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PubMed1999

Heat shock-induced necrosis and apoptosis in osteoblasts.

Damage to bone tissue due to heat shock is one of the main causes of the failure of osseointegration at the bone-implant interface. To investigate the effect of heat shock on regeneration of bone tissue, osteoblasts were exposed to heat shock for 10 minutes at 42, 45, or 48 degrees C or kept at 37 degrees C as a control. After 10 minutes of heat shock, disruption of actin filaments was seen in the cells and the degree of disruption increased with the temperature. The cytoskeleton reassembled after a 12-hour incubation at 37 degrees C in the cells treated at 42 or 45 degrees C, but this reversible recovery did not occur in the cells treated at 48 degrees C. Flow cytometric analysis showed that heat shock at 48 degrees C increased the number of necrotic cells to 15-20% within minutes (p < 0.05 compared with 37 degrees C). Apoptosis, evidenced by annexin V staining, DNA laddering, and caspase 3 activation, started after 6-8 hours of incubation, reached a peak at 12 hours, and gradually declined (p<0.05). Pretreatment with the antioxidant N-acetyl-L-cysteine reduced the necrosis induced at 48 degrees C of heat shock by one-half (p<0.05) but had no significant effect on caspase 3 activation induced by heat shock, suggesting that reactive oxygen species were critical in heat shock-induced necrosis but not in apoptosis. Heat shock at 48 degrees C induced a sustained translocation of p53 into the nucleus and a sustained activation of c-jun N-terminal kinase, whereas that at 42 and 45 degrees C induced only transient p53 translocation and c-jun N-terminal kinase activation. These results suggest that the sustained activation of p53 and c-jun N-terminal kinase pathways may contribute to heat shock-induced apoptosis. On the other hand, heat shock protein 70 increased dramatically in the cells treated at 45 or 48 degrees C, suggesting that the protecting mechanism in the cells was also activated. Such protection was able to prevent apoptosis in cells treated at 45 degrees C but not in those treated at 48 degrees C.

Actins↗
PubMed1989

Regulation of the inducible heat shock 71 genes in early neural development of cultured rat embryos.

Activation of the inducible heat shock 71 genes and their role in the heat shock response was studied in vitro in 9.5 day-old rat embryos at neural tube closure. The transcriptional response of a 71 kilodalton (kD) heat shock gene induced after various regimes of heat shock and acquired thermotolerance was investigated. Expression and accumulation of the heat shock (hs) 71 mRNA in the neuroectoderm was studied by Northern and dot blot analysis. Specific expression in various cell types and regions of the neuroectoderm were examined by in situ hybridization. Exposure of embryos to a heat shock at 43 degrees C for 7.5 min caused high levels of hs mRNA 71 accumulation in the neuroectoderm, pronounced protein synthesis inhibition, and regulated recovery. Specific neuroectoderm cell death followed, resulting in major developmental defects of the eye and forebrain region. A mild heat shock of 42 degrees C for 10 min induced the heat shock response, hsp synthesis, and cell recovery, but produced no cell death or deformities. Preheating the embryo at 42 degrees C resulted in acquired thermotolerance to an otherwise teratogenic 43 degrees C heat shock. Thermotolerance was associated with a rapid recovery of protein synthesis associated with hs 71 mRNA expression. Dot blot analysis showed that after a 42 degrees C heat shock, 71 mRNA was rapidly transcribed and transported into the cytoplasm where it was degraded within 2 hr of the initial response. The results suggest that the heat shock protein (hsp) 71 gene may have a protective rather than a rescuing function.

Animals↗
PubMed1996

Determination of body heat storage: how to select the weighting of rectal and skin temperatures for clothed subjects.

Two methods of estimating body heat storage were compared under differing conditions of clothing and acclimation to heat. Sixteen male subjects underwent 6 consecutive days or two 6-day periods, separated by a 1-day rest period of heat acclimation, exercising 60 min.day-1 at 45%-55% of maximal aerobic power in a hot, dry environment (dry bulb temperature 40 degrees C; relative humidity 30%; and wind speed 0.3 m.s-1). Before and after acclimation, the subjects entered the same environment, wearing either normal light combat clothing or clothing protective against nuclear, biological, and chemical agents; they walked on a treadmill at 1.34 m.s-1, 0% slope continuously (n = 11 for normal clothing) or as repeated 15-min bouts of exercise followed by 15-min sitting rest (n = 5 for normal clothing and n = 16 for protective clothing). Average exposure times were 147 min (preacclimation) and 150 min (postacclimation) for continuous exercise and 150 min (both pre- and postacclimation) for intermittent exercise while wearing normal clothing, and 103 min (preacclimation) and 116 min (postacclimation) for intermittent exercise while wearing protective clothing. Heat storage was determined calorimetrically (from heat gains and heat losses) and thermometrically [using various weightings of rectal temperature (Tre) and mean skin temperature (Tsk)]. There were only minor (<5%) differences in estimated heat storage, whether calculations used a single specific heat (3.47 kJ.kg-1.degree C-1) or a value computed according to the subject's body composition. When wearing normal clothing, a formula with an invariant relative weighting for Tre to Tsk of 4:1 provided the best thermometric estimate of heat storage. When wearing protective clothing, the invariant relative weighting of 4:1 underestimated heat storage by 2%-12%; underestimation was attenuated by using respective relative weightings for a thermoneutral and hot environment of 2:1 and 2:1 or 4:1 and 9:1 before acclimation and 4:1 and 9:1 after acclimation. We conclude that the accuracy of thermometric estimates of heat storage can be improved by modifying the weighting factors according to environment, acclimation, and type of clothing.

Adult↗
PubMed1998

Relevance of individual characteristics for human heat stress response is dependent on exercise intensity and climate type.

Multiple heterogeneous groups of subjects (both sexes and a wide range of maximal oxygen uptake VO2max, body mass, body surface area (AD),% body fat, and AD/mass coefficient) exercised on a cycle ergometer at a relative (%VO2max, REL) or an absolute (60 W) exercise intensity in a cool (CO 21 degrees C, 50% relative humidity), warm humid (WH 35 degrees C, 80%) and a hot dry (HD 45 degrees C, 20%) environment. Rectal temperature (Tre) responses were analysed for the influence of the individual's characteristics, environment and exercise intensity. Exposures consisted of 30-min rest, followed by 60-min exercise. The Tre was negatively correlated with mass in all conditions. Body mass acted as a passive heat sink in all the conditions tested. While negatively correlated with VO2max and VO2max per kilogram body mass in most climates, Tre was positively correlated with VO2max and VO2max per kilogram body mass in the WH/REL condition. Thus, when evaporative heat loss was limited as in WH, the higher heat production of the fitter subjects in the REL trials determined Tre and not the greater efficiency for heat loss associated with high VO2max. Body fatness significantly affected Tre only in the CO condition, where, with low skin blood flows (measured as increases in forearm blood flow), the insulative effect of fat was pronounced. In the warmer environments, high skin blood flows offset the resistance offered by peripheral adipose tissue. Contrary to other studies, Tre was positively correlated with AD/mass coefficient for all conditions tested. For both exercise types used, being big (a high heat loss area and heat capacity) was apparently more beneficial from a heat strain standpoint than having a favourable AD/mass coefficient (high in small subjects). The total amount of variance in Tre responses which could be attributed to individual characteristics was dependent on the climate and the type of exercise. Though substantial for absolute exercise intensities (52%-58%) the variance explained in Tre differed markedly for relative intensities: 72% for the WH climate with its limited evaporative capacity, and only 10%-26% for the HD and CO climates. The results showed that individual characteristics play a significant role in determining the responses of body core temperature in all conditions tested, but their contribution was low for relative exercise intensities when evaporative heat loss was not restricted. This study demonstrated that effects of individual characteristics on human responses to heat stress cannot be interpreted without taking into consideration both the heat transfer properties of the environment and the metabolic heat production resulting from the exercise type and intensity chosen. Their impact varies substantially among conditions.

Adipose Tissue↗
PubMed2005

Analyses of thermoregulatory responses of feeder cattle exposed to simulated heat waves.

Heat stress in feedlot cattle causes reduced performance, and in the most severe cases, death of the animals, thus causing the loss of millions of dollars in revenue to the cattle industry. A study was designed to evaluate dynamics of thermoregulation and feeding activities when feeder cattle were exposed to simulated heat waves, in comparison with repeated sinusoidal hot and thermoneutral environments. Nine beef steers were randomly assigned to an individual pen in one of three environmental chambers. Each chamber was subjected to each of three temperature regimes (heatwave simulation from Rockport, Mo., 1995, heatwave simulation from Columbia, Mo., 1999, and Controlled heat stress treatment of 32+/-7 degrees C) for a period of 18 days, according to a Latin square treatment design, with a 10-day thermoneutral period (18+/-7 degrees C) separating treatment periods. Respiration rate, core body temperature, heat production, feed intake, and feeding behavior were measured on each animal for the duration of the experiment. Differences were found in all treatments for all parameters except feeding behavior. It was shown that the two simulated heat waves elicited very different thermoregulatory responses. Based on these results the heat wave centered at Rockport, Mo. in 1995 was devastating because the animals were not acclimated to hot conditions, thus causing an acute response to heat stress. The responses of cattle to conditions at Columbia, Mo. showed some acclimation to heat prior to the peak stress days, and therefore a dampened response was seen. It appears the extreme conditions at Columbia, Mo., 1999 were made severe by environmental conditions not simulated during this study (low wind speed and intensive solar radiation). Overall, it was determined while a cyclic heat stress treatment is a representative model to test heat stress in cattle, further heat stress experiments should be conducted in an actual feedlot.

Adaptation, Physiological↗
PubMed2000

Heat-stress-related mortality in five cities in Southern Ontario: 1980-1996.

The Toronto-Windsor corridor of Southern Ontario, Canada, experiences hot and humid weather conditions in summer, thus exposing the population to heat stress and a greater risk of mortality. In the event of a climate change, heat-stress conditions may become more frequent and severe in Southern Ontario. To assess the impact of summer weather on health, we analyzed heat-related mortality in the elderly (older than 64 years) in the metropolitan areas of Windsor, London, Kitchener-Waterloo-Cambridge, Hamilton, and Toronto for a 17-year period. Demographic, socioeconomic, and housing factors were also evaluated to assess their effect on the potential of the population to adapt and their vulnerability to heat stress. Heat-stress days were defined as those with an apparent temperature (heat index) above 32 degrees C. Mortality among the elderly was significantly higher on heat-stress days than on non-heat-stress days in all cities except Windsor. The strongest relationships occurred in Toronto and London, followed by Hamilton. Cities with the greatest heat-related mortality have relatively high levels of urbanization and high costs of living. Even without the warming induced by a climate change, (1) vulnerability is likely to increase as the population ages, and (2) ongoing urban development and sprawl are expected to intensify heat-stress conditions in Southern Ontario. Actions should be taken to reduce vulnerability to heat stress conditions, and to develop a comprehensive hot weather watch/warning system for the region.

Aged↗
PubMed1987

Cellular localization of HSP23 during Drosophila development and following subsequent heat shock.

The low-molecular-weight heat-shock protein HSP23 is synthesized in the absence of heat shock during Drosophila development. Here, I present a quantitative analysis of this phenomenon and describe the cellular localization of this protein during normal development and after a subsequent heat shock. HSP23 is first detected in the late third instar larvae and continues to accumulate reaching a maximum level in late pupae. In a 1-week-old adult, HSP23 can no longer be detected. Following lysis of whole pupae, HSP23 is found in the soluble lysate fraction in a form which sediments between 10 and 20 S. Exposure of larvae, pupae, and the adult fly to heat stress (37 degrees C) results in an increased amount of HSP23 which, however, is recovered in an insoluble particulate form following insect lysis. During recovery from heat shock, HSP23 is again found in the soluble 10- to 20-S lysate fraction. In pupae which are exposed to a severe heat stress (41 degrees C) HSP23 remains in the pellet fraction after the heat stress and no pupae are able to emerge as adult flies. However, when pupae are first exposed to a mild heat-shock treatment prior to the 41 degrees C stress, the thermotolerance process is induced and HSP23 is again rapidly found in the soluble lysate fraction during the recovery from heat shock. These observations suggest a possible correlation between the survival of pupae after heat shock and the recovery of HSP23 in the soluble lysate fraction as 10- to 20-S structures after the heat shock.

Animals↗
PubMed1991

Binding activity of glucocorticoid receptors after heat shock.

The response of glucocorticoid receptors (GR) to heat was measured by the change in ligand binding activity both in control cells and in cells made tolerant to heat by a prior mild heat exposure. The study was prompted by earlier data showing that one of the heat shock proteins (HSP90) is an essential component of the GR complex and that treatment of mammalian cells with hydrocortisone induces resistance to heat damage. The GR rapidly loses binding activity after commencement of heating. There is a 50% loss of activity after 4 min at 45 degrees C, 8 min at 44 degrees C, or 17 min at 43 degrees C. The reduction in binding is due mainly to a reduction in affinity of binding to the ligand. The ability to bind glucocorticoid recovers quickly after heat treatment. Activity returns to levels 60-80% of normal by 2 h after a heat treatment that initially reduces binding to less than 20% of normal. However, complete restoration of binding activity takes approximately 3 days. The recovery of binding activity does not require protein synthesis. Pretreatment of cells with hydrocortisone, using conditions that induce heat resistance, reduces the activity to 10-20% of control, but residual receptors display a heat sensitivity similar to that of control cells. There was evidence for a limited degree of protection of GR from heat damage in thermotolerant cells.

Animals↗
PubMed1987

Asymmetric segregation of heat-shock proteins upon cell division in Caulobacter crescentus.

Three Caulobacter crescentus heat-shock proteins were shown to be immunologically related to the Escherichia coli heat-shock proteins GroEL, Lon and DnaK. A fourth heat-shock protein was detected with antibody to the C. crescentus RNA polymerase. This 37,000 Mr heat-shock protein might be related to the E. coli 32,000 Mr heat-shock sigma subunit. The synthesis of the major C. crescentus RNA polymerase sigma factor was not induced by heat shock. The E. coli GroEL protein and the related protein from C. crescentus were also induced by treatment with hydrogen peroxide. Like some of the proteins in the heat-shock protein families of Drosophila and yeast, the four heat-shock proteins in C. crescentus were found to be regulated developmentally under normal conditions. All four proteins were synthesized in the predivisional cell, but the progeny showed cell type-specific bias in the level of enhanced synthesis after heat shock. The 92,000 Mr Lon homolog and the 37,000 Mr RNA polymerase subunit were preferentially synthesized in the stalked cell, whereas the synthesis of the 62,000 Mr GroEL homolog was enhanced in the progeny swarmer cell. Furthermore, the four heat-shock proteins synthesized in the predivisional cell were partitioned in a specific manner upon cell division. The stalked cell, which initiates chromosome replication immediately upon division, received the Lon homolog, the DnaK homolog and the 37,000 Mr RNA polymerase subunit. The GroEL homolog, however, was distributed equally to both the stalked cell and the swarmer cell. These results provide access to the functions of C. crescentus heat-shock proteins under both normal and stress conditions. They also allow an investigation of the regulatory signals that modulate the asymmetric distribution of proteins and their subsequent cell type-specific expression in the initial stages of a developmental program.

Autoradiography↗
PubMed1992

Characterization of the major 68 kDa heat shock protein in a rat transformed astroglial cell line.

The heat shock response in a transformed astrocyte line was compared with nontransformed astrocytes. The synthesis of HSP 68, the major inducible heat shock protein (HSP 68) was induced by a non-lethal 45 degrees C, 10 min heat shock. Although the incorporation of [35S]methionine into HSP 68 suggested that similar amounts of protein were being synthesized after heat shock, Western immunoblotting demonstrated striking differences in the HSP immunostaining between the two cell types. By one- and 'two-dimensional gel electrophoresis the major 68 kDa heat shock protein (HSP 68) was similar in both cell types. However, HSP 68 from heat shocked, transformed astrocytes did not immunostain with the monoclonal antibody, C-92, which is specific for the major inducible heat shock protein of HeLa cells. In contrast HSP 68 from heat shocked, nontransformed astrocytes immunostained quite well. A polyclonal antibody raised against the inducible 72 kDa heat shock protein of HeLa cells immunostained the HSP 68 from both astrocytes and transformed astrocytes. Analysis of the mRNA from the two cell types after heat shock revealed two bands of approximately 2.5 and 2.8 kb in astrocytes but only a single 2.5 kb band in the heat shocked transformed astroglia. These results suggest that structural differences in the HSP 68 may be present in the transformed astrocytes compared to the normal astrocytes.

Animals↗
PubMed2006

Extracellular 70-kd heat shock protein in mid-trimester amniotic fluid and its effect on cytokine production by ex vivo-cultured amniotic fluid cells.

OBJECTIVE: The 70-kd heat shock protein is released from cells in response to stress and functions as a regulator of innate immunity. We hypothesized that 70-kd heat shock protein in mid-trimester amniotic fluid might regulate local immune system activation. STUDY DESIGN: Amniotic fluid that was obtained from 200 women who underwent amniocentesis at 15 to 19 weeks of gestation was tested by enzyme-linked immunosorbent assay for 70-kd heat shock protein, tumor necrosis factor-alpha, and interleukin-1beta and -6. The amniotic fluid cellular fraction also was evaluated for Mycoplasma hominis by gene amplification. Whole amniotic fluids were incubated ex vivo in medium alone or medium that contained peptidoglycan, a TLR2 ligand, or lipopolysaccharide, a TLR4 ligand. After 24 hours, the supernatants were collected and assayed for 70-kd heat shock protein. The influence of exogenous 70-kd heat shock protein on tumor necrosis factor-alpha and interleukin-1beta and -6 production by whole amniotic fluid was assessed similarly. RESULTS: The 70-kd heat shock protein was detected in all amniotic fluids with a median (range) of 11.5 ng/mL (1.2-76.7). The intra-amniotic 70-kd heat shock protein concentration was correlated positively only with amniotic fluid tumor necrosis factor-alpha levels (P = .0002). Detection of M hominis was associated with an increased 70-kd heat shock protein concentration (median, 17.2 ng/mL; P = .01). The addition of peptidoglycan resulted in a stimulation of 70-kd heat shock protein production, and exogenous 70-kd heat shock protein stimulated the release of tumor necrosis factor-alpha by amniotic fluid cells. CONCLUSION: The 70-kd heat shock protein is released from cells in mid-trimester amniotic fluid as a consequence of TLR2 stimulation and potentiates tumor necrosis factor-alpha production.

Amniotic Fluid↗
PubMed2004

Heat stress decreases pulmonary MCP-1 production in endotoxemia.

An exaggerated pro-inflammatory response in endotoxemia may lead to multiple organ damage including acute lung injury. Heat stress prior to endotoxemia results in attenuation of inflammation possibly by decreasing cytokine production. Monocyte chemoattractant protein (MCP)-1, a pro-inflammatory cytokine, is responsible for monocyte recruitment into the lung in acute lung injury. The objective of this study is to determine if pretreatment with heat results in decreased MCP-1 production in the lungs of endotoxemic rats at a transcriptional or post-transcriptional level. Rats were assigned to one of four groups: control, heat alone, heat with or without endotoxin. Rats were made endotoxemic by injection of Escherichia coli lipopolysaccharide. MCP-1 was measured in lavage fluid and MCP-1 mRNA in the lung tissue. Endotoxemia resulted in production of MCP-1. Control and heat alone rats had 21+/-4 vs. 20+/-3 pg/ml, p=0.75. MCP-1 concentration was decreased in the lavage fluid of pre-heated when compared to non-heated endotoxemic rats (37+/-28 vs. 70+/-35 pg/ml, p <0.02 ). However, the MCP-1 mRNA was higher in the heated compared to non-heated endotoxemic rats (1.59+/-0.35 vs. 0.74+/-0.51, MCP-1/beta-actin mRNA, p <0.01). Control and heat alone rats had undetectable mRNA MCP-1 in the lungs. Heat stress prior to endotoxemia results in decreased production of MCP-1 by a post-transcriptional mechanism.

Animals↗
PubMed2005

Effects of heating rate, temperature and iron catalysis on the thermal behaviour and decomposition of 2-nitrobenzoyl chloride.

Runaway reactions arising from the decomposition of thermally unstable materials are a concern in industry due to the potentially devastating effects that they yield. Studies into the occurrence of thermal runaway incidents have shown the most likely cause to be a result of an inadequate investigation of the process prior to its operation on a large-scale. The chlorination of ortho-nitrated carboxylic acids is an industrially important reaction in the fine and agrochemical industries. The products of these reactions, ortho-nitrated acid chlorides, have been involved in runaway incidents that have resulted in violent explosions; hence, their thermal stability must be studied. Previous studies [S.D. Lever, M. Papadaki, Study of condition-dependent decomposition reactions: the thermal behaviour and decomposition of 2-nitrobenzoyl chloride, Part I, J. Hazard. Mater. 115 (2004) 91-100] showed that the decomposition of the parent molecule, 2-nitrobenzoyl chloride, is highly condition-dependent with the sample heating rate and temperature of decomposition playing a preponderant role in the course of the decomposition. Here, we present the results of studies of the decomposition of 2-nitrobenzoyl chloride, when the sample is subjected to various heating treatments, temperatures and in the presence of iron. As the temperature of decomposition was increased from 150 to 162 degrees C, the heat of decomposition was reduced from -215 to -90 kJ/mol. As the heat up rate applied in bringing the sample to the decomposition temperature increased, the heat of decomposition also increased. An increase in the heat up rate from 2 to 7.5 degrees C/min resulted in an increase in the heat of decomposition from -90 to -215 kJ/mol. The presence of iron and silver was observed to lower the heat of decomposition from -185 to -160 and -110 kJ/mol, respectively. Under most conditions investigated, the temperature at which gas flow was initiated was 147-150 degrees C. The presence of iron reduced this temperature to 140 degrees C. Decomposition was observed to take place over two stages, where the sample was heated directly from 40 degrees C at the required heat up rate. Where the sample was heated in stages and where calibrations had been carried out preceding decomposition, the decomposition took place in one stage alone.

Benzoates↗
PubMed1986

Induction of heat-shock proteins in the embryonic chicken lens.

The 11-day embryonic chicken lens displays a rapid and vigorous response to a heat shock. Exposure of the lens to elevated temperature (45 degrees C) dramatically increased the synthesis of three proteins with subunit molecular weights of 89,000, 70,000 and 24,000. These lens heat-shock proteins are identical to the heat-shock proteins of cultured chicken embryo fibroblasts in electrophoretic mobility and immunological cross-reactivity. Maximum induction of lens heat-shock protein synthesis occurred upon incubation at 45 degrees C for about 1-1.5 hr and was blocked in the presence of actinomycin D. The functional half-lives at 37 degrees C of the mRNAs encoding the lens heat-shock proteins were about 3-5 hr. Synthesis of normal lens proteins continued throughout the heat shock, but delta-crystallin was unusual in that its synthesis initially rose upon heat shock, a behavior similar to that of a heat-shock protein. Proteins which co-migrated with each of the major lens heat-shock proteins were detected immunologically in non-stressed lens extracts. The endogenous lens protein, p24, which cross-reacted with antibodies raised against the small heat-shock protein (hsp 24) from chicken-embryo fibroblasts and co-migrated in one dimensional SDS gels with a major beta-crystallin was shown to be structurally similar to the chicken small heat shock protein but was distinct from the beta-crystallins.

Acetates↗
PubMed1999

Dinitrosyl iron complexes with thiol-containing ligands and S-nitroso-D,L-penicillamine as inductors of heat shock protein synthesis in H35 hepatoma cells.

The concentration-dependent effect of various nitric oxide donors on synthesis of different heat shock proteins was evaluated in Reuber H35 hepatoma cells and their heat shock protein-inducing ability was compared with the effect of a heat shock. A 6 h incubation of H35 cells with the dimeric (diamagnetic) form of dinitrosyl iron complex with glutathione or N-acetyl-L-cysteine activated synthesis of various heat shock proteins, heat shock protein 28, 32, 60, 70, 90 and 100. Synthesis of these proteins was evaluated by [35S]methionine and [35S]cysteine labelling with subsequent separation of proteins by polyacrylamide gel electrophoresis. The dinitrosyl iron complex with glutathione appeared to be the most efficient inductor of heat shock protein synthesis and initiated the synthesis of heat shock protein 28 even more efficiently than a 30 min heating of cells. In the same experiments, S-nitroso-D,L-penicillamine exerted a considerably lesser effect on the synthesis of heat shock proteins. It was suggested that the active moiety of dinitrosyl iron complexes as inductors of heat shock protein synthesis is represented by their Fe+(NO+)2 groups which move to thiol groups of the proteins participating in the initiation of heat shock protein synthesis.

Acetylcysteine↗
PubMed2001

Decreased expression of the heat shock protein hsp70-2 is associated with the pathogenesis of male infertility.

OBJECTIVE: To examine the expression of the heat shock protein hsp70-2, and the possible relationship with the pathogenesis of male infertility. DESIGN: Prospective study. SETTING: Reproductive testing laboratory in a university hospital. PATIENT(S): Men undergoing testicular biopsy during an investigation of subfertility. INTERVENTION(S): Testicular tissues were obtained from biopsies of men undergoing infertility evaluation and subdivided into three groups: normal testes, maturational arrest and Sertoli cell-only syndrome. Immunostaining and Western blotting techniques determined expression of the heat shock protein hsp70-2 MAIN OUTCOME MEASURE(S): Expression of the heat shock protein hsp70-2 in the testes. RESULT(S): The experimental data demonstrated that the heat shock protein hsp70-2 was expressed in the normal and maturation arrest testicular specimens. The heat shock protein hsp70-2 was strongly present in the cytoplasm of spermatocytes and spermatides in the adluminal compartment of the seminiferous epithelium in normal testis. However, maturation arrest testis tissue demonstrated light staining in spermatocytes and spermatides, and Sertoli-only specimens demonstrated no staining for the heat shock protein hsp70-2. The Western blotting data showed a 70-kDa heat shock protein in the normal and maturation arrest testicular tissues, but not in the Sertoli-only tissues. CONCLUSIONS: These results suggest that the heat shock protein hsp70-2 is expressed in spermatocytes and spermatides in normal and maturation arrest tissues. However, the expression of the heat shock protein hsp70-2 was low in maturation arrest, and no heat shock protein hsp70-2 was demonstrated in Sertoli-only specimens. Therefore the decreased expression of the heat shock protein hsp70-2 is associated with the pathogenesis of male infertility.

Adult↗
PubMed2003

Cell death induced by down-regulation of heat shock protein 70 in lung cancer cell lines is p53-independent and does not require DNA cleavage.

OBJECTIVE: The inducible form of heat shock protein 70 is known to be overexpressed in tumors and seems to be necessary for the survival of tumor cells via an unknown mechanism. We therefore evaluated whether selective depletion of heat shock protein 70 induces cell death in lung cancer cells. METHODS: An adenovirus expressing antisense heat shock protein 70 and an adenovirus with beta-galactosidase were used for transduction of the lung cancer cell lines A549, NCI-H358, LXF-289, LOU-NH91, normal human bronchial epithelial cells, and normal lung fibroblasts IMR90. Cell death was determined by morphology, propidium iodide uptake, and trypan blue staining; DNA cleavage was assessed by terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling. Expression of heat shock protein 70, heat shock cognate 70, and phosphorylated p53 was determined by Western blot analysis. RESULTS: Transduction of lung cancer cells with adenovirus expressing antisense heat shock protein 70 but not with adenovirus with beta-galactosidase resulted in extensive cell death after 96 hours (A549: 53.2 +/- 9.44% versus 12.9 +/- 6.6%; NCI-H358: 48.4 +/- 7.2% versus 25.2 +/- 1.4%; LXF-289: 58.8 +/- 6.5% versus 24.7 +/- 5.4%; LOU-NH91: 82.5 +/- 1.8% versus 38.5 +/- 2.6%). In contrast, adenovirus expressing antisense heat shock protein 70 showed much less cytotoxicity in normal human bronchial epithelial cells (16.0 +/- 0.5% versus 17.1 +/- 7.3%) and in normal lung fibroblasts IMR90 (17.2 +/- 3.6% versus 8.2 +/- 1.6%). After treatment with adenovirus expressing antisense heat shock protein 70, transactivation of p53 in A549 but not in NCI-H358, a cell line deleted for p53 has been observed. Furthermore, 22.0 +/- 3.0% of A549 cells treated for adenovirus expressing antisense heat shock protein 70 stained positive with terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling versus 10.2 +/- 4.0% treated with control virus. This effect but not cell death itself was blocked by treatment with 10 micromol/L zVAD-fmk, a broad caspase inhibitor. CONCLUSIONS: Selective down-regulation of heat shock protein 70 induces cell death in lung cancer but not in normal lung cells. The demonstrated effect is p53-independent and does not require DNA cleavage. The data suggest that gene transfer of antisense heat shock protein 70 might be useful in developing new strategies for the treatment of lung cancer.

Cell Death↗
PubMed1995

Accelerated recovery of postischemic stunned myocardium after induced expression of myocardial heat-shock protein (HSP70).

In vitro studies suggest that interventions targeted at myocardial gene regulation of endogenous cytoprotective elements, such as heat-shock protein, may attenuate myocardial ischemic injury. We tested the hypothesis that heat shock-induced expression of myocardial heat-shock protein before ischemia accelerates functional recovery of postischemic stunned myocardium in the intact circulation. Sixteen dogs underwent partial femoral arteriovenous bypass and core temperature was raised to 42 degrees C for 15 minutes in eight dogs (heat-shocked) and maintained at 37 degrees C in eight dogs (nonheat-shocked). After 24 hours dogs were studied to measure myocardial segment length in the circumflex artery region with ultrasonic dimension transducers, left ventricular pressure with a micromanometer, and circumflex coronary flow with an ultrasonic probe. Regional contractile function was quantified by the area beneath the linear preload recruitable stroke work relationship at baseline and at intervals during reperfusion after a 15-minute circumflex artery occlusion followed by 3 hours of reperfusion. Baseline and peak reperfusion hyperemic circumflex flows were 37 +/- 9 ml/min and 154 +/- 33 ml/min, respectively, in heat-shocked dogs (p < 0.001) and 46 +/- 24 ml/min and 171 +/- 57 ml/min, respectively, in nonheat-shocked dogs (p < 0.001), with no differences between groups (p = not significant) at any time during reperfusion. Heart rate and left ventricular peak pressure, end-diastolic pressure, and first derivative of left ventricular pressure were similar (all p = not significant) in heat-shocked and nonheat-shocked dogs during ischemia and reperfusion. Before ischemia, preload recruitable stroke work relationship did not differ (p = not significant) in heat-shocked and nonheat-shocked dogs. Ischemia reduced preload recruitable stroke work relationship to 32% +/- 8% control (p < 0.001) in heat-shocked dogs and to 19% +/- 15% control in nonheat-shocked dogs (p < 0.001) at 15 minutes of reperfusion, indicating a similar (p = not significant) initial degree of injury. During 3 hours of reperfusion, preload recruitable stroke work relationship returned to 80% +/- 38% control in heat-shocked dogs but to only 33% +/- 13% control in nonheat-shocked dogs (p < 0.0001). Myocardial expression of heat-shock protein, quantified by optical densitometry of Western blots using an antibody specific for HSP70, was greater in heat-shocked than in nonheat-shocked dogs (108 +/- 27 versus 71 +/- 14 densitometry units, p < 0.005).(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗