• 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.

• BMB Reports
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• 제31권2호
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• pp.201-208
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• 1998

Amino acid analogs, like other inducers of stress response, induce the synthesis of stress proteins in mammalian cells. In this study, Drosophila Kc cells, in which translation is tightly controlled during stress response, was treated with proline analogs, L-azetidine-2-carboxylic acid (AzC) and 3,4-dehydro-L-proline (dh-P). Kc cells exposed to AzC or dh-P induced the synthesis of several proteins which had the same molecular weights as known heat shock proteins. However, in Kc cells, normal protein synthesis still continued in the presence of amino acids analogs unlike in heat-shocked cells. For the induction of stress response, the incorporation of dh-P into the protein was not essential, but the incorporation of AzC was. The stress protein synthesis was regulated mainly at the transcriptional level by AzC, whereas it was regulated by dh-P at the transcription level and possibly posttranscription level. During recovery, the stress protein synthesis stopped sooner in analog-treated cells than in heat-shocked cells even though the accumulated amount of Hsp70 was much less in proline analogstreated cells. It could be concluded that the proline analogs, AzC and dh-P, induced stress response through a different mechanism from heat shock.

• 한국동물학회:뉴스레터
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• 제12권2호
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• pp.113.2-113
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• 1995

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
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• 한국동물학회 1995년도 한국생물과학협회 학술발표대회
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• pp.249.2-249
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• 1995

No Abstract, See Full Text

• 한국초지조사료학회지
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• 제31권2호
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• pp.99-106
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• 2011

프로테오믹스 기법을 이용하여 벼 고온 스트레스 관련 단백질을 분리 동정하기 위하여 $42^{\circ}C$에서 고온처리한 벼의 줄기로부터 단백질을 분리하였다. 분리한 단백질로부터 Rubisco 단백질을 제거하기 위해 15% PEG fractionation을 실시한 후 상등액 분획의 단백질을 이차원전기 영동한 후, CBB 염색을 통해 차별적 발현을 보이는 단백질을 분석하였다. 총 46개의 단백질 spot이 발현양에 변화를 보였으며, 그 중 24개의 단백질이 고온 스트레스에 의해 발현이 증가되었으며, 22개의 단백질이 감소하는 발현 양상을 나타내었다. 이들 단백질을 MALDI-TOF MS와 database를 통해 동정한 결과 에너지 대사관련 단백질, 산화 환원 관련 단백질 및 저분자량 small HSP 등, 10개의 단백질이 동정되었다. 이들 동정된 단백질들은 식물의 고온 스트레스에 대한 적응기작을 이해하는데 중요한 단서를 제공할 것이며, 특히 미토콘드리아 small HSP는 프로테옴 분석법에 의해 최초로 동정되었으며, 금후 내하고성 목초 분자육종에 활용될 수 있는 좋은 유전자로 판단된다.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVII)
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• pp.911-911
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• 2005

• 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.

• 미생물학회지
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• 제37권3호
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• pp.221-227
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• 2001

열충격 단백질(heat shock protein: HSP)은 변성된 단백질의 응집을 방지하여 가혹한환경에서 병원균의 생존을 증가시킨다. 세균에 알코을 stress를 가하면 다량의 DnaK와 GronEL이 유도되지만 폐렴구균에서는 DnaK와 GroEL이 전혀 유도되지 않는 대신 알코올탈수소효소(alcohol dehydrogenase : ADH)가 유도되었다. 이런 특성은 폐렴구균 ADH가 HSP처럼 chaperone 기능을 수행라고 있을 가능성을 제시하고 있으므로 본 연구에서는 일차적으로 ADH 유전자를 확인하고 ADH 의 면역특성 및 세포내 분포를 측정하였다. 폐렴구균 ADH는 이질아메바 ADH2 및 대장균 ADH 와 높은 유사성을 나타냈으며 883 개의 아미노산으로 구성된 등전점 6.09의 단백질로 추정된다. 그러나 폐렴구균 ADH와 유사성이 높은 대장균, 유산균 및 황색포도상구균의 용해액을 폐렴구균 ADH 항체와 immunoblot을 실시하였을 때 전혀 반응하지 않았다. 또한 세포질, membrane, periplasm에 있는 단백질 분획 및 폐렴구균 배양 상등액을 ADH 항체와 immune blot을 실시하였을 때 ADH 는 열충격에 관계없이 세포 밖으로 분비되는 단백질임을 확인하였다. 이런 결과는 폐렴구균 ADH가 진단용항원 및 백신으로 개발될 수 있는 가능성을 제시하고 있다.

• Journal of Microbiology and Biotechnology
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• 제24권8호
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• pp.1118-1122
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• 2014

The present study shows that DR1114 (Hsp20), a small heat shock protein of the radiation-resistant bacterium Deinococcus radiodurans, enhances tolerance to hydrogen peroxide ($H_2O_2$) stress when expressed in Escherichia coli. A protein profile comparison showed that E. coli cells overexpressing D. radiodurans Hsp20 (EC-pHsp20) activated the redox state proteins, thus maintaining redox homeostasis. The cells also showed increased expression of pseudouridine (psi) synthases, which are important to the stability and proper functioning of structural RNA molecules. We found that the D. radiodurans mutant strain, which lacks a psi synthase (DR0896), was more sensitive to $H_2O_2$ stress than wild type. These suggest that an increased expression of proteins involved in the control of redox state homeostasis along with more stable ribosomal function may explain the improved tolerance of EC-pHsp20 to $H_2O_2$ stress.

• Molecules and Cells
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• 제39권2호
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• pp.163-168
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• 2016

Caffeine has both positive and negative effects on physiological functions in a dose-dependent manner. C. elegans has been used as an animal model to investigate the effects of caffeine on development. Caffeine treatment at a high dose (30 mM) showed detrimental effects and caused early larval arrest. We performed a comparative proteomic analysis to investigate the mode of action of high-dose caffeine treatment in C. elegans and found that the stress response proteins, heat shock protein (HSP)-4 (endoplasmic reticulum [ER] chaperone), HSP-6 (mitochondrial chaperone), and HSP-16 (cytosolic chaperone), were induced and their expression was regulated at the transcriptional level. These findings suggest that high-dose caffeine intake causes a strong stress response and activates all three stress-response pathways in the worms, including the ER-, mitochondrial-, and cytosolic pathways. RNA interference of each hsp gene or in triple combination retarded growth. In addition, caffeine treatment stimulated a food-avoidance behavior (aversion phenotype), which was enhanced by RNAi depletion of the hsp-4 gene. Therefore, up-regulation of hsp genes after caffeine treatment appeared to be the major responses to alleviate stress and protect against developmental arrest.