scholarly journals Biochemical Analysis of the Differential Tissue Expression of Heat Shock Protein70 Following Exposure to Electromagnetic

2021 ◽  
Vol 14 (1) ◽  
pp. 273-282
Author(s):  
Nasser Al-Nazwani ◽  
Najam Siddiqi ◽  
Yahya Tamimi ◽  
Zoya Sheikh
Keyword(s):  
Heat Shock ◽  
Tissue Expression ◽  
Heart Tissue ◽  
Physical Stimulus ◽  
Hsp70 Mrna ◽  
Low Field ◽  
Set Up ◽  
Shock Proteins ◽  
Chicken Eggs ◽  
Concentration Methods

Low field electromagnetic radiation that is emitted from cell phones may induce morphological aberrations and change in gene expression of heat shock protein 70 (Hsp 70). Using Real Time PCR (RTPCR) and protein concentration methods, we studied changes in levels of Hsp70 mRNA and protein synthesis after exposure to the physical stimulus. We also evaluated the suitability of using chick embryo as a model to study alteration in heat shock proteins expression and translation using specific egg incubator set up. Zero-day fertilized chicken eggs were used and a popular mobile phone and service provider was selected with 1800 MHz frequency, power of 0.47 W/kg body and SAR 1.10 w/KG (head). The total daily exposure duration was 50 minutes in each 24 hours with variable maximum exposure time. Experimental samples were divided into controls with no exposure and experimental samples. The developing embryos were removed and different organs were isolated for estimation of Hsp70mRNA and protein. This physical stimulus caused a sequential increase of mRNA corresponding to the period of exposure. Liver tissue demonstrated higher levels of mRNA than heart tissue. Nonetheless, this increase in mRNA was not matched with an increase in the amount of protein of the corresponding mRNA in both tissues at different exposure times. Total protein in all tissues remained unchanged due to slow down of the clearance process and as an indication that the cell is struggling to preserve housekeeping proteins signaling attempt of survival.

scholarly journals Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells

1994 ◽  
Vol 300 (1) ◽  
pp. 201-209 ◽  
Author(s):  
G Elia ◽  
M G Santoro
Keyword(s):  
Heat Shock ◽  
Mammalian Cells ◽  
Elevated Temperatures ◽  
K562 Cells ◽  
Hsp70 Expression ◽  
Transcriptional Level ◽  
Hsp70 Mrna ◽  
Shock Proteins ◽  
Hsp70 Synthesis

Synthesis of heat-shock proteins (HSPs) is universally induced in eukaryotic and prokaryotic cells by exposure to elevated temperatures or to other types of environmental stress. In mammalian cells, HSPs belonging to the 70 kDa family (HSP70) have a regulatory role in several cellular processes, and have been shown to be involved in the control of cell proliferation and differentiation. Although many types of HSP70 inducers have been identified, only a few compounds, all belonging to the flavonoid group, have been shown to inhibit HSP70 induction. Because inhibitors of HSP70 synthesis could be an important tool with which to study the function of this protein, we have investigated the effect of quercetin, a flavonoid with antiproliferative activity which is widely distributed in nature, on HSP70 synthesis in human K562 erythroleukaemia cells after treatment with severe or mild heat shock and with other inducers. Quercetin was found to affect HSP70 synthesis at more than one level, depending on the conditions used. Indeed, after severe heat shock (45 degrees C for 20 min) treatment with quercetin, at non-toxic concentrations, was found to inhibit HSP70 synthesis for a period of 3-4 h. This block appeared to be exerted at the post-transcriptional level and to be cell-mediated, as the addition of quercetin during translation of HSP70 mRNA in vitro had no effect. After prolonged (90 min) exposure at 43 degrees C, however, quercetin was found to inhibit also HSP70 mRNA transcription. Pretreatment of K562 cells with quercetin had no effect on HSP70 expression, and quercetin needed to be present during induction to be effective. Under all conditions tested, the quercetin-induced block of HSP70 synthesis was found to be transient and, after an initial delay, synthesis of HSP70 reached the control rate and continued at the same level for several hours after the time at which HSP70 synthesis had been turned off in control cells. Finally, inhibition of HSP70 synthesis by quercetin appeared to be dependent on the temperature used and on the type of stressor.

scholarly journals Interleukin 1 induces the expression of a heat-shock gene in chondrocytes

1991 ◽  
Vol 277 (2) ◽  
pp. 327-330 ◽  
Author(s):  
T F Cruz ◽  
R A Kandel ◽  
I R Brown
Keyword(s):  
Heat Shock ◽  
Interleukin 1 ◽  
Heat Shock Gene ◽  
Proteoglycan Synthesis ◽  
Hsp70 Mrna ◽  
Mrna Species ◽  
Shock Gene ◽  
Shock Proteins ◽  
Arthritic Joints

The presence of T cells and antibodies reactive with heat-shock proteins (hsps) in the joints of patients with rheumatoid arthritis may indicate a role of hsps in this disease. In the present study we examined whether increased temperature and interleukin 1 (IL 1), both of which are elevated in arthritic joints, induced the expression of two hsp70 genes in bovine chondrocyte cultures. We found that heat shock resulted in increased expression of constitutive and inducible hsp70 mRNA species. IL 1 and phorbol 12-myristate 13-acetate (PMA) also induced an increase in the constitutive hsp70 mRNA species, but without affecting the expression of the inducible hsp70 gene. The increase induced by IL 1 was observed only after 3 h, whereas increases induced by PMA were observed within 1 h. For all treatments, the hsp70 mRNA decreased by 24 h. Heat treatment of chondrocytes did not affect levels of collagenase and caseinase activity in the medium, nor did it alter proteoglycan synthesis by these cells.

scholarly journals Effects of transport stress on pathological injury and expression of main heat shock proteins in the caprine stomach

2020 ◽  
Vol 16 (1) ◽  
Author(s):  
Wei Hu ◽  
Tian Ye ◽  
Yanzhen Yang ◽  
Ben Liu ◽  
Wenya Zheng
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Jiangxi Province ◽  
Control Group ◽  
Hsp70 Mrna ◽  
Stress Group ◽  
Protein Levels ◽  
Transport Stress ◽  
Shock Proteins

Abstract Background Transportation is necessary to introduce new breeds of goats to the farm and move the adult meat goat from the farm to the slaughterhouse. However, these actions may give rise to transport stress. Heat shock proteins (HSPs) are playing some important regulate roles during transport stress. The aim of this study was to evaluate the effects of transport stress on the pathological injury and HSPs expression in the stomach of goats. A total of three batches of Ganxi goats from western Jiangxi province were enrolled in this study. For each batch, twelve healthy adult male goats were randomly divided into three groups (four goats per batch and per group): Control group, stress group transported during 2 h and stress group transported during 6 h. Results Our results showed that the different degrees of stomach walls damage, with the change of expression levels of heat shock protein 27 (HSP27), heat shock protein 70 (HSP70) and heat shock protein 90 (HSP90), occurred after goats transportation. In rumen, the mRNA and protein expressions of HSP27 and HSP70 were increased after transport stress, but not HSP90. In reticulum, all three HSPs mRNA and protein levels were upregulated after 2 h transport, but decreased after 6 h transport. In omasum, HSP27 and HSP70 mRNA and protein were increased after transport stress, however, HSP90 mRNA level only had a slightly enhancement after transport stress. In abomasum, HSP70 and HSP90 mRNA and protein levels were increased after transport stress, but HSP27 was decreased after transport stress. Conclusions Taken together, these results revealed that the pathological changes in the gastric tissues and the stomach HSPs expression in goats are related to transport stress and duration. Moreover, this study also provides some new data to advocate reducing transport stress of goats and improving animal welfare.

Oxidative parameters and expression of 70kDa heat shock proteins in pig heart tissue after transport and slaughter

2014 ◽  
Vol 17 (3) ◽  
pp. 433-439
Author(s):  
R. Urban-Chmiel ◽  
R. Pyz-Łukasik ◽  
A. Dudzic ◽  
A. Wernicki
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Western Blotting ◽  
Thiobarbituric Acid ◽  
Heart Tissue ◽  
Markers Of Oxidative Stress ◽  
Effects Of Stress ◽  
Shock Proteins

Abstract In view of the significant role of Hsp70 in protecting the organism against the destructive effects of stress, and the possibility of using this protein as a marker of the infarction process in the heart, the aim of this study was to conduct an evaluation of the expression of 70kDa heat shock proteins (Hsp70) and the concentration of TBARS (thiobarbituric acid reactive substances) and nitric oxide ions (NO), determined as nitrite ions, as markers of oxidative stress in hearts obtained from healthy pigs following slaughter and pigs which had died during or immediately after transport with symptoms of sudden cardiac death. The material consisted of hearts obtained from 90 pigs following slaughter and from pigs which had died. Oxidative stress was determined in heart lysates based on the concentration of TBARS and nitrite ions. Expression and concentration of Hsp70 were determined using SDS-PAGE, Western blotting, and ELISA. Expression of Hsp70 was observed in hearts lysates obtained from slaughtered pigs and from those which had died with symptoms of sudden death. The strongest reaction in the Western Blotting was noted in hearts lysates from pigs with no pathological changes. The highest TBARS concentration was observed in lysates from hearts in pigs which had died during or immediately after transport. The highest concentration of NO ions, determined as nitrite ions, was noted in hearts from pigs with myocardial infarction lesions. The significant decrease observed in Hsp70 concentration in heart tissue obtained from the pigs which had died in comparison to the hearts from healthy pigs indicates the important role of this protein in protecting the heart muscle against the destructive effects of stress, which limits the occurrence of post-stress cardiomyopathy in pigs following transport.

Heat stress regulates the human 70-kDa heat-shock gene through the 3'-untranslated region

1993 ◽  
Vol 264 (6) ◽  
pp. L533-L537 ◽  
Author(s):  
P. L. Moseley ◽  
E. S. Wallen ◽  
J. D. McCafferty ◽  
S. Flanagan ◽  
J. A. Kern
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Posttranscriptional Regulation ◽  
Untranslated Region ◽  
Heat Shock Gene ◽  
Beta Globin ◽  
Sv40 Promoter ◽  
Posttranscriptional Control ◽  
Hsp70 Mrna ◽  
Shock Proteins

Cells respond to a variety of stresses by synthesizing a family of proteins termed heat-shock proteins (HSP). Recently, the 3'-untranslated regions (UTRs) of some mRNAs have been shown to be important in the posttranscriptional regulation of protein production. Therefore, we hypothesized that heat could regulate HSP70 production through the HSP70 3'-UTR, in addition to its known effects on transcription. To test this hypothesis, cells were transfected with either a plasmid containing sequences encoding the human HSP70 or beta-globin 3'-untranslated region placed downstream of a chloramphenicol acetyltransferase (CAT) reporter gene. In both plasmids, the CAT gene was driven by an SV40 promoter. Following heat stress, cells transfected with the CAT construct containing the HSP70 3'-UTR showed increased CAT activity relative to the beta-globin 3'-UTR construct. This effect paralleled increases in HSP70 mRNA and levels of the inducible HSP70 protein by Western blot. These studies identify a heat-induced mechanism of posttranscriptional control of HSP70 synthesis utilizing the HSP70 3'-UTR, which may be important in the cells ability to regulate the heat-shock response.

Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells

1997 ◽  
Vol 75 (6) ◽  
pp. 777-782 ◽  
Author(s):  
Douglas Briant ◽  
Nicholas Ohan ◽  
John J Heikkila
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Proteins ◽  
Cultured Cells ◽  
Concurrent Treatment ◽  
Hsp70 Mrna ◽  
Mild Heat ◽  
Herbimycin A ◽  
Shock Proteins

We have examined the effect of herbimycin A, a benzoquinoid ansamycin antibiotic, on the pattern of gene expression in amphibians. Exposure of Xenopus laevis A6 kidney epithelial cells to 1 µg/mL herbimycin A induced the synthesis of the heat shock proteins hsp30 and hsp70 as well as 33- and 45-kDa proteins. Enhanced synthesis of a 34-kDa protein appears to be specific to herbimycin A because its synthesis did not increase after heat shock (35°C). In addition, the synthesis of hsp30 and hsp70 induced by herbimycin A was accompanied by an increase in their mRNAs. Herbimycin A induced a transient accumulation of hsp30 and hsp70 mRNA, which peaked between 4 and 6 h. Finally, concurrent treatment of cells with 0.5 µg/mL herbimycin A and a mild heat shock of 27°C yielded a synergistic accumulation of hsp30 and hsp70 mRNA. These studies demonstrate that herbimycin A can induce the expression of a set of stress proteins in amphibians and that concurrent treatment with herbimycin A and mild heat shock has a synergistic effect on the accumulation of hsp30 and hsp70 mRNA. Key words: heat shock, heat shock proteins, Xenopus, herbimycin A, mRNA.

Castration inhibits exercise-induced accumulation of Hsp70 in male rodent hearts

2006 ◽  
Vol 290 (4) ◽  
pp. H1610-H1616 ◽  
Author(s):  
K. J. Milne ◽  
D. B. Thorp ◽  
C. W. J. Melling ◽  
E. G. Noble
Keyword(s):  
Heat Shock ◽  
Acute Exercise ◽  
Exercise Bout ◽  
Treadmill Running ◽  
Sprague Dawley ◽  
Intact Male ◽  
Hsp70 Mrna ◽  
Male Response ◽  
Exercise Induced ◽  
Shock Proteins

Intense exercise leads to accumulation of the inducible member of the 70-kDa family of heat shock proteins, Hsp70, in male, but not female, hearts. Estrogen is at least partially responsible for this difference. Because androgen receptors are expressed in the heart and castration leads to decreases in calcium regulatory proteins and altered cardiac function, testosterone (T) or its metabolites could also be involved. We hypothesized that removal of endogenous T production through castration would reduce cardiac Hsp70 accumulation after an acute exercise bout, whereas castrated animals supplemented with 5α-dihydrotestosterone (DHT) would show the intact male response. Fifty-four 8-wk-old male Sprague-Dawley rats were divided into intact, castrated, or castrated + DHT groups ( n = 18/group). At 11 wk of age, 12 animals in each group undertook a 60-min bout of treadmill running at 30 m/min (2% incline) while the remaining 6 in each group remained sedentary. At 30 min or 24 h after exercise ( n = 6/time point), blood and hearts were harvested for analysis. Serum T was undetectable in castrated and DHT-treated castrated rats, whereas serum DHT was significantly reduced in castrated animals only (∼60% reduction) ( P < 0.05). Although there were no differences in constitutive levels of Hsp70 protein, exercise significantly increased cardiac hsp70 mRNA and protein in intact and DHT-supplemented rats, but not in castrated animals ( P < 0.05). To examine whether castration eliminated the ability to respond to stress, another six intact and six castrated animals were subjected to a 15-min period of hyperthermia (core temperature raised to 42°C) and killed 24 h later. As opposed to exercise, castrated animals subjected to heat shock exhibited increases in Hsp70 above nonshocked (i.e., sedentary) animals, similarly to intact males ( P < 0.05). These data suggest that androgens, in addition to estrogen, play a role in the sexual dimorphism observed in the stress response to exercise but not heat shock.

Thermoregulatory and heat-shock protein response deficits in cold-exposed diabetic mice

1996 ◽  
Vol 270 (3) ◽  
pp. R525-R532 ◽  
Author(s):  
J. M. Matz ◽  
K. P. LaVoi ◽  
P. N. Epstein ◽  
M. J. Blake
Keyword(s):  
Heat Shock ◽  
Cold Exposure ◽  
Uncoupling Protein ◽  
Hsp70 Expression ◽  
Diabetic Mice ◽  
Induced Expression ◽  
Hsp70 Mrna ◽  
Brown Adipose ◽  
Shock Proteins ◽  
And Function

Cold-induced expression of heat-shock proteins (HSPs) has been suggested to facilitate thermogenesis in brown adipose tissue (BAT). However, the regulation of this response and the mechanism supporting this facilitation have not been established. Because of the significant role of insulin in maintaining BAT thermogenesis, we employed a transgenic mouse model of diabetes to investigate the regulation and function of HSPs in BAT thermogenesis. These transgenic mice overexpress a calmodulin minigene regulated by the rat insulin II promotor, resulting in severe diabetes characterized by elevated blood glucose and glucagon that coincides with reduced serum and pancreatic insulin. Body temperature (Tb) of diabetic mice dropped significantly faster during a 3-h cold exposure (6 degrees C) than Tb of similarly treated control littermates. Cold exposure resulted in increased levels of constitutive and inducible HSP70 transcripts in control mice, but only constitutive HSP70 mRNA transcripts were induced in diabetic mice. Diabetes did not affect uncoupling protein induction, but cold-induced expression of members of other HSP families was reduced. Correspondingly, heat-shock regulatory factors were not activated in diabetic mice even though these factors were present. Phenylephrine induced HSP70 expression in control and diabetic animals, indicating that alpha-receptor-coupled HSP induction remained intact in BAT of diabetic mice. Insulin replacement restored the Tb response of diabetic mice as well as the HSP response. From these results it is clear that physiological signals that regulate cold-induced activation of BAT also regulate HSP expression in this tissue. This diabetic model provides a novel system in which the HSP response to cold has been selectively knocked out, making it a useful tool for the study of HSP regulation and function in BAT.

TNF receptor I is required for induction of macrophage heat shock protein 70

2001 ◽  
Vol 281 (1) ◽  
pp. C241-C247 ◽  
Author(s):  
Julie K. Heimbach ◽  
Leonid L. Reznikov ◽  
Casey M. Calkins ◽  
Thomas N. Robinson ◽  
Charles A. Dinarello ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Cellular Stress ◽  
Hsp70 Expression ◽  
Hsp70 Mrna ◽  
Tnf Α ◽  
Independent Mechanism ◽  
Shock Proteins ◽  
Tnf Receptor I ◽  
Necrosis Factor

Expression of heat shock proteins (HSP) is an adaptive response to cellular stress. Stress induces tumor necrosis factor (TNF)-α production. In turn, TNF-α induces HSP70 expression. However, osmotic stress or ultraviolet radiation activates TNF-α receptor I (TNFR-I) in the absence of TNF-α. We postulated that TNF-α receptors are involved in the induction of HSP70 by cellular stress. Peritoneal Mφ were isolated from wild-type (WT), TNF-α knockout (KO), and TNFR (I or II) KO mice. Cells were cultured overnight and then heat stressed at 43 ± 0.5°C for 30 min followed by a 4-h recovery at 37°C. Cellular HSP70 expression was induced by heat stress or exposure to endotoxin [lipopolysaccharide (LPS)] as determined by immunoblotting. HSP70 expression induced by either heat or LPS was markedly decreased in TNFR-I KO Mφ, whereas TNFR-II KO Mφ exhibited HSP70 expression comparable to that in WT mice. Expression of HSP70 after heat stress in TNF-α KO Mφ was also similar to that in WT mice, suggesting that induction of HSP70 by TNFR-I occurs independently of TNF-α. In addition, levels of steady-state HSP70 mRNA were similar by RT-PCR in WT and TNFR-I KO Mφ despite differences in protein expression. Furthermore, the effect of TNFR-I appears to be cell specific, since HSP70 expression in splenocytes isolated from TNFR-I KO was similar to that in WT splenocytes. These studies demonstrate that TNFR-I is required for the synthesis of HSP70 in stressed Mφ by a TNF-independent mechanism and support an intracellular role for TNFR-I.

Thermotolerant desert lizards characteristically differ in terms of heat-shock system regulation

2000 ◽  
Vol 203 (6) ◽  
pp. 1017-1025 ◽  
Author(s):  
O.G. Zatsepina ◽  
K.A. Ulmasov ◽  
S.F. Beresten ◽  
V.B. Molodtsov ◽  
S.A. Rybtsov ◽  
...  
Keyword(s):  
Heat Shock ◽  
Gene Promoter ◽  
Heat Shock Gene ◽  
Ecological Niches ◽  
Lizard Species ◽  
Hsp70 Mrna ◽  
Desert Species ◽  
Shock System ◽  
Shock Gene ◽  
Shock Proteins

We compare the properties and activation of heat-shock transcription factor (HSF1) and the synthesis of a major family of heat-shock proteins (HSP70) in lizard species inhabiting ecological niches with strikingly different thermal parameters. Under normal non-heat-shock conditions, all desert-dwelling lizard species studied so far differ from a northern, non-desert species (Lacerta vivipara) in the electrophoretic mobility and content of proteins constitutively bound to the regulatory heat-shock elements in the heat-shock gene promoter. Under these conditions, levels of activated HSF1 and of both HSP70 mRNA and protein are higher in the desert species than in the non-desert species. Upon heat shock, HSF1 aggregates in all species studied, although in desert species HSF1 subsequently disaggregates more rapidly. Cells of the northern species have a lower thermal threshold for HSP expression than those of the desert species, which correlates with the relatively low constitutive level of HSPs and high basal content of HSF1 in their cells.

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