• 한국해양생명과학회지
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• 제5권2호
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• pp.92-98
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• 2020

Heat shock proteins (HSPs) are highly conserved cellular proteins that contribute to adaptive responses of organisms to a variety of stressors. In response to stressors, cellular levels of HSPs are increased and play critical roles in protein stability, folding and molecular trafficking. The mRNA expression pattern of two well-known heat shock protein transcripts, HSP70 and HSP90 were studied in two tissues of nerve ganglia, cerebral ganglion and pleuropedal ganglion of Pacific abalone (Haliotis discus hannai). It was observed that both HSP70 and HSP90 transcripts were upregulated under heat stress in both ganglion tissues. Expression level of HSP70 was found higher than HSP90 in both ganglia whereas cerebral ganglion showed higher expression than pleuropedal ganglion. The HSP70 and HSP90 showed higher expression at Day-1 after exposed to heat stress, later decreased at Day-3 and Day-7 onwards. The present result suggested that HSP70 and HSP90 synthesize in nerve ganglion tissues and may provide efficient protection from stress.

• 한국발생생물학회지:발생과생식
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• 제19권3호
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• pp.135-144
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• 2015

Heat shock protein (HSP) 70, the highly conserved stress protein families, plays important roles in protecting cells against heat and other stresses in most animal species. In the present study, we identified and characterized four Hsp70 (RuHSP4, RuHSC70, RuHSP12A, RuGRP78) family proteins based on the expressed sequence tag (EST) analysis of the Korean rose bitterling R. uyekii cDNA library. The deduced RuHSP70 family has high amino acid identities of 72-99% with those of other species. Phylogenetic analysis revealed that RuHsp70 family clustered with fish groups (HSP4, HSC70, HSP12A, GRP78) proteins. Quantitative RT-PCR analysis showed the specific expression patterns of RuHsp70 family members in the early developmental stages and several tissues in Korean rose bitterling. The expression of 4 groups of Hsp70 family was detected in all tested tissue. Particularly, Hsp70 family of Korean rose bitterling is highly expressed in hepatopancreas and sexual gonad (testis and ovary). The expression of Hsp70 family was differentially regulated in accordance with early development stage of Rhodeus uyekii.

• Journal of Microbiology and Biotechnology
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• 제31권8호
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• pp.1069-1078
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• 2021

Sevoflurane postconditioning (SPostC) has been proved effective in cardioprotection against myocardial ischemia/reperfusion injury. It was also reported that heat shock protein 70 (HSP70) could be induced by sevoflurane, which played a crucial role in hypoxic/reoxygenation (HR) injury of cardiomyocytes. However, the mechanism by which sevoflurane protects cardiomyocytes via HSP70 is still not understood. Here, we aimed to investigate the related mechanisms of SPostC inducing HSP70 expression to reduce the HR injury of cardiomyocytes. After the HR cardiomyocytes model was established, the cells transfected with siRNA for HSP70 (siHSP70) or not were treated with sevoflurane during reoxygenation. The lactate dehydrogenase (LDH) level was detected by colorimetry while cell viability and apoptosis were detected by MTT and flow cytometry. Reverse transcription-quantitative polymerase chain reaction (RT-qPCR) and Western blotting were used to detect HSP70, apoptosis-, cell cycle-associated factors, iNOS, and Cox-2 expressions. Enzyme-linked immuno sorbent assay (ELISA) was used to measure malondialdehyde (MDA) and superoxide dismutase (SOD). SPostC decreased apoptosis, cell injury, oxidative stress and inflammation and increased viability of HR-induced cardiomyocytes. In addition, SPostC downregulated Bax and cleaved caspase-3 levels, while SPostC upregulated Bcl-2, CDK-4, Cyclin D1, and HSP70 levels. SiHSP70 had the opposite effect that SPostC had on HR-induced cardiomyocytes. Moreover, siHSP70 further reversed the effect of SPostC on apoptosis, cell injury, oxidative stress, inflammation, viability and the expressions of HSP70, apoptosis-, and cell cycle-associated factors in HR-induced cardiomyocytes. In conclusion, this study demonstrates that SPostC can reduce the HR injury of cardiomyocytes by inducing HSP70 expression.

• 한국수정란이식학회지
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• 제20권3호
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• pp.289-295
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• 2005

본 연구는 돼지에서 스트레스 관련 HSP70 유전자의 다형성과 IVF 수정란의 배발달간의 관련성을 조사하기 위하여 수행되었으며 그 결과는 다음과 같다. HSP70-K1, -K3 및 -K4의 PCR 산물로부터 SSCP 다형성은 각각 다르게 확인되었다. 체외수정란의 분할율 시험에서 HSP70 K1-AA($73.1\%$) 및 K1-AB($62.3\%$) 난할율은 HSP70 K1-BB($49.3\%$)보다 유의적으로 높게 나타났다(p<0.05). 또한 HSP70 K3-AA($72.4\%$) and K3-AB($62.2\%$)형도 HSP70 K3-BB($49.1\%$)형보다 유의적으로 높았다(p<0.05). 돼지품종들과 정자의 HSP70 유전자형에 따른 2-cell 단계까지의 체외수정란 배발달은 유의적 차이를 보였다. Landrace(28.8)와 Duroc(29.8)에서 2세포기까지 발달된 수정란의 수는 Yo.kshire(10.9) 보다 유의적으로 높았다(p<0.05). 또한 HSP70 K4-AB(29.6)형의 2세포기 단계까지의 배발달 수정란 수는 HSP70 K4-AA(10.6)형보다 유의적으로 높았다(p<0.05). 그러나 돼지 품종 및 HSP70 유전자형에 따른 배반포기까지 수정란 배발달 정도는 유의적 차이는 없었다. 이러한 결과들은 돼지 체외수정란의 초기 배발달은 HSP70 유전자형과 품종에 따라서 영향을 받는 것으로 확인되었다.

• 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.

• BMB Reports
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• 제39권6호
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• pp.749-758
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• 2006

The cytosolic members of the HSP70 family of proteins play key roles in the molecular chaperone machinery of the cell. In the study we cloned and sequenced the full-length cDNA of Delia antiqua HSP70 gene, which is 2461 bp long and encodes 643 a.a. with a calculated molecular mass of 70,787 Da. We investigated gene copies of cytosolic HSP70 members of 4 insect species with complete genome available, and found that they are quite variable with species. In order to characterize this protein we carried out an alignment and a phylogenetic analysis with 41 complete protein sequences from insects. The analysis divided the cytosolic members of the family into two classes, HSP70 and HSC70, distinguishable on the basis of 15 residues. HSP70 class members were slightly shorter in length and smaller in molecular mass relative to the HSC70 class members, and the conservative and functional regions in these sequences were documented. Mainly, we investigated the expression of Delia antiqua HSP70 gene, in response to diapauses and thermal stresses. Both summer and winter diapauses elevated HSP70 transcript levels. Cold-stress led to increased HSP70 expression levels in summer- and winter-diapausing pupae, but heat-stress elevated the levels only in the winter-diapausing pupae. In all cases, the expression levels, after being elevated, gradually decreased with time. HSP70 expression was low in non-diapausing pupae but was up-regulated following cold- and heat-stresses. Heat-stress gradually increased the mRNA level with time whereas cold-stress gradually decreased levels after an initial increase.

• 한국수산과학회지
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• 제53권4호
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• pp.515-523
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• 2020

Basal and heat shock-induced mRNA expression patterns of major heat shock protein (HSP) genes, including those encoding heat shock protein (HSP) 90, HSP70, HSP70-12A, heat shock inducible protein 70 (HSIP70), heat shock binding protein 1 (HSPBP1), HSP60, and HSP40 were examined in the gill and hepatopancreas of 1-year-old diploid and triploid abalone Haliotis discus hannai juveniles. Under non-stimulated conditions at 19℃, triploid abalones displayed, in general, higher mRNA levels of various HSPs (HSP70, HSIP70, HSPBP1, HSP70-12A, and HSP60 in the gill and HSIP70, HSPBP1, and HSP60 in the hepatopancreas) than did communally cultured diploids. Conversely, only the hepatopancreatic expression of HSP70-12A was higher in diploids than in triploids. However, the fold changes in gene expression in response to an acute thermal challenge (elevation from 19 to 30℃) were generally greater in diploids than in triploids, such that the difference in basal expression was diminished, weakened, or even reversed after heat shock treatment. However, unlike other HSP genes, the basal expression of HSP60 (higher in 3N) was more pronounced after heat shock treatment. Collectively, the results of this study suggest that triploid abalones have different capacities for not only basal expression but also the heat-induced expression of HSPs in an HSP member-dependent manner.

• 생물정신의학
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• 제12권2호
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• pp.136-142
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• 2005

Object:The intracellular action of the antidepressant, venlafaxine, was studied in C6-gliomas using heat shock protein 70(HSP70) immunocytochemistry and HSP70 Western blots because HSP70 is associated with stress and depression. Methods:To examine how the glucocorticoid affects the expression of HSP70 in nerve cells, the rat C6 glioma cell was treated with dexamethasone for 6 hours. In addition, venlafaxine was administered to the experimental groups of C6 glioma cells for 1, 6, 24, and 72 hours each, after which the expression of HSP70 was investigated. Finally, venlafaxine and dexamethasone were simultaneously administered to the experimental groups for 1, 6, 24, and 72 hours, followed by an investigation of the expression of HSP70. Results:The short term(1 hour) venlafaxine treatment significantly increased the level of HSP70 expression. The short term treatment of venlafaxine with dexamethasone also increased the level of HSP70 expression but this reduction was not statistically significant. The long term(72 hours) venlafaxine with dexamethasone treatment significantly reduced the level of HSP70 expression. The long term treatment of venlafaxine also reduced the level of HSP70 expression but this reduction was not statistically significant. Dexamethasone(10uM, 6hours) did not affect the level of HSP70 expression compared with controls. Conclusion:Venlafaxine increases the expression of HSP70 at short term treatment, but prolonged treatment with dexamethasone suppresses the expression of HSP70.

• 동의생리병리학회지
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• 제18권1호
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• pp.167-171
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• 2004

This study investigated a HSP70 expression of Puerariae Radix in cerebral ischemia. The global cerebral ischemia was induced by bilateral common carotid arteries occlusion under hypotension (40 mmHg) in Sprague-Dawley rats. After the treatment of Puerariae Radix extract, the heat shock protein 70 (HSP70) expressions were measured immunohistochemically. The upregulation of HSP70 expression in hippocampal regions resulted by cerebral ischemia. Then Puerariae Radix treatment demonstrated significant decrease of HSP70 expressions in CA1 region and dentate gyrus of the hippocampus as compared with control group. These results suggested that Puerariae Radix reveals the neuroprotective effect through the control of noxious stress stimulations to neurons.

• International Journal of Industrial Entomology and Biomaterials
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• 제16권1호
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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.