• Clinical and Experimental Reproductive Medicine
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• 제25권3호
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• pp.305-313
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• 1998

Steroid hormone is known to cause the dynamic changes of mammalian uterus during reproductive cycle. However there is little information about the effect of estrogen (E) and progesterone (P) on the expression of various transcription factors involved in gene expression. Thus the present study was designed to demonstrate E and/or P-induced expression of c-Fos, CREB, ATF and HSP70 in rat uterus. Rats, ovariectomized (OVX) for two weeks, were divided into 6 experimental groups, 1) OVX, 2) OVX+V, 3) OVX+E, 4) OVX+P, 5) OVX+E+V, 6) OVX+E+P, and western blotting assay for nuclear extract and immunohistochemical staining were carried out for each experimental group. Treatment of E $(10{\mu}g)$ showed to increase the expression of c-Fos, CREB, ATF, and HSP70, and maximal expression was occured at $3\sim6$ hr after E administration. P (1mg) also increased, but much less than E, the expression of c-Fos, ATF, and HSP70. However, P did not reveal any effect on the expression CREE. P treatment 4 hr after E injection decreased c-Fos, CREB, and ATF expression, but did not show any change in the E-induced HSP70 expression. In immunohistochemical study c-Fos-, CREB-, and ATF-immunoreactivities were confined to the cells of luminal epithelium of uterine endometrium. These results suggest that proliferation and differentiation of rat uterus during reproductive cycle may mediated via expression of transcription factors, such as c-Fos, CREB, ATF, and HSP70.

• 한국해양생명과학회지
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• 제3권2호
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• pp.59-66
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• 2018

갯벌의 건강 수준에 대한 평가는 갯벌에 서식하는 생물의 건강에 의해 평가될 수 있다. 생체지표유전자의 발현 분석을 통하여 갯벌에 서식하는 생물의 건강 수준을 평가할 수 있다. 본 연구의 목적은 heat shock protein 70 (Hsp70), heat shock protein 90 (Hsp90), glutathione S-transferases (GST) 및 thioredoxin (TRX)과 같은 생체지표유전자를 이용하여 서해안 갯벌의 건강을 평가하는 것이다. 이들 유전자는 스트레스, 면역 및 항산화 관련한 유전자들로서 이들 유전자의 발현을 통해 생물의 건강 정도를 관찰하는 데 사용할 수 있다. 본 연구에서는 서해안의 8개 정점에서 바지락(Ruditapes philippinarum)을 수집했다. 유전자의 발현은 RT-qPCR 방법으로 분석하였다. 연구 결과 Hsp70, Hsp90, GST 및 TRX 유전자들의 발현이 8개 정점에서 차별적으로 발현되는 것으로 나타났다. 특히, Hsp90 및 GST의 발현 또는 Hsp70 및 TRX의 발현은 유사하였다. 이것은 각 유전자에 특이적으로 반응하는 물질이 존재하는 것으로 생각된다. 따라서 이화학적 분석결과에 근거하여 분석에 적합한 유전자를 선택할 수 있다고 생각한다. 이 결과는 Hsp70, Hsp90, GST 및 TRX 유전자는 갯벌의 건강을 평가하기 위한 생체지표유전자로서의 역할을 수행함을 시사한다.

• 한국발생생물학회지:발생과생식
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• 제14권3호
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• pp.179-184
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• 2010

Water temperature influences on various key biological events in fish, but the internal pathway of the temperature effects are not well understood. Heat shock proteins (HSPs), known to respond in the level of cells to many environmental factors including temperature, could improve our understanding on the pathway. Some biological processes such as gonadal development and sex differentiation in the Nile tilapia Oreochromis niloticus is particularly sensitive to water temperature. In this study, we have investigated the expressions of HSP70 and HSP90 genes in young tilapia at an ordinary temperature ($28^{\circ}C$) and elevated water temperature ($36^{\circ}C$). The distribution of the expressions of HSP70 and HSP90 mRNA in this species were found to be almost ubiquitous, being detected in all tissues studied here (brain, gonad, liver and muscle), suggesting the house keeping functions of these genes. Heat shock by elevating temperature from $28^{\circ}C$ to $36^{\circ}C$ significantly increased the expression of HSP70 mRNA in the gonad, liver and muscle for several hours (P<0.05) (brain tissue was not examined for this). The increased level of HSP70 gene expression recovered to the level at control temperature ($28^{\circ}C$) when fish were kept continuously at high temperature ($36^{\circ}C$) for 24 hours. Contrary to this, expression of HSP90 mRNA did not show significant increase in the gonad and muscle by the same heat shock (P>0.05), except in the liver where the expression of HSP90 mRNA increased continuously for 24 hours at $36^{\circ}C$. The results obtained in this study suggest that response to temperature change in different tissue or organ may utilize different heat shock proteins, and that HSP70 may have some importance in temperature-sensitive gonadal event in the Nile tilapia.

• 한국동물학회지
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• 제39권2호
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• pp.123-131
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• 1996

In this study, we examined the expression of heat shock proteins (HSPs) in fish cell line CHSE-2lnl and human HeLa cells exposed to heat shock. In fish CHSE-214 cells HSP70 was the major polvpeptide induced by an elevated temperature or an amino acid analog, while in HeLa cells HSP90 as well as HSP70 were prominently enhanced in response to these stresses. Pretreatment of actinomvcin D prior to heat shock completely inhibited the induction of fish HSP70, indicating the transcriptional regulation of fish HSP70 gene expression. In HeLa and CHSE-214 cells either recovering from heat shock or experiencing prolonged heat shock, attenuation in the HSP90 a'nd HSP70 induction occurred but both induction and repression of HSP70 synthesis appear 19 precede those of HSP90. Moreover, attenuation did not occur in the syntheses of 40 kDa and 42 kOto proteins which were only induced in CHSE-214 cells. The enhanced syntheses of these he proteins continued as long as CHSE-214 cells were Siven heat shock. These results suggest that down-regulation of HSP syntheses during prolonged heat shock may be controlled by several different. as vet undefined, mechanisms.

• 생태와환경
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• 제49권1호
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• pp.22-30
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• 2016

연안의 다양한 환경변화는 서식 생물에 영향을 미치고, 양식장의 생산량 감소와 연결되고 있는 추세이다. 본 연구에서는 가막만의 대표적인 양식종인 패류 C. gigas와 M. galloprovincialis의 서식환경에 따른 스트레스 정도를 파악하고자 하였다. 이를 위해, 각 종의 체중량, 각장과 각고, 양식장 사육기간을 조사하고, 각 종의 계통학적 HSP 70 sequence를 비교한 후, 각 종의 HSP 70 유전자 발현을 분석하였다. 그 결과, C. gigas의 체중량, 각장과 각고는 C2 양식장이 높게 나타났으나, 양식장 환경 사육기간과 HSP 70 유전자 발현은 C3 양식장이 가장 높았다. M. galloprovincialis는 M1 양식장의 체중량이 높게 나타났으며 각장과 각고, 사육기간은 M2와 유사하였으나, HSP 70 유전자 발현은 M2 양식장이 통계적으로 유의한 수준으로 높게 나타났다. 그리고 C. gigas와 M. galloprovincialis의 HSP 70 sequence 분석을 통해서 다른 해양 종들과 높은 유사성이 있음을 확인하였다. 이 결과는 서식환경에 따라 생물의 외부적 형질뿐만 아니라 내부적 스트레스를 HSP 70 유전자 발현을 통하여 파악할 수 있으며 HSP 70은 외부환경 스트레스를 평가하는 지표 유전자로서 활용할 수 있을 것이다.

• Journal of Genetic Medicine
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• 제1권1호
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• pp.51-56
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• 1997

Spermatogenesis is known to be regulated by a number of genes and several factors such as hormones, growth factors, cytokines and others. This study was done to evaluate the relationship between HSPs and DAZ genes in human spermatogenesis; we observed the expression pattern of HSP gene in azoospermia men with DAZ gene that regulated the gene expression related with human spermatogenesis. RT-PCR method was used to detect DAZ, HSP70A, and HSP70B transcripts in all RNA samples. Total RNA was extracted from 21 testis tissues using TRIZOL reagent. cDNAs were synthesized with reverse transcriptase, AMV. All PCR reaction were performed on a PCR themocycler with DAZ, HSP70A, and HSP70B-specific primers. Semen analysis, karyotyping and testis histology were performed. DAZ gene, known as a candidate gene of azoospermia factor(AZF), was deleted in 2 of 21 patients. To evaluate the only effects of HSPs in this patients, 2 DAZ deleted cases were removed. We observed the mRNA of HSP70B in 5 whereas none could be seen with regard to HSP70A. Furthermore, the sperm of these 5 men were discovered to be immature. In conclusion, HSP70B as well ad DAZ gene seem to be involved causing spermatogenic failure. We suggest that HSP70B plays an important role in spermatogenesis and it is one of factors induced sperm maturation in human.

• BMB Reports
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• 제45권5호
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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.

• 생명과학회지
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• 제15권4호
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• pp.607-612
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• 2005

열충격단백질 70 (HSP70)은 복수유전자족으로서 통상적으로 표현되는 Hsc70와 스트레스에 의하여 유도되는 Hsp70가 있다. 포유동물의 신경계통에서는 상당한 량의 HSP70가 정상조건에서도 표현되는 것으로 알려져 있다. 본 연구에서는 흰쥐의 소뇌 세포의 연접에서 Hsp70의 표현에 대한 연구를 하였다. 면역조직화학적으로 소뇌절편을 염색하여 관찰한 결과 Hsp70와 Hsc70 모두 표현되었는데, 소뇌 조롱박세포에서 가장 강하게 표현되었으며, 다음으로 소뇌 과립세포에서 강하게 표현되었다. 또한 깊은소뇌핵의 신경세포들도 강하게 염색되었다. 배양한 P1 소뇌신경 세포를 Hsp70 항체로 염색한 결과 Hsp70는 조롱박세포와 과립 세포에서 모두 표현되었으며, 세포체와 가지돌기를 따라 점박이를 형성하였다. 이들 점 박이들은 PSD95 점박이와 같이 위치하였다. 그리고 PSD 분획을 이용한 면역염색에서도 PSD70이 검출되었다. 본 연구결과는 Hsp70이 정상조건에서도 소뇌신경세포의 연접에 존재함을 의미한다.

• Asian Pacific Journal of Cancer Prevention
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• 제17권8호
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• pp.3929-3937
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• 2016

Gastric cancer (GC) is a major health problem worldwide and is one of the ten most commonly diagnosed cancers in Jordan. GC is usually diagnosed at late aggressive stages in which treatment options are limited. Recently, heat shock proteins (HSPs) were found to be overexpressed in a wide range of malignancies have been considered as promising candidate biomarkers for GC. The aim of this study was to investigate pathogenic roles of a panel of cytosolic HSPs including HSP90, HSP70, HSP60 and HSP27 in GC. Immunohistochemistry was used to assess the level of expression of these proteins in archived tumor samples (N=87) representing various pathological characteristics of GC. HSP90, HSP60 and HSP27 were expressed abundantly in gastric tumors. On the other hand, HSP70 was reduced significantly and also found to be associated with Helicobacter pylori infection in tissues collected from GC patients. Furthermore, HSP27 was found to be associated with the level of differentiation. Our findings indicate a role of HSP70 as a potential prognostic biomarker, patients harboring positive HSP70 expression displaying worse disease free survival than those with negative HSP70 expression. Differential expression of HSPs may play crucial roles in the initiation and progression of GC, and could be exploited as future therapeutic targets.

• Journal of Microbiology and Biotechnology
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• 제10권2호
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• pp.137-142
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• 2000

Environmental stres is known to induce heat shock proteins (HSPs) in eukaryotic cells. However, the induction of HSPs in host cells by microbial infection has not yet been well explained. Staphylococcus aureus (S. aureus) is one of the major pathogens in the pathogenesis of endovascular diseases such as infective endocarditis. In this study, the synthesis of stress-inducible 70 kDa HSP was investigated in the endothelial cells (ECs) after 3 h to 20 h of incubation with S. aureus. The dffect of S. aureus infection on the expression of HSP70 in cultured ECs was analyzed using laser scanning confocal microscopy (LSCM). The increase of HSP70 expression in ECs infected by S. aureus ($10^4{\;}cfu/ml$) for 20 h was 1.1-fold higher than that in heat shock treated ECs and 2.2-fold higher than that in untreated cells. Heat shock is known to induce intranucleus HSP70 expression in mammalian cells, whereas the S. aureus infection induced perinuclear expression in ECs as observed by LSCM. Consequently, the expression of HSP70 in ECs plays an important role in the pathogenesis of endovascular infection.