• 제목/요약/키워드: 70 kDa heat shock protein

검색결과 36건 처리시간 0.021초

생쥐 섬 유아세포에서 70 kDa 고온충격 단백질의 CDNA 클로닝과 염기서열 분석 (Isolation and Characterization of a CDNA Encoding a Protein Homologous to the Mouse 70 kDa Heat Shock Protein)

  • 김창환;정선미최준호
    • 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.

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Expression of Heat Shock Protein Protein 70 in Umbilical Vein Endothelial Cells Infected by Staphylococcus aureus

  • Chang, Hyun-Ah;Chang, Jun-Keun;Kim, Jong-Won;Kim, Mal-Nam
    • 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.

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자외선 B 파로 유도된 Hairless Mouse에서 타닌의 피부 독성 억제효과 및 Heat Shock Protein 70의 생성억제 효과 (Inhibitory Effects of Tannic Acid on the Skin Toxicity and Heat Shock Protein Induction by UVB Irradiation in Hairless Mouse)

  • 이세윤;이민경;장동덕;안령미;안형수
    • Toxicological Research
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    • 제13권1_2호
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    • pp.79-86
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    • 1997
  • Inhibitory effects of tannic acid on skin toxicity and heat shock protein induced by UVB were investigated. Tannic acid was administered either topically or orally for 3 days to hairless mice, which were previously irradiated with UVB. UVB was found to cause skin erythema . However, the skin erythema was decreased when tannic acid was administered either topically or orally. The heat shock proteins, Hsp-78 kDa and 70 kDa, were induced by UVB irradiation, but the induction was decreased by treatment of tannic acid in both topically and orally administered groups. The hsp induction was more prominent in orally administered groups than in topically administerd groups. However, the difference between two groups was not statistically significant. The route of administrations, topical and oral, does not affect the activity of tannic acid. In the skin tissue observation, tannic acid regenerated the epithelial cells with 7-9 cell layers which were injured by UVB. In conclusion, tannic acid has an ability to protect against UVB irradiation and regenerate the skin.

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어류 CHSE-214와 인간 HeLa 세포에서의 열충격에 의한 Heat Shock Protein의 발현 (Expression of the Heat Shock Proteins in HeLa and Fish CHSE-214 Cells Exposed to Heat Shock)

  • 공회정;강호성김한도
    • 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.

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Stress-shock Response of a Methylotrophic Bacterium Methylovorus sp. strain SSl DSM 11726

  • Park, Jong H.;Kim, Si W.;Kim, Eungbin;Young T. Ro;Kim, Young M.
    • Journal of Microbiology
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    • 제39권3호
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    • pp.162-167
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    • 2001
  • Methylovorus sp. strain SS1 DSM 11726 was found to grow continuously when it was transferred from 30$\^{C}$ to 40$\^{C}$ and 43$\^{C}$. A shift in growth temperature from 30$\^{C}$ to 45$\^{C}$, 47$\^{C}$ and 50$\^{C}$ reduced the viability of the cell population by more than 10$^2$, 10$^3$and 10$\^$5/ folds, respectively, after 1h cultivation. Cells transferred to 47$\^{C}$ and 50$\^{C}$ after preincubation for 15 min at 43$\^{C}$, however, exhibited 10-fold increase in viability. It was found that incubation for 15 min at 40$\^{C}$ of Methylovorus sp. strain SSl grown at 30$\^{C}$ was sufficient to accelerate the synthesis of a specific subset of proteins. The major heat shock proteins had apparent molecular masses of 90, 70, 66, 60, and 58 kDA. The 60 and 58 kDa proteins were found to cross-react with the antiserum raised against GroEL protein. The heat shock response persisted for over 1h. The shock proteins were stable for 90 min in the cell. Exposure of the cells to methanol induced proteins identical to the heat shock proteins. Addition of ethanol induced a unique protein with a molecular mass of about 40 kDa in addition to the heat-induced proteins. The proteins induced in paraquat-treated cells were different from the heat shock proteins, except the 70 and 60 kDa proteins.

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내염성 cyanobacteria로 부터 danK heat shock protein 유전자의 cloning 및 특성 해명 (Cloning and Characterization of dnaK Heat Shock Protein Gene in a Halotolerant Cyanobacterium)

  • 원성혜;윤병욱;김학윤;;이병현
    • 생명과학회지
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    • 제11권5호
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    • pp.464-469
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    • 2001
  • 내염성의 광합성 cyanobateria 인 Aphanothece halophytica로 부터 molecular chaperone으로 가능하는 HSP70 homolog인 dnaK2 유전자를 cloning 하였다. 이 danK2 유전자는 616개의 아미노산으로 구성되었으며 추정되는 분자량 68 kDa 의 단백질을 code하고 있었다. 아미노산 서열로부터 추정되는 DnaK2 단백질의 구조를 분석하여 본 결과, 다른 원핵생물의 DanK2 단백질들이 공통적으로 갖는 특성인 N-terminal ATPase domain과 C-terminal의 peptide-binding domain이 잘 보존되어 있었으며, 다른 HSP70/DanK 단백질들과의 높은은 상동성을 나타내었다. 한편 danK2 유전자는 생장온도인 28$^{\circ}C$에서 낮은 수준으로 구성적으로 발현하였으며 heat stress에 의해 그 발현량이 급격히 증가하였다. 또한 A. halophytica를 고농도의 염 스트레스로 처리한 결과, heat stress가 없음에도 불구하고 그 발현량이 급격히 증가하였다. 이러한 결과들은 DnaK 단백질의 고온 또는 염 스트레스에 따른 세포의 손상을 보호하기 위하여 중요한 기능을 담당하고 있기 때문에 추정된다.

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Antibodies to Heat Shock Protein 70kDa and 90kDa in the Patients with Schizophrenia, and Their Relationship with Clinical Variables

  • Kim, Jung Jin;Lee, Soo Jung;Toh, Kyu Young;Lee, Chang Uk;Lee, Chul;Paik, In Ho
    • 생물정신의학
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    • 제6권2호
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    • pp.202-208
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    • 1999
  • Schizophrenia has many clinical expressions and probably different etiologic factors. Infections, autoimmune mechanism and related neurodevelopmental abnormalities have been suggested as possible etiologic factors of schizophrenia. It has been reported that immunoreactivity to heat shock proteins, which play a protective role against environmental stresses in a cell, might be related to the pathogenesis of schizophrenia. Therefore, we examined the immunoreactivity to heat shock protein 70kDa and 90kDa(HSP70 and 90) in 91 patients with schizophrenia and 83 normal controls. Ig G antibodies to HSP70 and 90 of sera were quantitated by ELISA. The optical density(OD) was measured by an automated microplate reader at a wavelength of 490nm. The amounts of antibodies to HSPs were expressed as arbitrary units(AU)/ml related to a standard serum. The limit for elevated antibody titers(anti-HSPs positive or negative) was set at two standard deviations added to the mean of the normal controls. Twenty nine(31.9%) of the 91 patients showed anti-HSP70 positive and 19(20.9%) of those showed anti-HSP90 positive. On the other hand, only 1(1.4%) of the normal controls and 4(4.8%) of those showed anti-HSP70 positive and anti-HSP90 positive, respectively. The titers of anti-HSP70 positive were related with BPRS scores, while those of anti-HSP90 positive were not. There were no relationship between antibody titers and clinical variables including age at onset, duration of illness, family history of schizophrenia or number of admission. The titers of anti-HSP70 positive were significantly associated with anti-HSP90 positive. Our results suggest the presence of abnormal immune reactivity involving HSP70 and HSP90 in a subset of patients with schizophrenia.

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금강모치(Rhynchocypris kumgangensis)에서 heat shock protein 70의 클로닝과 수온상승에 의한 발현 변화 분석 (Cloning of Heat Shock Protein 70 and Its Expression Profile under an Increase of Water Temperature in Rhynchocypris kumgangensis)

  • 임지수;길성호
    • 한국물환경학회지
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    • 제29권2호
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    • pp.232-238
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    • 2013
  • Water temperature is key factor influencing growth and reproduction of fish and its increase give rise to various physiological changes including gene expression. Heat shock protein (Hsp), one of the molecular chaperones, is highly conserved throughout evolution and its expression is induced by various stressors such as temperature, oxidative, physical and chemical stresses. Here, we isolated partial cDNA clones encoding 70-kDa Hsp (Hsp70) and $\beta$-actin using reverse transcriptase-PCR (RT-PCR) from gut of Rhynchocypris kumgangensis, a Korean indigenous species and cold-water fish, and investigated expression profiles of Hsp70 under an increase of water temperature using $\beta$-actin as an internal control for RT-PCR. Cloned Hsp70 cDNA of R. kumgangensis showed homology to Ctenopharyngodon idella (96%), Hypophthalmichthys molitrix (96%), Danio rerio (93%) and Oncorhynchus mykiss (81%) Hsp70. Cloned $\beta$-actin cDNA of R. kumgangensis showed homology to D. rerio (98%), H. molitrix (97%), C. idella (97%) and O. mykiss (90%) $\beta$-actin. Both mRNA of Hsp70 and $\beta$-actin were expressed in gut, brain, and liver in R. kumgangensis. Futhermore, expression of Hsp70, in brain, was highly augmented by an increase of water temperature. These results suggest that Hsp70 mRNA expression level in brain can be used as a biological molecular marker to represent physiological stress against an increase of water temperature.

새로운 노화 방지 성분으로서 글루쿠로닉 애씨드의 기능과 화장품 응용 (Application of Glucuronic Acid with New Cosmetic Active Ingredient)

  • 이근수;김진화;이천일;표형배;이공주
    • 대한화장품학회지
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    • 제30권4호
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    • pp.471-477
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    • 2004
  • 피부 세포는 외부의 유해 요소 즉, 스트레스 환경에 노출되었을 때 세포 자신을 보호하기 위하여 다양한 방어 및 복구 체계를 가지고 있는데 그 중 하나가 보호단백질인 열충격단백질 70 kDa의 발현이다 Glucuronic acid를 피부세포에 다양한 농도로 전처리한 다음 유해자극(열, 활성산소)을 주었을 경우, western blottting을 통해 $0.12\%$ 농도에서 세포 내 열충격단백질이 발현됨을 알 수 있었다 그리고 confocal microscopy 및 세포생존율 실험을 이용하여 열 및 활성 산소에 대한 우수한 세포보호 효과를 확인하였다. 또한 마우스 피부를 이용하여 glucuronic acid 및 수중유(O/W)형 에멀젼에 적용하였을 때 경피 흡수 양상을 비교한 결과, glucuronic acid는 빠른 경피흡수거동을 보였다(투과속도 $0.83114 mg/cm^2/h,$ 지연시간 1.2 h, 분배계수 0.114). 에멀젼에서는 투과속도는 $0.04153{\;}{\mu}g/cm^{2}/h,$ 누적투과량은 $1456.25{\;}{\mu}g/cm^{2}$로 감소하였지만 지연시간은 2.48 h으로 증가하였고 지속적인 경피흡수(서방성)를 보였다.

담수산다슬기, Semisulcospira coreana의 열충격단백질 유전자 특성 및 발현분석 (Characterization of Heat Shock Protein 70 in Freshwater Snail, Semisulcospira coreana in Response to Temperature and Salinity)

  • 박승래;최영광;이화진;이상윤;김이경
    • 한국해양생명과학회지
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    • 제5권1호
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    • pp.17-24
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    • 2020
  • 참다슬기 아가미 조직으로부터 heat shock protein 70 유전자를 분리·동정하였다. 참다슬기 HSP70 cDNA의 open reading frame (ORF)는 1,917 bp로 639개의 아미노산을 암호화하여 분자량은 약 70 kDa으로 예측되었다. 생물정보학 배열분석에 의해 HSP 유전자 기능과 관여되어 있는 3가지 주요 signature motifs와 보존된 도메인을 확인하였다. 계통학적 분석을 통하여 참다슬기 HSP70 유전자는 왕우렁이 Pomacea canaliculate와 같은 클러스트에 포함된다는 사실을 확인하였다. 수온 및 염분 변화에 따라, 참다슬기 HSP70 mRNA 유전자 레벨은 유의적으로 증가하였으며(p < 0.05), 이는 외부자극요인을 파악할 있는 분자생물학적 마커로서 활용될 수 있을 것으로 사료된다.