998

Improved free musculocutaneous flap survival with induction of heat shock protein.

The cellular response to a wide variety of stresses results in the synthesis of a family of stress response proteins termed heat shock proteins. Recent studies have demonstrated that heat shock proteins produced in response to an initial stress seem to protect against subsequent unrelated stresses. Importantly, hyperthermia-induced heat shock proteins provided protection from ischemia/reperfusion injury in several organ transplantation models. We hypothesized that free musculocutaneous flap survival could be improved by enhancing the flap's tolerance to relative ischemia by the prior induction of heat shock proteins. Accordingly, we determined the heat shock protein response in skin and muscle after systemic or local heating and examined the effect on free musculocutaneous flap survival in a rat model. Free musculocutaneous flaps incorporating thigh adductor muscles and a 2 x 6-cm2 skin paddle were transplanted to the ipsilateral groin in three groups of male Wistar rats. Systemically heated rats (n = 6) were anesthetized and incubated for 30 minutes at 42 degrees C 6 hours before free musculocutaneous tissue transfer. Locally heated rats (n = 6) were anesthetized, and their donor site anterior thigh was placed for 30 minutes on a heating block set at 44 degrees C 6 hours before free tissue transfer. Control rats (n = 5) did not have heating pretreatment but underwent identical anesthesia. Animals were sacrificed on postoperative day 3, at which time skin loss (cm2) and muscle viability, quantified by nitroblue tetrazolium staining time, were assessed in a blinded fashion. The skin and muscle from the free flap were analyzed for HSP72 mRNA and protein using quantitative Northern and Western blot techniques. All free musculocutaneous flaps were viable. However, the locally and systemically heated rats demonstrated a marked improvement of skin survival, which correlated with increased skin levels of HSP72. There were no differences in nitroblue tetrazolium muscle staining times or muscle levels of HSP72 among the three groups. These findings suggest that prior heat-induced heat shock proteins result in improvement in musculocutaneous flap survival, which may have direct clinical applications, especially in high-risk patients.

Animals↗
PubMed2006

Induction of heat shock proteins in a rat composite tissue allotransplantation model of acute rejection.

BACKGROUND: Clinical cases of composite tissue allotransplantation have been reported, but the exact mechanisms of allograft rejection remain unclear. The current study examined the possible involvement of heat shock proteins in major histocompatibility complex-compatible minor-mismatch composite tissue allotransplantation rejection. METHODS: Allotransplantation (Fisher 344 to Lewis) and isotransplantation (Lewis to Lewis) of rat lower extremities were performed. Temporal profiles of 70-kDa and 60-kDa heat shock proteins (heat shock protein 70 and heat shock protein 60) were conducted by quantitative Western blot analysis and immunohistochemistry. Analyses were performed immediately after reperfusion (day 0) and on postoperative days 1, 3, 7, and 12 (n = 5 for quantitative Western blot analysis and n = 5 for immunohistochemistry). RESULTS: The expression levels of the inducible forms of heat shock protein 70 and heat shock protein 60 were uniformly and significantly augmented until postoperative day 7 in the allografts, compared with the isografts (p < 0.001 for each protein). Immunoreactivities to heat shock protein 70 and heat shock protein 60 in keratinocytes, hair follicular cells, and endothelial cells of the subdermal vascular plexus were enhanced in the allografts early on postoperative day 1. Positive staining of hair follicles extended to deeper parts of the hair follicles and hair bulbs in the allografts on postoperative day 3. Although dendritic cells were positive for both heat shock protein 70 and heat shock protein 60, infiltrating lymphocytes were positive only for heat shock protein 60. CONCLUSIONS: These results suggest the possible involvement of heat shock proteins in the process of major histocompatibility complex-compatible minor-mismatch composite tissue allotransplantation rejection. Thus, modulation of the function of heat shock proteins might be an important therapeutic option for improving the outcome of minor-mismatch allografts.

Animals↗
PubMed1984

Starved Tetrahymena thermophila cells that are unable to mount an effective heat shock response selectively degrade their rRNA.

Tetrahymena thermophila cells that had been shifted from log growth to a non-nutrient medium (60 mM Tris) were unable, during the first few hours of starvation, to mount a successful heat shock response and were killed by what should normally have been a nonlethal heat shock. An examination of the protein synthetic response of these short-starved cells during heat shock revealed that whereas they were able to initiate the synthesis of heat shock proteins, it was at a much reduced rate relative to controls and they quickly lost all capacity to synthesize any proteins. Certain pretreatments of cells, including a prior heat shock, abolished the heat shock inviability of these starved cells. Also, if cells were transferred to 10 mM Tris rather than 60 mM Tris, they were not killed by the same heat treatment. We found no abnormalities in either heat shock or non-heat shock mRNA metabolism in starved cells unable to survive a sublethal heat shock when compared with the response of those cells which can survive such a treatment. However, selective rRNA degradation occurred in the nonsurviving cells during the heat shock and this presumably accounted for their inviability. A prior heat shock administered to growing cells not only immunized them against the lethality of a heat shock while starved, but also prevented rRNA degradation from occurring.

Animals↗
PubMed1997

ATP-sensitive potassium channel mediates delayed ischemic protection by heat stress in rabbit heart.

Heat shock protects against myocardial ischemia-reperfusion injury possibly via increased expression of heat shock proteins. The direct evidence of heat shock protein protection in vivo remains circumstantial, and no other new mechanism of protection has been proposed. Recent studies suggest that opening of ATP-sensitive K+ channels (KATP channels) plays an important role in ischemic preconditioning; however, it is not known whether this channel is also important in delayed protection conferred by heat shock. Anesthetized rabbits underwent heat shock treatment by raising core temperature to 42 degrees C for 15 min. Twenty-four hours later, the animals were reanesthetized and subjected to regional ischemia-reperfusion. The specific KATP channel blockers glibenclamide (0.3 mg/kg i.p.) and sodium 5-hydroxydecanoate (5HD; 5 mg/kg i.v.) were used to block the channel function. The drugs were administered at two different times, either pre-heat stress or preischemia. Infarct size was determined by triphenyltetrazolium chloride staining. The 72-kDa heat shock protein (HSP 72) was measured by Western blots. Our results show that heat shock produced a marked reduction in infarct size (39.4 +/- 8.1 to 14.3 +/- 2.5% of risk area, P < 0.05). Glibenclamide and 5HD completely abolished heat shock-induced reduction in infarct size (42.3 +/- 0.32 and 33.7 +/- 4.8%) when given before ischemia-reperfusion; however, these antagonists failed to block protection when administered before the onset of heat shock. Furthermore, the enhanced expression of HSP 72 in heat shock groups was not diminished by glibenclamide or 5HD, suggesting a lack of a direct role of this protein in conferring cardiac protection by heat shock. The complete blockade of cardiac protection by glibenclamide and 5HD strongly suggests that opening of this channel is a very important component of heat shock-induced ischemic protection in rabbit hearts.

Animals↗
PubMed2004

Heat stress induces a biphasic thermoregulatory response in mice.

Previous animal models of heat stress have been compromised by methodologies, such as restraint and anesthesia, that have confounded our understanding of the core temperature (T(c)) responses elicited by heat stress. Using biotelemetry, we developed a heat stress model to examine T(c) responses in conscious, unrestrained C57BL/6J male mice. Before heat stress, mice were acclimated for >4 wk to an ambient temperature (T(a)) of 25 degrees C. Mice were exposed to T(a) of 39.5 +/- 0.2 degrees C, in the absence of food and water, until they reached maximum T(c) of 42.4 (n = 11), 42.7 (n = 12), or 43.0 degrees C (n = 11), defined as mild, moderate, and extreme heat stress, respectively. Heat stress induced an approximately 13% body weight loss that did not differ by final group T(c); however, survival rate was affected by final T(c) (100% at 42.4 degrees C, 92% at 42.7 degrees C, and 46% at 43 degrees C). Hypothermia (T(c) < 34.5 degrees C) developed after heat stress, with the depth and duration of hypothermia significantly enhanced in the moderate and extreme compared with the mild group. Regardless of heat stress severity, every mouse that transitioned out of hypothermia (survivors only) developed a virtually identical elevation in T(c) the next day, but not night, compared with nonheated controls. To test the effect of the recovery T(a), a group of mice (n = 5) were acclimated for >4 wk and recovered at T(a) of 30 degrees C after moderate heat stress. Recovery at 30 degrees C resulted in 0% survival within approximately 2 h after cessation of heat stress. Using biotelemetry to monitor T(c) in the unrestrained mouse, we show that recovery from acute heat stress is associated with prolonged hypothermia followed by an elevation in daytime T(c) that is dependent on T(a). These thermoregulatory responses to heat stress are key biomarkers that may provide insight into heat stroke pathophysiology.

Acclimatization↗
PubMed1992

Distribution of the 72-kd heat-shock protein as a function of transient focal cerebral ischemia in rats.

BACKGROUND AND PURPOSE: The significance and physiological implications of the expression of the 72-kd heat-shock protein in ischemic tissue are unknown. To enhance our understanding of the relation between ischemic cell damage and 72-kd heat-shock protein expression, we evaluated the cellular expression and the anatomic distribution of 72-kd heat-shock protein in conjunction with the morphological analysis of rat brain, as a function of the duration of a single arterial occlusion. METHODS: Adult Wistar rats were subjected to graded transient middle cerebral artery occlusion (for a duration of 10, 20, 30, 60, 90, and 120 minutes and sham; n = 4 per group). Forty-eight hours after reopening the artery, brain tissue sections were analyzed to determine the extent of neuronal damage (hematoxylin and eosin staining), the extent of astrocytic reactivity (immunohistochemistry, using anti-glial fibrillary acidic protein), and the distribution of 72-kd heat-shock protein (immunohistochemistry, using a monoclonal antibody to 72-kd heat-shock protein). RESULTS: We found that 72-kd heat-shock protein was sequentially expressed in morphologically intact neurons, microglia, and endothelial cells with increasing duration of ischemia; 72-kd heat-shock protein immunoreactivity was not detected in astrocytes. The duration of ischemia required to evoke a 72-kd heat-shock protein response in neurons was dependent on the anatomic site and followed a pattern of increasing neuronal sensitivity to ischemic cell damage with duration of ischemia: 72-kd heat-shock protein and neuronal damage were sequentially detected in the caudate putamen, globus pallidus, cerebral cortex, amygdala, and hippocampus with increasing duration of ischemia. With ischemia of long duration (greater than or equal to 90 minutes), neurons expressing 72-kd heat-shock protein were localized to a zone peripheral to the severely damaged ischemic core. CONCLUSIONS: These studies suggest that 1) the expression of 72-kd heat-shock protein in neurons precedes the development of ischemic cellular alterations detectable by conventional hematoxylin and eosin light microscopy methods; 2) there is a hierarchy of cell types and anatomic sites that express 72-kd heat-shock protein, and this hierarchy reflects cellular and anatomic vulnerability to ischemic cell damage; and 3) 72-kd heat-shock protein induction in neurons bordering a necrotic ischemic core may be the morphological equivalent of the ischemic penumbra.

Animals↗
PubMed2005

Epidemiology of hospitalizations and deaths from heat illness in soldiers.

PURPOSE: Serious heat illness has received considerable recent attention due to catastrophic heat waves in the United States and Europe, the deaths of high-profile athletes, and military deployments. METHODS: This study documents heat illness hospitalizations and deaths for the U.S. Army from 1980 through 2002. Hospitalization data were obtained from the Total Army Injury Health Outcomes Database (TAIHOD) coded according to the International Classification of Diseases, Ninth Revision, Clinical Modification (ICD-9-CM). North Atlantic Treaty Organization Standardization Agreement codes were searched for heat injuries in an effort to detect cases that were not found during the ICD-9-CM search. RESULTS: Five-thousand two-hundred forty-six soldiers were hospitalized, and 37 died due to heat illness. Our results indicate: 1) approximately 60% reduction in hospitalization rates (fewer heat exhaustion cases) over the 22-yr period; 2) fivefold increase in heat stroke hospitalization rates (1.8 per 100,000 in 1980 to 14.5 per 100,000 in 2001); 3) heat stroke cases were associated with dehydration (17%), rhabdomyolysis (25%), and acute renal failure (13%); 4) lower hospitalizations rates among African and Hispanic Americans compared with Caucasians (incidence density ratio, 0.76 [95% confidence interval, 0.71-0.82]; 5) greater rates of hospitalizations and heat strokes among recruits from northern than southern states (incidence density ratio, 1.69 [95% confidence interval, 1.42-1.90]; and 6) greater rates of hospitalizations and heat strokes among women than men (incidence density ratio, 1.18 [95% confidence interval, 1.09-1.27]). CONCLUSIONS: Exertional heat illness continues to be a military problem during training and operations. Whereas the hospitalization rate of heat illness is declining, heat stroke has markedly increased.

Adolescent↗
PubMed2005

Estimates of heat stress relief needs for Holstein dairy cows.

Estimates of environmental heat stress are required for heat stress relief measures in cattle. Heat stress is commonly assessed by the temperature-humidity index (THI), the sum of dry and wet bulb temperatures. The THI does not include an interaction between temperature and humidity, although evaporative heat loss increases with rising air temperature. Coat, air velocity, and radiation effects also are not accounted for in the THI. The Holstein dairy cow is the primary target of heat stress relief, followed by feedlot cattle. Heat stress may be estimated for a variety of conditions by thermal balance models. The models consist of animal-specific data (BW, metabolic heat production, tissue and coat insulation, skin water loss, coat depth, and minimal and maximal tidal volumes) and of general heat exchange equations. A thermal balance simulation model was modified to adapt it for Holstein cows by using Holstein data for the animal characteristics in the model, and was validated by comparing its outputs to experimental data. Model outputs include radiant, convective, skin evaporative, respiratory heat loss and rate of change of body temperature. Effects of milk production (35 and 45 kg/d), hair coat depth (3 and 6 mm), air temperature (20 to 45 degrees C), air velocity (0.2 to 2.0 m/s), air humidity (0.8 to 3.9 kPa), and exposed body surface (100, 75, and 50%) on thermal balance outputs were examined. Environmental conditions at which respiratory heat loss attained approximately 50% of its maximal value were defined as thresholds for intermediate heat stress. Air velocity increased and humidity significantly decreased threshold temperatures, particularly at higher coat depth. The effect of air velocity was amplified at high humidity. Increasing milk production from 35 to 45 kg/d decreased threshold temperature by 5 degrees C. In the lying cow, the lower air velocity in the proximity of body surface and the smaller exposed surface markedly decrease threshold temperature. The large variation in thresholds due to environmental and animal factors justifies the use of thermal balance-based indices for estimating heat stress. Such an approach may make possible estimates of threshold temperatures at which heat stress relief is required for widely different cattle types and environmental situations.

Animals↗
PubMed1996

Comparative study of antigen retrieval heating methods: microwave, microwave and pressure cooker, autoclave, and steamer.

We present a study comparing the most popular heating methods currently used for antigen retrieval (AR) immunostaining: the microwave oven, microwave with pressure cooker, autoclave, and steamer heating. A panel of 21 antibodies was tested on formalin fixed, paraffin embedded sections using these heating methods and Tris-HC1 buffer, pH 9.5, plus 5% urea as the AR solution. Three observers independently evaluated the intensity of AR immunostaining. All heating methods yielded good results for AR immunostaining. There were only minor differences among the heating methods for AR when the optimal concentration of primary antibody for normal immunostaining was used; however, background staining may occasionally be troublesome if antibodies are not retitrated and diluted further for use on tissues after AR. Significant differences were observed only after further dilution of the primary antibodies: the microwave pressure cooker, extended microwave heating (5 min x 4) and autoclave heating then showed a similar intensity of staining that was stronger than results obtained with the steamer (20 min) or regular microwave heating (5 min x 2). Extension of the steamer heating time, however, yielded equivalent results. This study indicates that different heating methods can yield similar intensities of AR immunostaining if the heating times are adjusted appropriately. It is noteworthy that, in general, the adjusted conditions for maximal retrieval differ from those most widely cited in the literature, or recommended by manufacturers. That several heating devices may provide similar results permits the use of different AR heating methods according to the equipment available. This study also is an early step in standardizing the AR immunostaining protocol by providing uniform conditions for "maximal retrieval" as a common end point for all laboratories.

Antigens↗
PubMed1999

N(omega)-nitro-L-arginine decreases resting cytosolic [Ca2+] and enhances heat stress-induced increase in cytosolic [Ca2+] in human colon carcinoma T84 cells.

N(omega)-nitro-L-arginine (LNNA) inhibits the synthesis of heat shock proteins in animals and cultured cells exposed to heat stress. Heat shock protein synthesis is known to be Ca2+-dependent. In this study, we have characterized the effect of LNNA on [Ca2+]i before and after heat stress in human colon carcinoma T84 cells. In untreated cells incubated in the presence of external Ca2+, the resting [Ca2+]i was 201+/-3 nM. If these cells were exposed to 45 degrees C for 10 min, [Ca2+]i increased by 50+/-2%. Preincubation with LNNA (100 microM) without subsequent heating led to a decrease in [Ca2+]i in a LNNA concentration-dependent manner. Preincubation with LNNA followed by heating increased [Ca2+]i to levels 88+/-5% greater than cells heated without LNNA pretreatment. Incubating cells in medium without external Ca2+ (no heating, no LNNA treatment) lowered resting [Ca2+]i to 115+/-2 nM and greatly reduced the increase in [Ca2+]i observed if cells were heated in the presence of Ca2+, indicating that external Ca2+ plays an important role in the maintenance of [Ca2+]i in T84 cells. With external Ca2+ absent, LNNA pretreatment further reduced [Ca2+]i in unheated cells, and heating failed to enhance [Ca2+]i. We determined (with external Ca2+ present) that the heat-stress induced increase in [Ca2+]i in T84 cells was blocked by dichlorobenzamil, a Na+/Ca2+ exchanger inhibitor, suggesting that the exchanger mediates Ca2+ entry. The median inhibitory concentration (IC50) in cells not treated with LNNA was 0.970+/-0.028 microM. With LNNA pretreatment, the IC50 was 5.099+/-0.107 microM. Heat stress of T84 cells did not affect the binding affinity of the Na+/Ca2+ exchanger for external Ca2+, but it increased the maximal velocity of the exchanger. In unheated cells, preincubation with LNNA decreased the binding affinity of the exchanger for Ca2+, but after heat treatment, both the binding affinity and maximal velocity of the exchanger increased. Our data are consistent with the idea that LNNA affects the activity of the Na+/Ca2+ exchanger. We also determined there are intracellular Ca2+ pools in T84 cells sensitive to thapsigargin, monensin, and ionomycin. Treatment with TMB-8, a blocker of Ca2+ sequestration and mobilization, or ionomycin inhibited the LNNA-induced decrease in [Ca2+]i observed in the absence of external Ca2+, suggesting that LNNA promotes Ca2+ sequestration.

Amiloride↗