• 대한기관식도과학회지
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• 제7권1호
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• pp.24-28
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• 2001

Background and Objectives： Heat shock protein(HSP) 27 is a member of the small HSP family that plays a part in the epithelial cell growth and differentiation, wound healing. apoptosis and cell protection against inflammatory cytotoxic mediators. The expression of HSP27 was investigated in normal laryngeal tissue and squamous cell carcinoma of the larynx. Materials and Methods : We studied expression of HSP27 by Western blot on 20 patients of laryngeal squamous cell carcinoma. Results： HSP27 expressed in all normal and cancer tissues. In 9 cases(45%), expression of HSP27 more prominent in cancer tissue. Statistically, there were no significant difference in the expression of HSP27 in normal and cancer tissue, clinical stage and tumor differentiation. Conclusion 45% of cancer tissues was more prominent than normal tissue. But further studies on expression of HSP27 in laryngeal cancer and relationship with clinical parameter should be done.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• 제30권4호
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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.

• Oncology Letters
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• 제41권5호
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• pp.3119-3126
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• 2019

Redd1 is a stress response protein that functions as a repressor of mTORC1, a central regulator of protein translation, resulting in the inhibition of cell growth and metabolism. However, paradoxically, high Redd1 expression favors cancer progression and generates resistance to cancer therapy. Herein, we revealed that constitutive overexpression of Redd1 induced HSP27 and HSP70 expression in lung cancer cells. The expression of Redd1, HSP27 and HSP70 was highly increased in lung cancer tissues compared with that in normal lung tissues. Inhibition of HSP27 or HSP70 suppressed AKT phosphorylation, which was induced by constitutive overexpression of Redd1 and enhanced the inhibitory effects on viability of Redd1-overexpressing cells. Inhibition of AKT phosphorylation resulted in a decrease of HSP27 and HSP70 expression in Redd1-overexpressing cells. These data indicated that HSPs and AKT in Redd1-overexpressing cells positively regulated the function and expression of each other and were involved in lung cancer cell survival. Knockdown of HSP27, HSP70 or AKT enhanced ionizing radiation (IR) sensitivity, particularly in lung cancer cells in which Redd1 was stably overexpressed. Collectively, constitutive overexpression of Redd1 led to HSP27 and HSP70 induction and AKT activation, which were involved in lung cancer cell survival and resistance to IR, suggesting that Redd1 may be used as a therapeutic target for lung cancer.

• Nuclear Engineering and Technology
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• 제38권3호
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• pp.285-292
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• 2006

Thermoresistant (TR) clones of radiation-induced fibrosarcoma (RIF) cells have been reported to show an adaptive response to 1cGy of low dose radiation, and HSP25 and inducible HSP70 are involved in this process. In this study, to further elucidate the mechanism by which HSP25 and inducible HSP70 regulate the adaptive response, HSP25 or inducible HSP70 overexpressed RIF cells were irradiated with 1cGy and the cell cycle was analyzed. HSP25 or inducible HSP70 overexpressed cells together with TR cells showed increased G1 phase after 1cGy irradiation, while RIF cells did not. $[^3H]-Thymidine$ and BrdU incorporation also indicated that both HSP25 and inducible HSP70 are involved in G1 arrest after 1cGy irradiation. Molecular analysis revealed upregulation of p27Cip/Kip protein in HSP25 and inducible HSP70 overexpressed cells, and cotransfection of p27Cip/Kip antisense abolished the induction of the adaptive response and 1cGy-mediated G1 arrest. The above results indicate that induction of an adaptive response by HSP25 and inducible HSP70 is mediated by upregulation of p27Cip/Kip protein, resulting in low dose radiation-induced G1 arrest.

• 국제물리치료학회지
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• 제2권2호
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• pp.281-287
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• 2011

This research was attempted to seek for a positive approach within the framework of physical therapy instead of the drug treatment in the past, with regard to the ischemic brain injury in the early stage. Accordingly, the aim of this research is to observe the change of HSP27 and HSP70, the genes that are expressed in the early stage of brain injury and to investigate the effects of needle electrode electrical stimulation(NEES), upon applying NEES after ischemia. The experimental method is to give rise to global ischemia and apply NEES to 27 SD-Pat rats with the particulars of being eight-week-old, male, around 300g, and adapted to laboratory environment for more than a week, and divide them into three groups, that is, GV20 NEES group(n=9), L14 NEES group(n=9), no applied NEES global ischemia(GI) group(n=9), and then observe their changes of HSP27 and HSP70 at the time lapse of 6, 9 hr and 12 hr after ischemia, using immunohistochemistry methods. Upon observing through the immunohistochemistry method, it was noticed that there was a significant difference between the GV20 NEES group and the L14 NEES group as for HSP27 and there were significant differences among all groups as for HSP70(p<.05). Accordingly, it is supposed that the application of NEES after the outbreak of cerebral ischemia delay the apoptosis in the early ischemic part of forebrain or protect neurons against apoptosis.

• Maxillofacial Plastic and Reconstructive Surgery
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• 제30권1호
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• pp.11-21
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• 2008

Aim of the study: Thermal stress is a central determinant of osseous surgical outcomes. Interestingly, the temperatures measured during endosseous surgeries coincide with the temperatures that elicit the heat shock response of mammalian cells. The heat shock response is a coordinated biochemical response that helps to protect cells from stresses of various forms. Several protective proteins, termed heat shock proteins (hsp) are produced as part of this response. To begin to understand the role of the stress response of osteoblasts during surgical manipulation of bone, the heat shock protein response was evaluated in osteoblastic cells. Materials & methods: With primary cell culture studies and ROS 17/2.8 osteoblastic cells transfected with hsp27 encoding vectors culture studies, the thermal stress response of mammalian osteoblastic cells was evaluated by immunohistochemistry and western blot analysis. Results: Immunocytochemistry indicated that hsp27 was present in unstressed osteoblastic cells, but not fibroblastic cells. Primarily cultured osteoblasts and fibroblasts expressed the major hsp in response to thermal stress, however, the small Mr hsp, hsp27 was shown to be a constitutive product only in osteoblasts. Creation of stable transformed osteoblastic cells expressing abundant hsp27 protein was used to demonstrate that hsp27 confers stress resistance to osteoblastic cells. Conclusions: The demonstrable presence and function of hsp27 in cultured bones and cells implicates this protein as a determinant of osteoblastic cell fate in vivo.

• Journal of Gastric Cancer
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• 제4권3호
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• pp.169-175
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• 2004

Purpose: The tumor suppressor gene p53 has been shown to be a factor in the carcinogenesis or progression of gastric cancer. The mutant p53 has been reported to cause a higher risk of lymph-node metastasis. Futhermore, mutation of the p53 has been linked to a poor prognosis for gastric cancer. The heat shock protein-27 (HSP27), a stress protein, has also been reported to be a poor prognostic factor in ovarian and breast cancers. However, in gastric-cancer patients, controversies exist as to its influence on the prognosis. In the present study, we used an immunohistochemical stain to observe the effects of p53 and HSP27 on the clinicopathological factors and on the prognosis for gastric-cancer patients. Materials and Methods: To evaluate the significance of p53 and HSP27 in gastric cancer patients, we analyzed 212 cases of gastric cancer (stage I.IV). Tissue samples of 212 patients were stained immunohistochemically for the mutant p53 protein and for HSP27. The correlations between protein expression and the clinicopathological factors were investigated. Results: The overall expression rates for p53 and HSP27 were $36.9\%\;and\;27.8\%$, respectively. p53 and HSP27 were correlated to each other because the HSP27 expression rate was higher in the p53-positive group (P=0.046). Statistically, the p53 and the HSP27 expression rates were significantly increased in the case of tumor invasiveness, lymphatic metastasis and vessel involvement. Therefore, they play a role in cancer progression. The 5-year survival rates of the p53-positive and the p53-negative groups were $62.8\%\;and\;60.1\%$, respectively (P=0.793) while the 5-year survival rates for the HSP27-positive and HSP27-negative groups were $54.2\%\;and\;63.1\%$, respectively (P=0.090). Conclusion: p53 and HSP27 were correlated to each other in our immunohistochemical study of gastric carcinomas and they were not independent prognostic factors in gastric- cancer patients. However, further studies are needed to determine their prognostic values for gastric-cancer patients.

• Fisheries and Aquatic Sciences
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• 제2권1호
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• pp.85-92
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• 1999

We examined the expression patterns of heat shock proteins in primary cultured hepatocytes from flounder (Paralichthys olivaceus) exposed to heat shock. The expression of hsp90, hsp70, hsp40, hsp30, and hsp27 was induced and major polypeptides were hsp70, hsp30 and hsp27. Northern blot analysis showed that expression of hsp70 was inhibited by transcriptional inhibitor actinomycin D, suggesting that expression of hsp70 gene is regulated at the transcriptional level. Prolonged exposure of cells to an elevated incubation temperature $(30^{\circ}C)$ induced the transient synthesis of hsp90, hsp70, hsp40, and hsp30 whereas maintenance of cells at a slightly higher incubation temperature $(32^{\circ}C)$ induced the continuous syntheses of these hsps. When cells were incubated at a higher temperatures $(35^{\circ}C\;or\;37^{\circ}C)$, the synthesis of hsps was almost similar to that of hsps in cells exposed to 32't except for the induction of hsp27 synthesis. These results that temperature and incubation time for optimum expression of each hsp during prolonged heat shock are different.

• Molecules and Cells
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• 제27권5호
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• pp.533-538
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• 2009

Heat shock protein 27 (Hsp27) is a molecular chaperone protein which regulates cell apoptosis by interacting directly with the caspase activation components in the apoptotic pathways. With the assistance of the Tat protein transduction domain we directly delivered the Hsp27 into the myocardial cell line, H9c2 and demonstrate that this protein can reverse hypoxia-induced apoptosis of cells. In order to characterize the contribution of Hsp27 in blocking the two major apoptotic pathways operational within cells, we exposed H9c2 cells to staurosporine and cobalt chloride, agents that induce mitochondria-dependent (intrinsic) and -independent (extrinsic) pathways of apoptosis in cells respectively. The Tat-Hsp27 fusion protein showed a greater propensity to inhibit the effect induced by the cobalt chloride treatment. These data suggest that the Hsp27 predominantly exerts its protective effect by interfering with the components of the extrinsic pathway of apoptosis.

• Bulletin of the Korean Chemical Society
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• 제31권9호
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• pp.2649-2655
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• 2010

$PKC{\delta}$-catalytic V5 Heptapeptide (FEQFLDI, FP7) interacts with heat shock protein 27 (HSP27) and inhibits HSP27-mediated resistance to cell death against various stimuli including radiation therapy. Here, we prepared radio-iodinated heptapeptide and further investigated its uptake properties in HSP27 expression cells. Peptide sequence of FP7 and a negative control peptide (WSLLEKR, QP7) was modified by substituting their C-terminus residue to tyrosine (FP6Y and QP6Y) to label radio-iodine. Iodinated peptides were confirmed by LC mass analysis with cold iodine reaction mixture. Accumulation of [$^{125}I$]iodo-FP6Y and [$^{125}I$]iodo-QP6Y in NCI-H1299 cell line, with higher level of HSP27, and NCI-H460 cell line, with lower level of HSP27, was measured by NaI(Tl) scintillation counter. The modification of substituting C-terminus residue of FP7 to tyrosine (FP6Y) did not affect its interaction with HSP27. Accumulation of [$^{125}I$]iodo-FP6Y in NCI-H1299 cells was 3 fold higher than in NCI-H460 cells. The novel radio-iodinated FP6Y would be used as a tracer for targeting HSP27 protein.