• Journal of Periodontal and Implant Science
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• 제33권4호
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• pp.555-562
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• 2003

The present study has been performed to evaluate Porphyromonas gingivalis (P.gingivalis) heat shock protein(HSP)60 as a candidate vaccine to inhibit multiple bacteria-induced alveolar bone loss. Rats were immunized with P.gingivalis HSP60 and experimental alveolar bone loss was induced by infection with multiple periodonto -pathogenic bacteria. Post-immune rat anti-P.gingivalis HSP IgG levels were significantly elevated and have demonstrated highly significant inverse relationship with the amount of alveolar bone loss induced by multiple bacteria. Results from PCR detection of subgingival bacterial plaque indicated that the vaccine successfully eradicated the multiple pathogenic species. We concluded that P.gingivalis HSP60 could potentially be developed as a vaccine to inhibit periodontal disease induced by multiple pathogenic bacteria.

• Bulletin of the Korean Chemical Society
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• 제19권3호
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• pp.295-299
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• 1998

HSP104 protein in Saccharomyces cerevisiae is known to provide thermotolerance when induced by various kinds of stresses, such as a mild heat shock, ethanol, and hypoxia. It helps cells survive at an otherwise lethal temperature. Mechanisms by which HSP104 protein works are yet to be elucidated. In order to understand a molecular basis of thermotolerance due to HSP104 protein induced by a mild heat shock, studies on respiratory pathways were carried out in the wild type as well as in the hsp104 deleted mutant. Especially the degree of 13C-acetate incorporation into glutamate-C4 was examined for both strains using 13C-13C homonuclear spin coupling measurements, since glutamate is in a rapid equilibrium with α-ketoglutarate in the TCA cycle. In addition, the temperature effects on the rate of 13C incorporation are compared with or without HSP104 protein expressed. Finally, the inhibitory effect of HSP104 on the respiration pathway was confirmed by the measurements of oxygen consumption rates for both strains.

• 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.

• Molecules and Cells
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• 제20권2호
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• pp.173-182
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• 2005

Heat shock protein gp96 is an endoplasmic reticulum chaperone, belonging to the HSP90 family. The function of gp96 as a molecular chaperone was discovered more than 10 years ago, but its importance has been overshadowed by the brilliance of its role in immune responses. It is now clear that gp96 is instrumental in the initiation of both the innate and adaptive immunity. Recently, the roles of gp96 in protein homeostasis, as well as in cell differentiation and development, are beginning to draw more attention due to rapid development in the structural study of HSP90 and some surprising new discoveries from genetic studies of gp96. In this review, we focus on the aspect of gp96 as an ER molecular chaperone in protein maturation, peptide binding and the regulation of its activity.

• Molecules and Cells
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• 제24권2호
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• pp.210-214
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• 2007

The 90-kDa heat shock protein (HSP90) normally functions as a molecular chaperone participating in folding and stabilizing newly synthesized proteins, and refolding denatured proteins. The HSP90 inhibitor geldanamycin (GA) occupies the ATP/ADP binding pocket of HSP90 so inhibits its chaperone activity and causes subsequent degradation of HSP90 client proteins by proteasomes. Here we show that GA reduces the level of endogenous c-Jun in human embryonic kidney 293 (HEK293) cells in a time and dose dependent manner, and that this decrease can be reversed by transfection of HSP90 plasmids. Transfection of HSP90 plasmids in the absence of GA increases the level of endogenous c-Jun protein, but has no obvious affect on c-Jun mRNA levels. We also showed that HSP90 prolongs the half-life of c-Jun by stabilizing the protein; the proteasome inhibitor N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132) blocks the degradation of c-Jun promoted by GA. Transfection of HSP90 plasmids did not obviously alter phosphorylation of c-Jun, and a Jun-2 luciferase activity assay indicated that over-expression of HSP90 elevated the total protein activity of c-Jun in HEK293 cells. All our evidence indicates that HSP90 stabilizes c-Jun protein, and so increases the total activity of c-Jun in HEK293 cells.

• 한국초지학회:학술대회논문집
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• 한국초지조사료학회 1999년도 제24회 정기총회 및 프로그램, 제37회 학술발표회 및 특별강연 초록
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• pp.71.2-72
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• 1999

고등식물에 있어서 엽록체에 존재하는 저 분자량 heat shock protein (smHSP)은 식물의 내열성 획득에 있어서 필수유전자임이 mutant를 이용한 유전학적인 연구에 의해 보고된 바 있다. 고온내성이 강한 작물인 벼로부터 엽록체 smHSP cDNA를 분리하고자 벼의 잎에서 분리한 mRNA로 작성한 cDNA library로부터 screening하였다. 선발된 smHSP cDNA는 1,026 bp의 염기로 구성되어 있었으며, 239개의 아미노산으로 구성되는 예상분자량 26.6 kDa의 단백질을 code하고 있었다. 또한 다른 식물로부터(중략)

• 대한기관식도과학회지
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• 제7권1호
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• pp.24-28
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• 2001

Background and Objectives： Heat shock protein(HSP) 27 is a member of the small HSP family that plays a part in the epithelial cell growth and differentiation, wound healing. apoptosis and cell protection against inflammatory cytotoxic mediators. The expression of HSP27 was investigated in normal laryngeal tissue and squamous cell carcinoma of the larynx. Materials and Methods : We studied expression of HSP27 by Western blot on 20 patients of laryngeal squamous cell carcinoma. Results： HSP27 expressed in all normal and cancer tissues. In 9 cases(45%), expression of HSP27 more prominent in cancer tissue. Statistically, there were no significant difference in the expression of HSP27 in normal and cancer tissue, clinical stage and tumor differentiation. Conclusion 45% of cancer tissues was more prominent than normal tissue. But further studies on expression of HSP27 in laryngeal cancer and relationship with clinical parameter should be done.

• 한국동물위생학회지
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• 제29권4호
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• pp.469-482
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• 2006

The term 'heat shock protein (Hsps)' was derived from the fact that these proteins were initially discovered to be induced by hyperthermic conditions. In response to a range of stressful stimuli, including hyperthermia, immobilization, UV radiation, amino acid analogues, arsenite, various chemicals, and drugs the mammalian brain demonstrates a rapid and intense induction of the heat shock protein. Moreover, Hsps were expressed on the various pathological conditions including trauma, focal or global ischemia, hypoxia, infarction, infections, starvation, and anoxia. Especially, Hsp25 has a protective activity, facilitated by the ability of the protein to decrease the intracellular levels of reactive oxygen species (ROS) as well as its chaperone activity, which favors the degradation of oxidized proteins. Recently, it has clearly demonstrated that Hsp25 is constitutively expressed in the adult mouse cerebellum by parasagittal bands of purkinje cells in three distinct regions, the central zone (lobule VI-VII) and nodular zone (lobule IX-X), and paraflocculus. The Mongolian gerbil has been introduced into stroke study model because of its unique brain vasculature. There are no significant connections between the basilarvertebral system and the carotid system. This anatomy feature renders the mongolian gerbil susceptible to forebrain ischemia-induced seizure. The present study is designed to examine the pattern of Hsp25 expression in the cerebellum of this animal in comparison with that in mouse.

• 생명과학회지
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• 제7권4호
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• pp.276-281
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• 1997

This study was investigated to determine whether nicotine causes the morphological changes and expression of heat shock protein(HSP) 70 in the central nervous system of rat embryo. The pregnant rats were injected s.c. twice daily with 3 mg nicotine per 100g body weight from day 0 to 14 of gestation and embryos were removed on gestation day 15. As morphological changes, retardation of cell proliferaton was observed in the telencephalon of nicotine-treated groups and no changes in the other region were found. Minimal HSP 70 was expressed over chole central nervous system was similar between control and nicotine-treated group, the expression of blood cells in the meinges and chroid plexus was significantly greater in nicotine-treated group than in control.

• 생명과학회지
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• 제28권6호
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• pp.639-647
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• 2018

한국의 고급 양식대상 어종인 붉바리(Epinephelus akaara)로부터 새로운 heat shock protein (Hsp) 70을 동정하였다. 붉바리 Hsp70 (RgHsp70)의 cDNA는 RACE (rapid amplification of cDNA ends)법을 사용하였고, RgHsp70 cDNA의 전장은 2,152 bp이고, 5'-terminal untranslated region (UTR)은 105 bp, 3'-terminal UTR은 274 bp, 590개의 아미노산을 암호화하는 open reading frame (ORF)는 1,773 bp였으며, 분자무게(molecular weight)는 64.9 kDa 및 등전위값(isoelectric point, pI)은 5.2였다. 추정되는 아미노산 비교 및 계통발생학적 분석 결과, 다른 어종과 마찬가지로 Hsp70 고유의 signature를 포함하는 것을 비롯하여 높은 유사성을 나타내었으므로 RgHsp70이 Hsp70 family임을 확인할 수 있었다 RgHsp70 mRNA는 간과 두신 조직에서 높은 발현을 보였으며, 48시간 동안 수온별(21, 18, 15 및 $12^{\circ}C$) 노출 후 간 조직에서 대조구인 $21^{\circ}C$보다 $12^{\circ}C$에서 발현이 증가함을 확인하였다. 본 연구에서는, 수온이 하강함에 따라 RgHsp70 mRNA 발현에 주요한 영향을 미치는 것으로 보아, 수온변화에 따른 스트레스로 인해 발현의 변화를 나타내는 주요 스트레스성 단백질임을 확인할 수 있었다.