• 한국동물학회지
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• 제38권2호
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• pp.153-159
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• 1995

임신 10일부터 20일까지 흰쥐 태반형성과정에서 heat shock protein 27(HSP27) 분포를 면역조직화학적으로 조사하였다 임신 10일 태반에 자궁간막 탈락막세포. 영양막세포 및 거대영양막세포가 찰찰되었다. 이후 탈락막세포수는 감소하고 영양막세포는 증가하는데 특히 임신 14일에 현저하며 영양막은 해면영양막과 미로영양막으로 구분되었다 거대영양 막세포수의 변화는 현저하지 않았다. 자궁간막 탈락막에서 HSP27은 임신 10일 및 12일에 탈락막세포의 세포질 또는 핵에 반응이 나타나고 특히 핵에 반응하는 세포수가 많았으며 임신 14일 이후 탈락막 세포수 감소와 함께 반응이 나타나지 않았다 거대영양막세포는 임신 10일부터 일부 세포의 세포질 또는 핵에 반응이 관찰되나 임신 18일부터는 반응이 나타나지 않았다 영양막의 HSP27은 임신 10 및 12일에 일부 세포에서만 세포질 또는 핵에 반응이 관찰되나, 임신 14일부터 반응세포수 증가와 함께 대부분 핵에 반응을 나타내고 반응정도는 임신 16일 및 18일에 가장 현저하였으며, 미로영양막에서 반응세포수가 더 많았다.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2000년도 춘계학술발표대회
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• pp.355-356
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• 2000

Three 'stress probe' plasmids were constructed and characterized which utilize a green fluorescent protein (CFP) as a non-invasive reporter to elucidate Escherichia coli cellular stress responses in quiescent or 'resting' cells. Facile detection of cellular stress levels was achieved by fusion of three heat shock stress protein promoter elements, those of the heat shock transcription factor ${\sigma}^{32}$, pretense subunit ClpB, and chaperone DnaK, to the reporter gene $gfp_{uv}$. When perturbed by chemical or physical stress (such as heat shock, nutrient (amino acid) limitation, addition of IPTG, acetic acid, ethanol, phenol, antifoam, and salt (osmotic shock), the E. coli cells produced GFPuv which was easily detected from within the cells as emitted green fluorescence. A temporal and amplitudinal mapping of these responses was performed, demonstrating regions where quantitative delineation of cell stress was afforded.

• Journal of Microbiology and Biotechnology
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• 제8권4호
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• pp.361-368
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• 1998

The E2 protein of HCV (hepatitis C virus) is thought to have a potential role in the development of subunit vaccines and diagnostics. To express it by the insect cell/baculovirus expression (Bacu) system, we constructed a recombinant Autographa californica nuclear polyhedrosis virus (AcIL3E2), determined the most appropriate expression conditions in terms of host cell line and culture medium, and characterized the expressed HCV E2 protein. A culture system using Trichoplusia ni BTI-TN5Bl-4 cells and SF 900IISFM medium expressed a relatively high level of HCV E2 protein. It was revealed that its glycosylation properties and subcellular localization were almost the same as the ones in the mammalian cell expression system previously reported, suggesting the recombinant HCV E2 protein derived from our Bacu system can be utilized for development of a subunit vaccine and diagnostics. Interestingly, HCV E2 protein was not degraded at all even at 43 h post-heat shock in the heat shock-induced necrotic cells, probably due to its integration into the microsomal membrane, indicating that heat shock can be employed to purify HCV E2 protein.

• Genomics & Informatics
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• 제7권1호
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• pp.26-31
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• 2009

Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell's danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.

• Clinical and Experimental Reproductive Medicine
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• 제29권1호
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• pp.37-44
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• 2002

Objective : Heat shock protein family is related to protective mechanism of cells by environmental changes. This study was performed to evaluate the effect of cryopreservation on the heat shock protein 90 (Hsp90) expression in mouse ovarian tissue. Methods : Cryopreservation of mouse ovarian tissue was carried out by slow freezing method. The mRNA level of Hsp90 expression in both fresh and cryopreserved mouse ovarian tissue was analyzed by RT-PCR. The protein expression of Hsp90 was evaluated by Western blot analysis and immunohistochemistry. Results: The mRNA and protein of Hsp90 were expressed in both fresh and cryopreserved mouse ovarian tissue. The amount of Hsp90 mRNA was increased in cryopreserved ovarian tissue after 60 and 90 minutes after thawing and incubation. The amount of Hsp90 protein was increased in the cryopreserved ovarian tissue after 6 hours of the incubation in Western blot analysis. In immunohistochemical study, Hsp90 protein was localized in cytoplasm of oocytes and granulosa cells. Significant level of immunoreactive Hsp90 protein was detected in theca cells contrast to the weak expression in ovarian epithelial cells. Conclusion: This results showed the increase of Hsp90 expression in both mRNA and protein level in the cryopreserved mouse ovarian tissue. It can be suggested that Hsp90 may play a role in the protective or recovery mechanism against the cell damage during cryopreservaion.

• Asian-Australasian Journal of Animal Sciences
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• 제30권1호
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• pp.94-99
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• 2017

Objective: The aim of this study was to investigate the expression of heat shock protein (HSP) 90, 70, and 60 in chicken muscles and their possible relationship with quality traits of meat. Methods: The breast muscles from one hundred broiler chickens were analyzed for drip loss and other quality parameters, and the levels of heat shock protein (HSP) 90, 70, and 60 were determined by immunoblots. Results: Based on the data, chicken breast muscles were segregated into low (drip loss${\leq}5%$), intermediate (5%${\geq}9.5$) drip loss groups. The expression of HSP90 and HSP60 were significantly lower in the high drip loss group compared to that in the low and intermediate drip loss group (p<0.05), while HSP70 was equivalent in abundance in all groups (p>0.05). Conclusion: Results of this study suggests that higher levels of HSP90 and HSP60 may be advantageous for maintenance of cell function and reduction of water loss, and they could act as potential indicator for better water holding capacity of meat.

• Biomolecules & Therapeutics
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• 제9권2호
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• pp.79-87
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• 2001

Heat shock proteins serve as chaperone by preventing the aggregation of denatured proteins and promote survival of pathogens in harsh environments. In this study, heat shock gene encoding a 84-kDa (p84) protein, which is one of the three major heat shock proteins in S. pneumoniae, was cloned and characterized. PCR with a forward primer derived from N-terminal amino acid sequence of the p84 and a reverse primer derived from the conserved second ATP-binding region of Clp family was used for amplification of the gene encoding the p84 and subsequently the PCR product was used for sequence determination. Sequence analysis of the p84 gene demonstrated that it is a member of ClpL. The deduced amino acid sequence of pneumococcal ClpL shows homology with other members of the Clp family, and particularly, even in variable leader region, with bovine Clp-like protein and L. lactis ClpL. S. pneumoniae clpL is the smallest clop member (701 amono acids) containing the two conserved ATP-binding regions, and hydrophilic N-terminal variable region of pneu-mococcal Clp ATPase is much shorter than any known Clp ATPases. Histidine tagged ClpL was overexpressed and purified from E. coli. Immunoblot analysis employing antisera raised against pneumococcus p84 demonstrated no cross-reactivity with Clp analog in Eschericha coli, Staphylococcus aureus and human HeLa cells. Preimmunization of mice with ClpL extended mice life partially but did not protect them from death.

• 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.

• 한국동물학회지
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• 제35권2호
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• pp.203-210
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• 1992

Hsp70, a 70 kDa protein, is the maior protein expressed when cells are heat-shocked. A cDNA library from mouse ID13 cells was screened with the human hsp70 gene as a probe, and a positive clone was obtained. The positive clone was subcloned into puc19 and the precise restriction was obtained. The CDNA was sequenced by the Sanger's dideoxv termination method. Single open reading frame that codes for a protein of 70 kDa was found. The DNA sequence of the cloned mouse DNA shows great homology (66-90%) with other mouse hsp70 genes and somewhat less homology (50",) with E. coli hsp70 gene (dnak). With the exception of one amino acid, the protein sequence deduced from the CDNA is identical to the mouse that shock cognate protein 70 (hsc70) that is constitutivelv expressed at normal temperature. The result suggests that the cloned CDNA encodes a hsc70 family rather than a heatinducible family.mily.

• 한국가금학회지
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• 제43권4호
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• pp.213-218
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• 2016

본 연구는 고온 스트레스 하에 타우린 첨가가 육계의 간에서 heat shock protein 70(hsp 70) 및 cell free system 상태에서 단백질 합성에 미치는 영향을 조사하였다. 공시동물은 1일령 육계 120수를 2주간 사육 후, 대조(CO, $24^{\circ}C$)와 고온스트레스 처리($34^{\circ}C$)에서 타우린을 공급하지 않은 처리구(HO)와 타우린 0.1%를 공급한 처리구(HT)로 나누어 3처리 4반복, 반복 당 10수씩 배치하였다. 고온 스트레스는 3, 6, 9, 12일간 진행하였다. 최종 체중과 간 무게는 HO와 HT가 CO보다 유의적으로 낮았다(P<0.05). 그러나 타우린을 첨가한 HT은 HO보다 유의적으로 높았다(P<0.05). 육계 간에서 hsp70 발현은 HO가 CO와 HT보다 유의적으로 높았으나(P<0.05), CO와 HT는 유의적인 차이가 없었다. In vitro 실험에서 고온 및 타우린은 21일령 육계 간의 총 단백질 합성률에 영향을 미치지 않았다. 따라서 타우린 섭취가 in vivo 육계의 성장에서 고온 스트레스를 완화시키지만, 생체 내의 단백질 합성에 직접적인 영향을 미치지 않는 것을 보이며, 이러한 결과는 타우린이 다양한 생리학적 기전을 통해 단백질 turnover 대사에 간접적으로 영향을 미칠 수 있다는 것으로 사료된다.