• 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.

• Toxicological Research
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• v.13 no.1_2
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• pp.79-86
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• 1997

Inhibitory effects of tannic acid on skin toxicity and heat shock protein induced by UVB were investigated. Tannic acid was administered either topically or orally for 3 days to hairless mice, which were previously irradiated with UVB. UVB was found to cause skin erythema . However, the skin erythema was decreased when tannic acid was administered either topically or orally. The heat shock proteins, Hsp-78 kDa and 70 kDa, were induced by UVB irradiation, but the induction was decreased by treatment of tannic acid in both topically and orally administered groups. The hsp induction was more prominent in orally administered groups than in topically administerd groups. However, the difference between two groups was not statistically significant. The route of administrations, topical and oral, does not affect the activity of tannic acid. In the skin tissue observation, tannic acid regenerated the epithelial cells with 7-9 cell layers which were injured by UVB. In conclusion, tannic acid has an ability to protect against UVB irradiation and regenerate the skin.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.25 no.8
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• pp.1096-1101
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• 2012

Intrauterine growth retardation (IUGR) leads to the dysfunction in digestive system, as well as the alteration in the expression of some functional proteins. Heat shock protein 70 (Hsp70) could be induced by various stress factors, but whether Hsp70 expression is changed in neonatal IUGR infants has not been demonstrated. This study was conducted to explore the expression of Hsp70 in the liver by using the IUGR piglet model. Liver and plasma samples were obtained from IUGR and normal birth weight (NBW) piglets at birth. The neonatal IUGR piglets had significantly lower liver weight than their counterparts. The activities of aspartate aminotransferase and alanine aminotransferase in serum were enhanced significantly in IUGR indicating liver dysfunction. The activities of superoxide dismutase (p<0.01), glutathione peroxidase (p<0.01) and catalase (p>0.05) were lower and the level of malondialdehybe was higher (p<0.05) in IUGR liver compared with in NBW. According to the results of histological tests, fatty hepatic infiltrates and cytoplasmic vacuolization were present in the liver of IUGR piglets, but not in NBW liver. The expression of Hsp70 protein was significantly higher (p<0.05) in IUGR piglet liver than in NBW. Similar to where the hepatic injuries were observed, location of Hsp70 was mostly in the midzonal hepatic lobule indicating that oxidative stress might be responsible for the increased expression of Hsp70.

• BMB Reports
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• v.45 no.5
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• pp.299-304
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• 2012

The ubiquitin-proteasome system is a major proteolytic system for nonlysosomal degradation of cellular proteins. Here, we investigated the response of mouse embryonic stem (ES) cells under proteotoxic stress. Proteasome inhibitors induced expression of heat shock protein 70 (HSP70) in a concentration- and time-dependent manner, and also induced apoptosis of ES cells. Importantly, more apoptotic cells were observed in ES cells compared with other somatic cells. To understand this phenomenon, we further investigated the expression of HSP70 and pluripotent cell markers. HSP70 expression was more significantly increased in somatic cells than in ES cells, and expression levels of pluripotent cell markers such as Oct4 and Nanog were decreased in ES cells. These results suggest that higher sensitivity of ES cells to proteotoxic stress may be related with lower capacity of HSP70 expression and decreased pluripotent cell marker expression, which is essential for the survival of ES cells.

• 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.

• Applied Microscopy
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• v.37 no.3
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• pp.167-174
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• 2007

Heat shock protein (HSP) 70 functions as a molecular chaperon and reduces stress-induced denaturation and aggregation of intracellular proteins. Erythropoietin (EPO) plays an important role during acute renal failure repair process by rapidly correcting anemia and enhancing renal tubular regeneration. The purpose of this study was to examine the effect of EPO treatment on renal HSP70 expression. Male Sprague-Dawley rats were injected rHUEPO. Kidney were preserved by in vivo perfusion with paraformaldehyde-lysine-periodate (PLP) and processed for immunohistochemistry and electron microscopy. In control kidney, HSP70 was expressed in the cortex, outer medulla and inner medulla. Especially, HSP immunoreactiviy was mainly founded in descending thin limb of outer medulla and inner medullary collecting duct. In EPO treated kidney, HSP70 expression markedly increased in the descending thin limb of outer medulla and newly detected in cortical collecting duct. Electron microscopy showed the presence of HSP immunoreactivity on the intracelluar vesicles and Golgi complex of descending thin limb and cortical collecting duct. These findings suggest that EPO treatment leads to new production of HSP70 in renal tubular cells, and induction of HSP70 by rHuEPO is causally related to protective function.

• BMB Reports
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• v.38 no.1
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• pp.111-114
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• 2005

Heat shock proteins (HSPs) are known to protect cells from oxidative stress and other types of injuries. We previously reported the neuroprotective effect of HSP70 following cerebral ischemia and reperfusion using hsp 70.1 knockout (KO) mice. However, the precise role of HSP70 in neuroprotection has not been established yet. The purpose of this study was to investigate the relationship between HSP70 and antioxidant enzymes using hsp 70.1 KO mice. The activities of both SOD-1 and SOD-2 were significantly decreased in hsp 70.1 KO mice than in the wild type (WT) littermates. SOD-1 protein level in the hsp 70.1 KO mice was lower than that of WT. We speculate that HSP70 might be involved in regulation of expression of SOD-1 at the level of transcription or by post-transcriptional modification.

• Genomics & Informatics
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• v.11 no.1
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• pp.52-54
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• 2013

Proteins in DNAJ/K families are ubiquitous, from prokaryotes to eukaryotes, and function as molecular chaperones. For systematic phylogenomics of the DNAJ/K families, we developed the Eukaryotic DNAJ/K Database (EDD). A total of 12,908 DNAJs and 4,886 DNAKs were identified from 339 eukaryotic genomes in the EDD. Kingdom-wide comparison of DNAJ/K families provides new insights on the evolutionary relationship within these families. Empowered by 'class', 'cluster', and 'taxonomy' browsers and the 'favorite' function, the EDD provides a versatile platform for comparative genomic analyses of DNAJ/K families.

• Journal of Life Science
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• v.11 no.5
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• pp.464-469
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• 2001

A gene, dnaK2, encoding a distinct member of the HSP70 family of molecular chaperones is isolated from the halotolerant cyanobactrium Aphanothece halophytica. The dnak2 gene encodes a molecular wight of 68 kDa polypeptide with predicted 616 amino acid residues. The DnaK2 protein has a structural characteristic of bacterial DnaK homologues and shows high similarity to other HSP70/Dank proteins. The danK2 transcripts are hardly detectable at 28$^{\circ}C$ and strongly induced upon heat stress. It is also found that dnaK2 transcript is increased by high-salinity stress even in the absence of heat stress. These results suggest that the DnaK2 protein plays an important role in protecting A. halophytica against damage caused by salt stress at well as heat stress.