• Journal of Periodontal and Implant Science
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• v.35 no.1
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• pp.1-8
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• 2005

Bacterial heat shock protein has been one of the components that are responsible to induce autoimmune disease mechanisms in the pathogenesis of atherosclerosis due to high level of homology in sequence with human counterpart. This mechanism may explain how bacterial infectious disease, such as periodontal disease, might contribute to the acceleration of the disease process of atherosclerosis. Porphyromonas gingivalis which is a major periodontal pathogenic bacterial species, has been implicated as one of the pathogenic bacteria playing the role in this context. The present study has been performed to evaluate the anti-atherosclerotic effect of adoptive transfer of Porphyromonas gingivalis heat shock protein epitope-specific T cell lines into severe combined immunodeficiency (SCID) mice. Peptide no. 15 with amino acid sequence VKEVASKTND-specific T cell line was selected for the transfer. When experimental atherosclerosis was induced in SCID mice adoptively transferred either by the T cell lines (experimental group) or by non-specific mouse T cells (control group), there was no significant difference in the severity and extent of the atherosclerosis induced by hypercholesterol diet.

• Proceedings of the Botanical Society of Korea Conference
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• 1999.04a
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• pp.18-18
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• 1999

We characterized a cDNA clone for a low molecular weight heat-shock protein (LMW HSP) from tobacco named TLHS-l. Nucleotide sequence determination of TLHS-1 identified an open reading frame for 159 amino acids. To the upstream of the open reading frame, a sequence of 124 nucleotides was determined. To the 3' downstream of the open reading frame, 212 nucleotides were identified which carried poly(A)-tail. Comparison of the open reading frame and hydropathy plot of TLHS-1 with the previously reported class I LMW HSPs showed high identity which classified TLHS-1 as a class I LMW HSP cDNA clone. We proposed that there are six consensus regions in class I LMW HSPs. RNA blot hybridization for TLHS-1 showed a typical expression pattern of heat-shock-inducible gene from three common tobacco cultivars. The open reading frame of TLHS-1 was overexpressed in Escherichia coli. TLHS-1 protein confers thermal protection of other proteins in vitro and in vivo. Thermal induced aggregation of citrate synthase was reduced by purified TLHS-1 protein, and thermal death rate at $50^{\circ}C$ was reduced in E. coli expressing TLHS-l. From these data, we can expect that TLHS-1 acts as a molecular chaperone.perone.

• Bulletin of the Korean Chemical Society
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• v.34 no.11
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• pp.3405-3409
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• 2013

The activation of heat shock factor 1 (HSF1) can be induced by the changes in environmental pH, but the mechanism of HSF1 activation by acidification is not completely understood. This paper reports that a low pH (pH~6.0) can trigger human HSF1 activation. Considering the involvement of the imidazole group of histidine residues under acid pH stress, an in vitro EMSA experiment, Trp-fluorescence spectroscopy, and protein structural analysis showed that the residue, His83, is the essential for pH-dependent human HSF1-activation. To determine the roles of His83 in the HSF1-mediated stress response affecting the cellular acid resistance, mouse embryo fibroblasts with normal wild-type or mutant mouse HSF1 expression were preconditioned by heating or pH stress. The results suggest that His83 is essential for HSF1 activation or the HSF1-mediated transcription of heat shock proteins, in protecting cells from acid pH stress.

• Journal of Animal Science and Technology
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• v.65 no.4
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• pp.683-697
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• 2023

The threat posed by increased surface temperatures worldwide has attracted the attention of researchers to the reaction of animals to heat stress. Spermatogenesis in animals such as stallions is a temperature-dependent process, ideally occurring at temperatures slightly below the core body temperature. Thus, proper thermoregulation is essential, especially because stallion spermatogenesis and the resulting spermatozoa are negatively affected by increased testicular temperature. Consequently, the failure of thermoregulation resulting in heat stress may diminish sperm quality and increase the likelihood of stallion infertility. In this review, we emphasize upon the impact of heat stress on spermatogenesis and the somatic and germ cells and describe the subsequent testicular alterations. In addition, we explore the functions and molecular responses of heat shock proteins, including HSP60, HSP70, HSP90, and HSP105, in heat-induced stress conditions. Finally, we discuss the use of various therapies to alleviate heat stress-induced reproductive harm by modulating distinct signaling pathways.

• Journal of Microbiology and Biotechnology
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• v.30 no.1
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• pp.136-145
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• 2020

Chlorella sp. HS2, which previously showed excellent performance in phototrophic cultivation and has tolerance for wide ranges of salinity, pH, and temperature, was cultivated heterotrophically. However, this conventional medium has been newly optimized based on a composition analysis using elemental analysis and ICP-OES. In addition, in order to maintain a favorable dissolved oxygen level, stepwise elevation of revolutions per minute was adopted. These optimizations led to 40 and 13% increases in the biomass and lipid productivity, respectively (7.0 and 2.25 g l^-1d^-1 each). To increase the lipid content even further, 12 h heat shock at 50℃ was applied and this enhanced the biomass and lipid productivity up to 4 and 17% respectively (7.3 and 2.64 g l^-1d^-1, each) relative to the optimized conditions above, and the values were 17 and 14% higher than ordinary lipid-accumulating N-limitation (6.2 and 2.31 g l^-1d^-1). On this basis, heat shock was successfully adopted in novel Chlorella sp. HS2 cultivation as a lipid inducer for the first time. Considering its fast and cost-effective characteristics, heat shock will enhance the overall microalgal biofuel production process.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.30 no.4
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• pp.323-330
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• 2004

Estrogen may promote osteoblast/osteocyte viability by limiting apoptotic cell death. We hypothesize that hsp27 is an estrogen- regulated protein that can promote osteoblast viability by increasing osteoblast resistance to apoptosis. The purpose of this study was to determine the effect of estrogen treatment and heat shock on $TNF{\alpha}$ - induced apoptosis in the MC3T3-E1 cell line. Cells were treated with 0 - 100 nM $17{\beta}$ estradiol (or ICI 182780) for 0 - 24 hours before heat shock. After recovery, apoptosis was induced by treatment with 0 - 10 ng/ml TNF${\alpha}$. Hsp levels were evaluated by Northern and Western analysis using hsp27, hsp47, hsp70c and hsp70i - specific reagents. Apoptosis was revealed by in situ labeling with Terminal Deoxyribonucleotide Transferase (TUNEL). A 5 - fold increase in hsp27 protein and mRNA was noted after 5 hours of treatment with 10 - 20 nM $17{\beta}$ estradiol prior to heat shock. Increased abundance of hsp47, hsp70c or hsp70i was not observed. TUNEL indicated that estrogen treatment also reduced (50%) MC3T3-E1 cell susceptibility to $TNF{\alpha}$ - induced apoptosis. Treatment with hsp27-specific antisense oligonucleotides prevented hsp27 protein expression and abolished the protective effects of heat shock and estrogen treatment on $TNF{\alpha}$- induced apoptosis. Hsp27 is a determinant of osteoblast apoptosis, and estrogen treatment increases hsp27 levels in cultured osteoblastic cells. Hsp27 contributes to the control of osteoblast apoptosis and may be manipulated by estrogenic or alternative pathways for the improvement of bone mass.

• Clinical and Experimental Reproductive Medicine
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• v.29 no.1
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• pp.37-44
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• 2002

Objective : Heat shock protein family is related to protective mechanism of cells by environmental changes. This study was performed to evaluate the effect of cryopreservation on the heat shock protein 90 (Hsp90) expression in mouse ovarian tissue. Methods : Cryopreservation of mouse ovarian tissue was carried out by slow freezing method. The mRNA level of Hsp90 expression in both fresh and cryopreserved mouse ovarian tissue was analyzed by RT-PCR. The protein expression of Hsp90 was evaluated by Western blot analysis and immunohistochemistry. Results: The mRNA and protein of Hsp90 were expressed in both fresh and cryopreserved mouse ovarian tissue. The amount of Hsp90 mRNA was increased in cryopreserved ovarian tissue after 60 and 90 minutes after thawing and incubation. The amount of Hsp90 protein was increased in the cryopreserved ovarian tissue after 6 hours of the incubation in Western blot analysis. In immunohistochemical study, Hsp90 protein was localized in cytoplasm of oocytes and granulosa cells. Significant level of immunoreactive Hsp90 protein was detected in theca cells contrast to the weak expression in ovarian epithelial cells. Conclusion: This results showed the increase of Hsp90 expression in both mRNA and protein level in the cryopreserved mouse ovarian tissue. It can be suggested that Hsp90 may play a role in the protective or recovery mechanism against the cell damage during cryopreservaion.

• The Korean Journal of Physiology and Pharmacology
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• v.22 no.4
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• pp.457-465
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• 2018

The expression of BCL-2 interacting cell death suppressor (BIS), an anti-stress or anti-apoptotic protein, has been shown to be regulated at the transcriptional level by heat shock factor 1 (HSF1) upon various stresses. Recently, HSF1 was also shown to bind to BIS, but the significance of these protein-protein interactions on HSF1 activity has not been fully defined. In the present study, we observed that complete depletion of BIS using a CRISPR/Cas9 system in A549 non-small cell lung cancer did not affect the induction of heat shock protein (HSP) 70 and HSP27 mRNAs under various stress conditions such as heat shock, proteotoxic stress, and oxidative stress. The lack of a functional association of BIS with HSF1 activity was also demonstrated by transient downregulation of BIS by siRNA in A549 and U87 glioblastoma cells. Endogenous BIS mRNA levels were significantly suppressed in BIS knockout (KO) A549 cells compared to BIS wild type (WT) A549 cells at the constitutive and inducible levels. The promoter activities of BIS and HSP70 as well as the degradation rate of BIS mRNA were not influenced by depletion of BIS. In addition, the expression levels of the mutant BIS construct, in which 14 bp were deleted as in BIS-KO A549 cells, were not different from those of the WT BIS construct, indicating that mRNA stability was not the mechanism for autoregulation of BIS. Our results suggested that BIS was not required for HSF1 activity, but was required for its own expression, which involved an HSF1-independent pathway.

• International Journal of Industrial Entomology and Biomaterials
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• v.16 no.1
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• pp.21-27
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• 2008

The expression of heat shock protein genes (Hsp 70, Hsp 40, Hsp 20.8 and Hsp 20.4) against thermal stress in silkworm Bombyx mori was performed through semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR). Upon exposure of silkworm to two temperature regimes ($38^{\circ}C$ and $42^{\circ}C$), significant change in the expression of Hsp gene was observed as compared to the control. Hsp 70 and Hsp 40 showed increased expression than the small heat shock protein genes Hsp 20.8 and Hsp 20.4. The Hsp 70 showed increased expression during the recovery period as compared to 1 hr thermal treatments ($38^{\circ}C$/1 hr and $42^{\circ}C$/1 hr). Whereas, Hsp 40, Hsp 20.8 and Hsp 20.4 genes showed higher expression level at initial stages that later gradually decrease during recovery period. Tissue specific expression of Hsp 70 showed variation in the level of expression amongst the tissues. The mid gut and fat body tissues showed higher expression than the cuticle and silk gland tissue. The Hsp 70, Hsp 40 gene expression was analyzed in thermotolerant (Nistari) and thermo susceptible silk worm strain (NB4D2) and results showed significant variation in their expression level. The Nistari showed higher expression of Hsp 70 and Hsp 40 genes than the NB4D2. These findings provide a better understanding of cellular protection mechanisms against environmental stress such as heat shock, as these Hsps are involved in an organism thermotolerance.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.48 no.3
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• pp.354-361
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• 2015

Mitochondrial heat shock protein 75 (mtHSP75) is a member of the HSP90 family and plays essential roles in refolding proteins of the mitochondrial matrix. Mitochondria provide energy in the form of ATP and generate reactive oxygen species (ROS). Heat shock proteins (HSPs) are activated in response to stress, and protect cells. In this study, we characterized the mtHSP75 of the big-belly seahorse Hippocampus abdominalis. The protein (BsmtHSP75) is encoded by an open reading frame (ORF) of 2,157 nucleotides, has 719 amino acids (aa), and is of molecular mass 82 kDa. BsmtHSP75 has two functional domains, a histidine kinase-like ATPase (HATPase_c) domain (123-276 aa) and an HSP90 family domain (302-718 aa). BsmtHSP75 was expressed in all tested tissues of healthy seahorses. The ovary contained the highest transcription level, followed (in order) by the blood, brain, and muscle. Pouch tissue showed the lowest expression level. The expression of BsmtHSP75 was significantly (P<0.05) up-regulated on viral or bacterial challenge, suggesting that BsmtHSP75 plays a role in the immune defense against bacterial and viral pathogens.