• BMB Reports
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• v.55 no.10
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• pp.488-493
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• 2022

The specific pair of heat shock protein 70 (Hsp70) and Hsp40 constitutes an essential molecular chaperone system involved in numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members are characterized by the presence of a conserved J-domain (JD) that functions as a co-chaperone of Hsp70. Tumorous imaginal disc 1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3 subfamily of Hsp40 and functions as a co-chaperone of the mitochondrial Hsp70, mortalin. In this work, we performed nuclear magnetic resonance spectroscopy to determine the solution structure of JD and its interaction with the glycine/phenylalanine-rich region (GF-motif) of human Tid1. Notably, Tid1-JD, whose conformation was consistent with that of the DNAJB1 JD, appeared to stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present results demonstrate that the functional and regulatory mode of Tid1 resembles that of the DNAJB1 subfamily members rather than DNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggested that an allosteric interaction between mortalin and Tid1 is involved in the mitochondrial Hsp70/Hsp40 chaperone system.

• Journal of Aquaculture
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• v.12 no.2
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• pp.91-100
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• 1999

The complete nucleotide sequence of olive flounder (Paralichthys olivaceus) hsp70-related rDNA was determined by RT- and RACE-PCR methods. A full-length of hsp70-related cDNA has an open reading frame of 1.95 kb encoding 650 amino acids with a calculated molecular weight of 71.1 kD. A corresponding hsp70-related protein contains a number of conserved elements including an ATP-binding domain, a nuclear localization signal and the carboxyl terminal motif, EEVD, which may have a role in chaperone function. Comparison of nucleotide and predicted amino acid sequence between olive flounder hsp70-related gene and hsp/hsc70 genes of other species revealed a high similarity with the cognate form of these genes. These results indicated that we recovered likely to be a olive flounder cognate hsc70 gene.

• Tuberculosis and Respiratory Diseases
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• v.44 no.1
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• pp.175-182
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• 1997

Several stresses are known to induce synthesis of heat shock protein The present study was performed to see whether pulmonary ischemia, induced by the bronchial artery occlusion, produced HSP70 in cat lung. To This aim, we compared experimental and control groups of cats with respect to the HSP70 production in the lung. Experimental animals were subjected to 10-min bronchial artery occlusion followed by reperfusion. The interval between the end of the occlusion and the end of the reperfusion was 1 hour, 4 hours and 8 hours, whereas control animal was not subjected 10 any manipulation except anesthesia. According to the interval differences, experimental animals were divided into 1HR, 4HRs and 8HRs groups. To determine The induction of HSP70 in each group, total proteins of lung tissues were extracted and separated by PAGE electrophoresis. Immunoblotting with a mouse monoclonal anti -HSP70 IgG antibody revealed that HSP70 was not detected in the pulmonary tissues resected from control, 1HR or 4HRs groups. In contrast. HSP70 expression in 8HRs group was marked. These results suggest that pulmonary ischemia by the bronchial artery occlusion produces HSP70 in a delayed manner.

• Korean Journal of Environmental Biology
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• v.21 no.3
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• pp.313-318
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• 2003

Environmental stresses, such as heat shock, alcohol and physiological salt have been shown to induce a group of protein called heat shock protein (HSPs) in various tissues. In this investigation, we studied that arsenic stress would alter contraction of isolated rat aorta and expression of heat shock protein 70 and investigated the relation between expression of HSP 70 and vascular contractility of isolated rat aorta. Rat aorta strips, mounted in organ baths were exposed to 0, 0.5, 1,2 and 4 mM arsonic for 60 min. and 1,3 and 8 hours later tested for contractile response and expression of heat shock protein 70. Contractility of rat aorta were determined by isometric transducer connected to computerized physiograph and expression of HSP 70 was characterized by western blotting, respectively. Potassium chloride (55 mM) significantly augmented vascular contractility of yat aorta by 39％ compared with the control at 8 hours but not one or three hours after treatment of 4 mM arsenic. Arsonic stress (4 mM) also increased the expression of HSP 70 in rat aorta at 8 hours but one or three hours compared with the control and HSP expressed in vascular smooth muscle cells and some expressed in endothelium cells. These results suggest that arsenic stress not only did alter the magnitude of the contractile response to high potassium chloride but also increased the expression of HSP 70 in the rat aorta.

• Maxillofacial Plastic and Reconstructive Surgery
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• v.23 no.2
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• pp.124-136
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• 2001

Heat shock protein (HSP) expression is unregulated in tumor cells and, HSP expression is likely marker of the malignant potential of oral epithelial lesion. Furthermore, the 70kDa HSP is implicated in the degree of tumor differentiation, the rate of tumor proliferation and the magnitude of the anti-tumor Immune response. Accordingly, the distribution and intensity of HSP70 and HSP47 expression was assessed in the DMBA induced oral carcinogenesis in hamster. Golden Syrian hamsters which were 3 months-age and $90{\sim}120g$ were collected. 9,10-dimethyl -1,2-benzanthracene (DMBA) in a 0.5% solution in mineral oil was painted on the buccal pouch mucosa 3 times per week in the study group. In each control and experimental groups of 6, 8, 10, 12, 14, 16, 18, 20 weeks, specimen were sectioned for immunohistochemical study with anti-HSP47 and anti-HSP70 antibody. The following results were obtained. 1. HSP47 positive cells were race or negative of normal oral mucosa, increased mildly in basal and suprabasal basal layer, and spinous cell layer after experimental 6 weeks (dysplastic or CIS stage). In CIS stage, HSP47 expression is prominent in dysplastic free or normal adjacent epithelium. 2. HSP47 positive cells in connective tissue were mainly inflammatory cells, which is gradually increased from control to precancerous and cancer stage. But HSP47 positive cells after 14 weeks were decreased, especially normal and cancer adjacent epithelium. 3. The positive staining cells of HSP70 in control, dysplastic, and CIS stage were not seen. But they were mild findings in basal layer and moderate findings in spinous layer after experimental 14 weeks (cancer stage). 4. HSP70 positive cells were increased in precancerous and cancer stage than control group in connective tissue. After experimental 16 weeks, we could not find the HSP expression in cancer cells according to cancer differentiation or cancer stage. It is concluded that HSP70 or HSP47 expression is not a definitive marker of oral malignancy or malignant potential. However, with further development, HSP immunoreactivity may be valuable as an adjunct to conventional histology for assessing the malignant potential of oral mucosal lesions.

• Maxillofacial Plastic and Reconstructive Surgery
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• v.20 no.4
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• pp.362-372
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• 1998

Heat shock protein (HSP) expression is unregulated in tumor cells and, HSP expression is likely marker of the malignant potential of oral epithelial lesion. Furthermore, the 70kDa HSP is implicated in the degree of tumor differentiation, the rate of tumor proliferation and the magnitude of the anti-tumor immune response. Accordingly, the distribution and intensity of HSP 70 and HSP 47 expression was assessed in the DMBA induced oral carcinogenesis in hamster. Golden Syrian hamsters which were 3 months-age and 90-120g were collected. 9,10-dimethyl-1,2-benzanthracene (DMBA) in a 0.5% solution in mineral oil was painted on the buccal pouch mucosa 3 times per week in the study group. In each control and experimental groups of 6, 8, 10, 12, 14, 16, 18, 20 weeks, specimen were sectioned for immunohistochemical study with anti-HSP47 and anti-HSP70 antibody. The following results were obtained. 1. HSP47 positive cells were rare or negative of normal oral mucosa, increased mildly in basal and suprabasal basal layer, and spinous cell layer after experimental 6 weeks (dysplastic or CIS stage). In CIS stage, HSP47 expression is prominent in dysplastic free or normal adjacent epithelium. 2. HSP 47 positive cells in connective tissue were mainly inflammatory cells, which is gradually increased from control to precancerous and cancer stage. But HSP47 positive cells after 14 weeks were decreased, especially normal and cancer adjacent epithelium. 3. The positive staining cells of HSP70 in control, dysplastic, and CIS stage were not seen. But they were mild findings in basal layer and moderate findings in spinous layer after experimental 14 weeks (cancer stage). 4. HSP70 positive cells were increased in precancerous and cancer stage than control group in connective tissue. After experimental 16 weeks, we could not find the HSP expression in cancer cells according to cancer differentiation or cancer stage. It is concluded that HSP70 or HSP47 expression is not a definitive marker of oral malignancy or malignant potential. However, with further development, HSP immunoreactivity may be valuable as an adjunct to conventional histology for assessing the malignant potential of oral mucosal lesions.

• The Korean Journal of Zoology
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• v.35 no.2
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• pp.203-210
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• 1992

Hsp70, a 70 kDa protein, is the maior protein expressed when cells are heat-shocked. A cDNA library from mouse ID13 cells was screened with the human hsp70 gene as a probe, and a positive clone was obtained. The positive clone was subcloned into puc19 and the precise restriction was obtained. The CDNA was sequenced by the Sanger's dideoxv termination method. Single open reading frame that codes for a protein of 70 kDa was found. The DNA sequence of the cloned mouse DNA shows great homology (66-90%) with other mouse hsp70 genes and somewhat less homology (50",) with E. coli hsp70 gene (dnak). With the exception of one amino acid, the protein sequence deduced from the CDNA is identical to the mouse that shock cognate protein 70 (hsc70) that is constitutivelv expressed at normal temperature. The result suggests that the cloned CDNA encodes a hsc70 family rather than a heatinducible family.mily.

• Journal of the Korean Society of Physical Medicine
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• v.8 no.1
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• pp.111-116
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• 2013

연구목적: 본 연구는 흰쥐를 대상으로 정강뼈의 관절연골에 적용한 맥동전자장과 맥동초음파가 HSP70(Heat shock protein 70)의 발현을 통한 연골 형성에 미치는 영향을 알아보고자 실시하였다. 연구방법: 36마리의 200~250g의 Sprague-Dawley 흰쥐를 대조군, 맥동전자장 적용군, 맥동초음파 적용군으로 각 집단별로 12마리씩 무작위 배정하여 실험을 진행하였다. 맥동전자장은 27.12 MHz의 주파수, 5가우스의 강도, 450 W의 출력으로 10분간 적용하였고, 맥동초음파는 20%의 맥동비, 1MHz의 주파수, $1.5W/cm^2$의 강도로 10분간 적용하였다. 연구결과: 맥동전자장 적용군과 맥동초음파 적용군의 관절연골 조직에서 유의한 수준의 HSP70 발현량을 나타냈다. 또한 맥동전자장 적용군과 맥동초음파 적용군에서는 Akt, Erk1, CREB의 높은 활성도를 나타내었고, 맥동초음파 적용군에 비해서 맥동전자장 적용군의 더 높은 수준의 활성도를 보였다. 결론: 맥동전자장과 맥동초음파는 HSP70의 과발현을 유발하고, 이를 통해 연골형성을 증가시키는 것으로 나타나, 향후 관절연골의 손상에 대한 임상적 적용을 위한 추가적인 연구가 진행되어야 할 것으로 생각된다.

• BMB Reports
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• v.44 no.3
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• pp.176-181
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• 2011

Inhibiting histone deacetylase (HDAC) activity modulates the epigenetic status of cells, resulting in an alteration of gene expression and cellular function. Here, we investigated the effects of HDAC inhibitors on mouse embryonic stem (ES) cells. The HDAC inhibitors trichostatin A, suberoylanilide hydroxamic acid, sodium butyrate, and valproic acid induced early differentiation of mouse ES cells and triggered induction of heat-shock protein (HSP)70. In contrast, class III HDAC inhibitors failed to induce differentiation or HSP70 expression. Transcriptional upregulation of HSP70 was confirmed by mRNA expression analysis, an inhibitor study, and chromatin immunoprecipitation. HSP70 induction was dependent on the SAPK/JNK, p38, and PI3K/Akt pathways. Differentiation and induction of HSP70 by a subset of HDAC inhibitors was also examined in human ES cells, which suggests that the phenomenon generally occurs in ES cells. A better understanding of the effects of HDAC inhibitors may give more insight into their application in stem cell biology.

• The Journal of Korean Medicine
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• v.23 no.2
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• pp.139-150
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• 2002

OBJECTIVES : Schizandra chinensis is well known for its efficacy at liver function reinforcement, relieving thirst and recovery from fatigue. In this study, we examined the effects of sports drink containing Schizandra chinensis on serum metabolic substrate, electrolyte, stress indicators, related-enzyme and exercise performance, rectal temperature, and heat shock proteinb70 (HSP70). METHODS : Elite long-distance runners (male, 21.3yrs, n=16) were selected and divided into two groups; an experimental group (EXP, n=8) and a control group (CON, n=8). A beverage containing Schizandra chinensis was supplemented 3 times per day to EXP for 4 weeks. Serum biochemical elements (glucose, lactate, total cholesterol, triglyceride, high density lipoprotein cholesterol, glutamate oxaloacetate transaminase, glutamate pyruvate transaminase, creatinine, creatine phosphokinase, lactate dehydrogenase, blood urea nitrogen, Na, K, Cl) were analyzed by auto blood analyzer. Exercise performance was measured by treadmill exercise test, HSP70 was detected by electrophoresis and Western blotting, and rectal temperature was measured by rectal temperature probe. RESULTS : Administration of the beverage increased significantly the rest level of blood Na, Cl and glucose and decreased significantly lactate dehydrogenase, glutamate oxaloacetate transaminase. No difference was found in exercise performance, rectal temperature increment or HSP70 concentration between groups. CONCLUSIONS : Administration of a sports drink containing Schizandra chinensis altered blood glucose, lactate dehydrogenase, glutamate oxaloacetate transaminase, Na and Cl levels.