• The Journal of Korean Physical Therapy
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• v.12 no.1
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• pp.147-151
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• 2000

Heat shock protein 70(HSP70) is induced by elevated temperature and many other types of stresses in cell. HSP70 ensures cell survival under stressful condition that would lead to irreversible cell damage and ultimately to cell death. HSP70 plays essential role in the synthesis, transport, and folding of proteins and is often refferred to as molecular chaperones. Increased levels of HSPs occur after arthritis, infection, imflammation, autoimmune disease and CNS injury such as infarction, ischemia, seizure and Alzheimer's disease. Also, HSP70 increases resistance to apoptosis. The recent studies that the expression of the HSP has been processed at various field. However, they an still relatively line studied in clinically application. This review summarizes the fundamental knowledge of HSP.

• Korean Journal of Poultry Science
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• v.42 no.2
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• pp.157-167
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• 2015

We compared the degrees of stress response of 12 domestic purebred chicken strains that have been bred at National Institute of Animal Science, RDA, Korea since 1980. As a physiological marker of stress response, the expression levels of heat shock protein (HSP)-70, HSP-$90{\alpha}$, HSP-$90{\beta}$, hydroxyl-3-methyl-glutaryl coenzyme A reductase (HMGCR) genes and telomere length were measured by quantitative real-time polymerase chain reaction using the lymphocytes of 1,101 chickens. There was significant difference in HSP-70, HSP-$90{\alpha}$, HMGCR expression and telomere length among the strains. There was also significant difference in HSP-$90{\alpha}$, HSP-$90{\beta}$, and HMGCR expression between male and female chickens. Different age groups of chicken exhibited different expression levels of HSP-70, HSP-$90{\alpha}$ and telomere length. The results of the HSPs expression level suggested that, the strains of R, L and Y were highly resistant to stress, whereas the strains of S, O and W were susceptible to stress. Although the statistical differences in some of HSPs gene expression existed between genders, the HSP expression results varied in different strains that some opposed to the others, and there might be interaction between strains and genders, which conclude that there was no difference in stress response between male and female chickens. Moreover, despite of significant difference in some of HSPs expression level, it was considered that there was no difference in stress response between ages due to the inconsistent trends among HSP markers.

• Journal of Life Science
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• v.16 no.6
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• pp.1052-1059
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• 2006

The heat shock response is induced by environmental stress, pathophysiological state and non-stress conditions and wide spread from bacteria to human. Although translations of most proteins are stopped under a heat shock response, heat shock proteins (HSPs) are produced to protect cell from stress. When heat shock response is induced, conformation of HSF1 was changed from monomer to trimer and HSF1 specifically binds to DNA, which was called a heat shock element(HSE) within the promoter of the heat shock genes. Human HSF1(hHSFl) contains five cysteine(Cys) residues. A thiol group(R-SH) of Cys is a strong nucleophile, the most readily oxidized and nitrosylated in amino acid chain. This consideration suggests that Cys residues may regulate the change of conformation and the activity of hHSF1 through a redox-dependent thiol/disulfide exchange reaction. We want to construct role of five Cys residues of hHSF by redox reagents. According to two studies, Cys residues are related to trimer formation of hHSF1. In this study, we want to demonstrate the correlation between structural change and DNA-binding activity of HSF1 through forming disulfide bond and trimerization. In this results, we could deduce that DNA binding activity of DNA binding domain wasn't affected by redox for always expose outside to easily bind to DNA. DNA binding activity of wild-type HSF's DNA binding domain was affected by conformational change, as conformational structure change (trimerization) caused DNA binding domain.

• 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.

• Food Science and Preservation
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• v.21 no.6
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• pp.776-783
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• 2014

Kimchi cabbages were cut ($3{\times}3cm$), and were pre-heat treated at $40^{\circ}C$, and their physicochemical qualities and browning degrees were investigated during 8 weeks storage at $5^{\circ}C$. The Cut kimchi cabbages were treated at $40^{\circ}C$ (1~8 hrs) and their protein bands profiles were determined by sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE). The 60, 39, 33, and 12 kDa bands considered heat shock proteins (HSPs) were expressed in the cut kimchi cabbage, and the 4-hr pre-heat treatment (HS 4) exhibited the strongest band ratio. The weight ratios and titratable acidities of the pre-heat treated cut kimchi cabbages were not changed so much after 8 weeks storage at $5^{\circ}C$, and the soluble solid contents of HS 4 decreased less than that of any other treatments. The browning degree of HS 4 after 8 week storage was also shown to be the least among the treatments. The polyphenol oxidase (PPO) activities of all treatments slightly rose during the over all storage period, in contrast with the decrease of total phenolic contents. The expression of HSPs was identified in the pre-heat treated cut kimchi cabbages, and HS 4 exhibited the best quality and appearance after 8 weeks storage at $5^{\circ}C$.

• Korean Journal of Environmental Agriculture
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• v.32 no.1
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• pp.48-54
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• 2013

BACKGROUND: Sorghum (Sorghum bicolor (L.) Moench) ranks as the 6th most planted crop in the world behind wheat, rice, maize, soybean, and barley. The objective of this study was to identify bio-marker among sorghum cultivars using proteomics approach such as two-dimensional polyacrylamide gel electrophoresis (2-DE) coupled with mass spectrometry (MS). METHODS AND RESULTS: Proteins were extracted from sorghum seed, and separated by 2-DE. Total 652 spots were detected from 4 different sorghum seed after staining of 2-DE with colloidal Coomassie brilliant blue (CBB). Among them, 8 spots were differentially expressed and were identified using MALDI-TOF/TOF mass spectrometry. They were involved in RNA metabolism (spot1, spot 4), heat shock proteins (HSPs, spot 2), storage proteins (spot 3, spot 5, and spot 6), and redox related proteins (spot 8). Eight of these proteins were highly up-regulated in Whinchalsusu (WCS). The HSPs, Cupin family protein, and Globulin were specifically accumulated in WCS. The DEAD-box helicase was expressed in 3 cultivars except for WCS. Ribonuclease T2 and aldo-keto reductase were only expressed in 3 cultivars except for Daepung-susu (DPS). CONCLUSION(S): Functions of identified proteins were mainly involved in RNA metabolism, heat shock protein (HSP), and redox related protein. Thus, they may provide new insight into a better understanding of the charactreization between the cultivars of sorghum.

• Korean Journal of Biological Psychiatry
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• v.6 no.2
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• pp.202-208
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• 1999

Schizophrenia has many clinical expressions and probably different etiologic factors. Infections, autoimmune mechanism and related neurodevelopmental abnormalities have been suggested as possible etiologic factors of schizophrenia. It has been reported that immunoreactivity to heat shock proteins, which play a protective role against environmental stresses in a cell, might be related to the pathogenesis of schizophrenia. Therefore, we examined the immunoreactivity to heat shock protein 70kDa and 90kDa(HSP70 and 90) in 91 patients with schizophrenia and 83 normal controls. Ig G antibodies to HSP70 and 90 of sera were quantitated by ELISA. The optical density(OD) was measured by an automated microplate reader at a wavelength of 490nm. The amounts of antibodies to HSPs were expressed as arbitrary units(AU)/ml related to a standard serum. The limit for elevated antibody titers(anti-HSPs positive or negative) was set at two standard deviations added to the mean of the normal controls. Twenty nine(31.9%) of the 91 patients showed anti-HSP70 positive and 19(20.9%) of those showed anti-HSP90 positive. On the other hand, only 1(1.4%) of the normal controls and 4(4.8%) of those showed anti-HSP70 positive and anti-HSP90 positive, respectively. The titers of anti-HSP70 positive were related with BPRS scores, while those of anti-HSP90 positive were not. There were no relationship between antibody titers and clinical variables including age at onset, duration of illness, family history of schizophrenia or number of admission. The titers of anti-HSP70 positive were significantly associated with anti-HSP90 positive. Our results suggest the presence of abnormal immune reactivity involving HSP70 and HSP90 in a subset of patients with schizophrenia.

• Korean Journal of Clinical Laboratory Science
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• v.49 no.4
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• pp.460-469
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• 2017

Heat shock proteins (HSPs) are induced as a self-defense mechanism of cells when exposed to various external stresses, such as high fever, infection, free radicals, and heavy metals. They affect the prognosis in the process of tumor formation. HSP is classified into four families: HSP27, HSP60, HSP90, and HSP100, depending on molecular weight. Heat shock protein 90 (HSP90), a molecular chaperone, plays an important role in the cellular protection against various stressful stimuli and in the regulation of cell cycle progression and apoptosis. In the present study, we assessed the differential expression of HSP90 family proteins in non-small cell lung cancer (NSCLC), and the correlation of their expression levels with clinicopathologic factors and patient survival rates. The result of this study can be summarized as follows; $HSP90{\alpha}$ showed higher expression in patients with no lymphovascular invasion (p=0.014). $HSP90{\beta}$ showed a higher expression of squamous cell carcinoma (p=0.003), and an over expression of glucose-related protein (GRP94) was significantly associated with poor differentiation (p=0.048). However, none of the HSP90 proteins showed a significant association with the survival status in patients with NSCLC. This study also indicates that $HSP90{\alpha}$ might contribute more to the carcinogenesis of NSCLC than $HSP90{\beta}$, and GRP94 and isoform selectivity should be considered when HSP90 inhibitors are studied or utilized in the treatment of NSCLC.

• 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.

• Korean Journal of Poultry Science
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• v.46 no.2
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• pp.77-86
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• 2019

This study was conducted to compare the heat stress response and production performance of chicks hatched in winter and summer. Among the 2,090 Korean native chickens examined, 1,156 hatched in winter and 934 hatched in summer. The amount of telomeric DNA, the expression of heat shock protein (HSP) genes, survival rate, egg production, and body weight were analyzed to evaluate the stress response and production performance of chickens. The results showed that the expression of HSP-70, $HSP-90{\alpha}$, and $HSP-90{\beta}$ genes in the winter-hatched chickens were significantly higher than those in the summer-hatched chickens during the growing and laying period (P<0.05). There was no significant difference in the amount of telomeric DNA between summer- and winter-hatched chickens. The survival rate was significantly higher in the summer-hatched chickens than in the winter-hatched chickens at the laying period (P<0.01). The hen-day egg production and egg weight in the summer-hatched chickens were also significantly higher than those in the winter-hatched chickens (P<0.05). In contrast, age of sexual maturity of winter-hatched chickens was significantly earlier than that of summer-hatched chickens (P<0.01). The body weights from birth to 24 weeks were significantly lighter in the summer-hatched chickens than in the winter-hatched chickens, however, it was reversed after 28 weeks (P<0.05). In conclusion, the chicks hatched in the summer are more resistant to heat stress, with better productivity than the chicks hatched in the winter. These results suggest that the chicks grown at high temperatures have greater adaptability to the thermal environment.