• 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.

• Molecules and Cells
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• 제23권2호
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• pp.123-131
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• 2007

Extracellular stresses induce heat shock response and render cells resistant to lethal stresses. Heat shock response involves induction of heat shock proteins (Hsps). Recently the roles of Hsps in neurodegenerative diseases and cancer are attracting increasing attention and have accelerated the study of heat shock response mechanism. This review focuses on the stress sensing steps, molecules involved in Hsps production, diseases related to Hsp malfunctions, and the potential of proteomics as a tool for understanding the complex signaling pathways relevant to these events.

• Animal cells and systems
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• 제4권2호
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• pp.181-186
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• 2000

The expression of $p21^{WAF1/ClP1/SDl1}$, one of the cyclin-dependent kinase inhibitors, is regulated by a variety of transcription factors including p53 and STAT. Heat shock induces the expression of p21 in a temperature- and time-dependent manner. Although the p21 induction by heat shock has been reported to be controlled by p53, a p53-independent mechanism Is also involved. To understand the p53-independent regulation of heat shock-induced p21 expression, we searched the promoter region of p21 gene and found one or two heat shock element (HSE)-like sequences in human, rat, and mouse. Electromobility shift assay (EMSA) showed that heat shock factor (HSF) could bind to these HSE-like sequences In response to heat shock, even though to a lesser extent than to HSE. In addition, p21 promoter deletion analysis revealed that heat shock activated a p21 deletion promoter construct containing the HSE-like sequences but lacking p53-binding sites, but not a promoter construct containing neither HSE-like sequences nor the p53-responsive element. Furthermore, the p21 induction by heat shook was significantly inhibited in confluent cells in which heat shock-induced HSF activation was reduced. These results suggest that the transcriptional regulation of p21 by heat shock may be mediated through activation and binding to HSE-like sequences of HSF.

• 미생물학회지
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• 제29권1호
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• pp.49-55
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• 1991

The heat shock responses of Campylobacter jejuni were studied by examination of their survival rates and synthesis of heat shocd proteins. When C. jejuni cells were treated at the sublethal temperatures of 48.deg.C for 30 minutes, most of the cells maintained their viabilities and synthesized the heat shock proteins of 90, 73, and 66 kD in molecular weight. By the method of two-dimensional electrophoresis, the heat shock proteins of C. jejuni were identified to be Hsp90, Hsp73, and Hsp66. During the heat shock at 48.deg.C, the heat shock proteins were induced from about 5 minutes after the heat shock treatment. Their synthesis was continued upto 30 minutes, but remarkably retarded after 50 minutes. When C. jejune cells were heat shocked at 51.deg.C for 30 minutes, the survival rates of the cells were decreased by about $10^{3}$ fold and synthesis of heat shock proteins and normal proteins was also generally retarded. The cells exposed to 55.deg.C for 30 minutes died off by more than $10^{5}$ cells and the new protein synthesis was not observed. But when C. jejuni cells were heat-shocked at the sublethal temperature of 48.deg.C for 15 to 20 minutes and then were exposed at the lethal temperature of 55.deg.C for 30 minutes, their viabilities were higher than those exposed at 55.deg.C for 30 minutes without pre-heat shock at 48.deg.C. Therefore, the heat shock proteins synthesized at the sublethal temperature of 48.deg.C in C. jejuni were thought to be responsible for thermotolerance. However, when C. jejuni cells heat-shocked at various ranges of sublethal and lethal temperatures were placed back to the optimum temperature of 42.deg.C, the multiplication patterns of the cells pretreated at different temperatures were not much different each other.

• BMB Reports
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• 제40권4호
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• pp.554-561
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• 2007

Shen and colleagues (Lin et al., 2004) have recently shown that overexpression of the Drosophila DNA methyltransferase 2 isoform C, dDnmt2c, extended life span of fruit flies, probably due to increased expression of small heat shock proteins such as Hsp22 or Hsp26. Here, I demonstrate with immunoprecipitations that overexpressed dDnmt2c interacts with endogenous Hsp70 protein in vivo in S2 cells. However, its C-terminal half, dDnmt2c(178-345) forms approximately 10-fold more Hsp70-containing protein complexe than wild-type dDnmt2c. Overexpressed dDnmt2c(178-345) but not the full length dDnmt2c is able to increase endogenous mRNA levels of the small heat shock proteins, Hsp26 and Hsp22. I provide evidence that dDnmt2c(178-345) increases Hsp26 promoter activity via two heat shock elements, HSE6 and HSE7. Simultaneously overexpressed Hsp40 or a dominant negative form of heat shock factor abrogates the dDnmt2c(178-345)-dependent increase in Hsp26 transcription. The data support a model in which the activation of heat shock factor normally found as an inactive monomer bound to chaperones is linked to the overexpressed C-terminus of dDnmt2c. Despite the differences observed in flies and S2 cells, these findings provide a possible explanation for the extended lifespan in dDnmt2c-overexpressing flies with increased levels of small heat shock proteins.

• 동의신경정신과학회지
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• 제11권1호
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• pp.37-46
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• 2000

We investigated the effects of lemon pure essential oils on the heat shock-induced apoptosis in human astrocyte cell line CCF-STTG1. In previous studies, hear shock has been reported to induce the apoptosis or programmed cell death through the activation of caspase-3. Treatment of CCF-STTG1 cells with heat shock markedly induced apoptotic cell death as determined by flow cytometry. Interestingly, pretreatment of CCF-STTG1 cells with lemon pure essential oils inhibited the heat shock-induced apoptosis. Lemon also inhibited the heat shock-induced apoptosis in primary cultured rat astrocytes. To determine whether lemon inhibits the heat shock-induced activation of these apoptotic proteases, activation of CPP32 was assessed by Western blotting. Consistent with flow cytometry, DNA fragmentation and giemsa staining, heat shock-induced activation of CPP32 was blocked by lemon pure essential oil. PARP, cysteine protease substrates were fragmented as a consequence of apoptosis by heat shock. Lemon oil inhibited the PARP fragmentation. This essential oil also inhibited the heat shock-induced activation of caspase-3. These results suggest that lemon pure essential oils may modulate the apoptosis through the activation of the ICE-like caspases.

• Journal of Periodontal and Implant Science
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• 제34권1호
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• pp.29-33
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• 2004

The present study was done to evaluate the environmental factors responsible for the expression of Porphyromonas gingivalis heat shock protein. The intensity of the heat shock protein gene expression was comparable to those seen by the heat shock ptreatment of the bacteria $(44^{\circ}C)$ when the bacteria was grown as a mixed culture or biofilm state at $37^{\circ}C$.

• 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.

• 미생물학회지
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• 제30권3호
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• pp.232-238
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• 1992

Campylobacter jejuni 에 열처리를 했을 때 그들의 생존성 및 열충격 단백질 합성의 양상과 더불어, dnaK 와 groESL 유전자를 이용하여 C. jejuni 의 열충격 유전자를 검출하여 그 특성을 E. coli 의 열충격 유전자와 비교하였다. C. jejuni 의 열충격 단백질은 48.deg.C 에서 가장 잘 발형되었으며, 48.deg.C 에서 30 분간의 처리중 세포들의 생존율은 떨어지지 않았다. C. jejuni 의 열충격 단백질로서의 Hsp90, Hsp66, Hsp60 이 합성되는 것을 SDS-PAGE 및 방사선사진법을 통해 확인하였다. dnaK 와 groESL 을 DNA 탐침자로 이용하여 Southern hybridization 한 결과, C. jejuni 의 열충격 유전자도 groESL 과 dnaK 유전자와 상동성을 가진 염기서열을 가지고 있었으나, 두 균주사이에는 열충격유전자를 내포하고 있는 DNA 상에서 제한효소의 절단부위에 차이가 있었다.

• 동의신경정신과학회지
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• 제11권2호
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• pp.1-9
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• 2000

In previous studies, heat shock has been reported to induce the apoptosis or programmed cell death through the activation of caspase-3. 1 investigated the effect of juniper pure essential oil on the heat shock-induced apoptosis in human astrocyte cell line CCF-STTGI. Treatment of the astrocytes with heat shock markedly induced apoptotic cell death. However, pretreatment of the astrocytes with juniper oil ingibited the heat shock-induced apoptosis. To determine whether juniper inhibits the heat shock-induced activation of these apoptotic proteases, activation of CPP32 was assessed by Western blotting. Consistent with flow cytometry. DNA fragmentation and giemsa staining, heat shock-induced activation of CPP32 was blocked by juniper oil. Poly(ADP-ribose) polymerase (PARP), cysteine protease substrates were fragmented as a consequence of apoptosis by heat shock. Juniper oil inhibited the PARP fragmentation. This juniper oil also inhibited the heat shock-induced activation of caspase-3. These results suggest that juniper oil may modulate the apoptosis through the activation of the interleukin-1-converting enzyme-like protease.