• The Korean Journal of Physiology and Pharmacology
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• v.8 no.3
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• pp.147-151
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• 2004

The present study was undertaken to determine the regulation of heat shock proteins (HSP) in the kidney in hypertension. Two-kidney, one clip (2K1C) or deoxycorticosterone acetate (DOCA)-salt hypertension was induced in male Sprague-Dawley rats. At weeks 1 and 4 after inducing the hypertension, the expression of HSP70, HSP32 and HSP25 was determined in the kidney by Western blot analysis. In 2K1C hypertension, the expression of HSP70, HSP32 and HSP25 was increased in the clipped kidney at both weeks 1 and 4. However, in the contralateral kidney, their expression was not significantly altered at week 1, but increased at week 4. In DOCA-salt hypertension, the expression of HSP remained unaltered in the remnant kidney at week 1, but significantly increased at week 4. These results indicate that HSP are differentially regulated in the kidney according to the duration and the model of hypertension.

• Journal of Life Science
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• v.26 no.7
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• pp.826-834
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• 2016

The present investigation was undertaken to examine the effectiveness of the combination treatment of an Hsp90 inhibitor and a SIRT1 inhibitor on suppressing the growth of chemo-resistant human cancer cells. We showed that inhibition of SIRT1 effectively potentiated the cytotoxicity of 17-allylamino-17-demethoxygeldanamycin (17-AAG) and reversed Hsp90 inhibitor resistance in multidrug-resistant (MDR) human ovarian HeyA8-MDR cells. Amurensin G, a potent natural SIRT1 inhibitor, enhanced Hsp90 inhibitor-mediated abrogation of the Hsp90 chaperone function and accelerated degradation of mutated p53 (mut p53), an Hsp90 client protein, by up-regulation of ubiquitin ligase CHIP. Knock-down of CHIP significantly attenuated amurensin G-induced mut p53 degradation. Down-regulation of mut p53 reduced the expression of heat shock factor1 (HSF1)/heat shock proteins (Hsps), a major cause of Hsp90 inhibitor resistance, which led to sensitization of the MDR cells to the Hsp90 inhibitor by the SIRT1 inhibitor. Amurensin G potentiated cytotoxicity of the Hsp90 inhibitor in HeyA8-MDR cells through suppression of 17-AAG-induced Hsp70 and Hsp27 induction via down-regulation of mut p53/HSF1, and it caused activation of PARP and inhibition of Bcl-2. Our data suggests that SIRT1 inhibitors could be used to sensitize MDR cells to Hsp90 inhibitors, possibly through suppression of the mut p53/HSF1-dependent pathway, and a novel mut p53-directed action of SIRT1 inhibition could effectively prevent mut p53 accumulation in MDR cells.

• Clinical and Experimental Reproductive Medicine
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• v.25 no.3
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• pp.305-313
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• 1998

Steroid hormone is known to cause the dynamic changes of mammalian uterus during reproductive cycle. However there is little information about the effect of estrogen (E) and progesterone (P) on the expression of various transcription factors involved in gene expression. Thus the present study was designed to demonstrate E and/or P-induced expression of c-Fos, CREB, ATF and HSP70 in rat uterus. Rats, ovariectomized (OVX) for two weeks, were divided into 6 experimental groups, 1) OVX, 2) OVX+V, 3) OVX+E, 4) OVX+P, 5) OVX+E+V, 6) OVX+E+P, and western blotting assay for nuclear extract and immunohistochemical staining were carried out for each experimental group. Treatment of E $(10{\mu}g)$ showed to increase the expression of c-Fos, CREB, ATF, and HSP70, and maximal expression was occured at $3\sim6$ hr after E administration. P (1mg) also increased, but much less than E, the expression of c-Fos, ATF, and HSP70. However, P did not reveal any effect on the expression CREE. P treatment 4 hr after E injection decreased c-Fos, CREB, and ATF expression, but did not show any change in the E-induced HSP70 expression. In immunohistochemical study c-Fos-, CREB-, and ATF-immunoreactivities were confined to the cells of luminal epithelium of uterine endometrium. These results suggest that proliferation and differentiation of rat uterus during reproductive cycle may mediated via expression of transcription factors, such as c-Fos, CREB, ATF, and HSP70.

• The korean journal of orthodontics
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• v.31 no.2 s.85
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• pp.249-259
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• 2001

This study was designed to evaluate the expression of heat shock protein in tooth and surrounding tissue during the experimental movement of rat incisors, by LSAB(labelled streptavidine biotin) immunohistochemical staining for heat shock protein. Twenty seven Sprague-Dawley rats were divided into a control group(3 rats), and 6 experimental groups(24 rats), to which 75g of force was applied from helical springs across the maxillary incisors. Rats of experimental groups were sacrificed at 0.5, 1, 4, 7, 14 and 28 days after force application, respectively. And the periodontal tissues of a control group and experimental groups were studied immunohistochemically. The results were as follows : 1. In control group, the expression of HSP47 was rare in gingiva, dentin and cementum, and mild in periodontal ligament and alveolar bone. But it was more evident than that of HSP70. 2. The expression of HSP47 or HSP70 was rare or mild in dentin, cementum and odontoblast of experimental group, regardless of the duration of force application, which was not different from that of control group. 3. In experimental group, the expression of HSP47 got to the highest degree in periodontal ligament and alveolar bone at 4 days after force application, and then decreased. And the expression was more evident in the pressure side than in the tension side of periodontal ligament 4. The expression of HSP70 began to increase at 12 hours after force application and got to the highest degree at 4 days, in the capillary of pulp and periodontal ligament. And the expression was more evident in the pressure side than in the tension side of periodontal ligament 5. The expression of HSP70 in alveolar bone of experimental group was rare, which was similar to that of control group.

• Animal Bioscience
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• v.36 no.12
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• pp.1796-1805
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• 2023

Objective: This study aims to identify heat shock protein70-2 (HSP70-2) and protamine-1 (PRM1) mRNA and protein in Madura bull sperm and demonstrate their relation as bull fertility biomarkers. Methods: The Madura bull fertility rates were grouped based on the percentage of first service conception rate (%FSCR) as high fertility (HF) (79.04%; n = 4), and low fertility (LF) (65.84%; n = 4). mRNA of HSP70-2 and PRM1 with peptidylprolyl isomerase A (PPIA) as a housekeeping gene were determined by quantitative real-time polymerase chain reaction, while enzyme-linked immunoassay was used to measure protein abundance. In the post-thawed semen samples, sperm motility, viability, acrosome integrity, and sperm DNA fragmentation index were analyzed. Data analysis was performed on the measured parameters of semen quality, relative mRNA expression, and protein abundance of HSP70-2 and PRM1, among the bulls with various fertility levels (HF and LF) in a one-way analysis of variance analysis. The Pearson correlation was used to analyze the relationship between semen quality, mRNA, proteins, and fertility rate. Results: Relative mRNA expression and protein abundance of HSP70-2 and PRM1 were detected and were found to be highly expressed in bulls with HF (p<0.05) and were associated with several parameters of semen quality. Conclusion: HSP70-2 and PRM1 mRNA and protein molecules have great potential to serve as molecular markers for determining bull fertility.

• Journal of Periodontal and Implant Science
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• v.28 no.1
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• pp.103-120
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• 1998

Prokaryotic and eukaryotic cells respond to heat stress and other environmental abuses by synthesizing a small set of stress proteins and by inhibiting post-transcription synthesis of normal proteins. The purpose of the present study was to document the stress response produced by inflamed gingival tissue in vivo, and cytokine inducted human periodontal ligament cells. Human PDL cells were exposed to TNF-$\alpha$(1ng/ml), INF-$\gamma$(200 U/ml), LPS(100ug/ml), combination of cytokine, and SDS-PAGE gels running and Western blotting analysis was done. In vivo studies, the healthy gingival tissusse of a control group and inflamed gingival tissue of adult periodontitis were studied by immunohistochemistry and histology. The results were as follows 1. HSP 47 was distributed on basal layer in healthy gingiva, but stronger stained in basal, suprabasal, and spinous layer of inflamed gingiva. 2. HSP 47 was rare on endothelial cells and mononuclear cells in healthy gingiva, but stronger expressed in inflamed gingiva. 3. HSP 70 expression was rare on epihelium and inflammatory cells hi both healthy & inflamed gingiva. 4. HSP 70 was actively expressed on endothelial cells and inflammatory cells of capillary lumen in moderately & mild inflamend gingiva. 5. PDL cells showed low level of HSP 47 protein expression which was significantly induced by cytokine stimulation (LSP only and combination). 6. Maximum HSP 70 protein induction was seen with stimulation by a combination of the cytokine, Combination of TNF-$\alpha$, INF-$\gamma$, LPS have been shown to synergistically effects of HSP 70 expression. On the above findings, HSP Is influenced by cytokine and chronic inflammation in vivo, and may be involved in protection of tissue during periodontal inflammatiom.

• Korean Journal of Ichthyology
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• v.19 no.4
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• pp.266-273
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• 2007

Heat shock proteins (HSPs) are a family of highly conserved proteins playing an important role in the functioning of unstressed and stressed cells. The HSP70 family, the most widely studied of the hsps, is constitutively expressed (hsc70) in unstressed cells and is also induced in response to stressors (hsp70), especially those affecting the protein machinery. The HSP/HSC70 proteins act as molecular chaperones and are crucial for protein functioning, including folding, intracellular localization, regulation, secretion, and protein degradation. Here, we report the identification and characterization of the putative amino acid sequence deduced from one cDNA clone identified as heat shock protein 70. The alignment showed that the putative sequence is 100% identical to the heat shock protein 70 cognate (HSC 70) of olive flounder. The 5'-flanking region sequence (approximately 1 kb) ahead of the hsc70 gene was cloned by genome walking and a putative core promoter region and transcription elements were identified. We characterized the promoter of the olive flounder hsc70 gene by examining the ability of 5'-upstream fragments to drive expression of green fluorescent protein (GFP) in live embryos.

• The Journal of Korean Physical Therapy
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• v.26 no.6
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• pp.418-424
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• 2014

Purpose: This study was performed to investigate the effect of joint mobilization on pain relief and cartilage repair in an induced osteoarthritis rat model by analyzing the expression of heat shock protein 70 in articular cartilage. Methods: MIA was injected into SD rats to induce osteoarthritis. These rats were divided into 4 groups: control group (n=30), no further treatment after the MIA injection ; experimental group I(n=30), performed swimming exercise after the MIA injection experimental group II (n=30), underwent joint mobilization after the MIA injection and experimental group III (n=30), performed swimming exercise and underwent joint mobilization after the MIA injection. For the histologic and pathophysiologic evaluation, safranin-O staining and for the immunohistochemical evaluation, the expression of HSP 70 in articular cartilage was analyzed 1, 7, 14, and 21 days after the MIA injection. Results: The inflammatory response and loss of tissue declined in experimental groups I and II over time, whereas the greatest decreases were noted in experimental group III. In the articular cartilage, low expression of HSP 70 was observed in every group on day 1, whereas HSP 70 expression was elevated on days 7 and 14 in experimental groups II and III. After 21 days, experimental group II displayed the strongest positive reaction, whereas HSP 70 was higher in experimental group III at this time point compared to that after 14 days. Conclusion: Our results showed that swimming exercise and joint mobilization had positive effects on pain relief and histologic and functional recovery in an induced osteoarthritis rat model.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.3
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• pp.1285-1290
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• 2014

The aim was to determine whether ultrasound targeted microbubble destruction (UTMD) promotes dual targeting of HSP72 and HSC70 for therapy of castration-resistant prostate cancer (CRPC), to improve the specific and efficient delivery of siRNA, to induce tumor cell specific apoptosis, and to find new therapeutic targets specific of CRPC.VCaP cells were transfected with siRNA oligonucleotides. HSP70, HSP90 and cleaved caspase-3 expression were determined by real-time quantitative polymerase chain reaction and Western blotting. Apoptosis and transfection efficiency were assessed by flow cytometry. Cell viability assays were used to evaluate safety. We found HSP72, HSC70 and HSP90 expression to be absent or weak in normal prostate epithelial cells (RWPE-1), but uniformly strong in prostate cancerous cells (VCaP). UTMD combined with dual targeting of HSP72 and HSC70 siRNA improve the efficiency of transfection, cell uptake of siRNA, downregulation of HSP70 and HSP90 expression in VCaP cells at the mRNA and protein level, and induction of extensive tumor-specific apoptosis. Cell counting kit-8 assays showed decreased cellular viability in the HSP72/HSC70-siRNA silenced group. These results suggest that the combination of UTMD with dual targeting HSP70 therapy for PCa may be most efficacious, providng a novel, reliable, non-invasive, safe targeted approach to improve the specific and efficient delivery of siRNA, and achieve maximal effects.

• Journal of fish pathology
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• v.21 no.1
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• pp.13-20
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• 2008

This study evaluates the pathogenicity in striped beakperch, Oplegnathus fasciatus infected with red sea bream iridovirus (RSIV) at different water temperature (17°C, 20°C, 25°C and 27°C). When the fish group was infected with RSIV at 17°C and 20°C, cumulative mortality did not show any significant difference with control group. In contrast, the case at 25°C and 27°C, cumulative mortality reached more than 80%. However, RSIV was detected from all of the fish in each temperature. To confirm a relationship between temperature change and heat shock protein (HSP), partial HSP70 cDNA was isolated from striped beakperch.