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RISS 인기검색어
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- 저자 : 이철호 ( Il Jun Kang (검색결과 4 건)
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GPX1 및 hOGG1 유전자다형성에 따른 유전자의 산화적 손상 및 폐암 발생 위험도 평가
이철호,이계영,최강현,홍윤철,노성일,엄상용,고영준,장연위,임동혁,강종원,김헌,김용대,Lee, Chul-Ho,Lee, Kye-Young,Choe, Kang-Hyeon,Hong, Yun-Chul,Noh, Sung-Il,Eom, Sang-Yong,Ko, Young-Jun,Zhang, Yan-Wei,Yim, Dong-Hyuk,Kang, Jong-Won,Kim, H 대한예방의학회 2006 예방의학회지 Vol.39 No.2
Objectives : Oxidative DNA damage is a known risk factor of lung cancer. The glutathione peroxidase (GPX) antioxidant enzyme that reduces hydrogen peroxide and lipid peroxides plays a significant role in protecting cells from the oxidative stress induced by reactive oxygen species. The aim of this case-control study was to investigate effects of oxidative stress and genetic polymorphisms of the GPX1 genes and the interaction between them in the carcinogenesis of lung cancer. Methods : Two hundreds patients with lung cancer and 200 age- and sex-matched controls were enrolled in this study. Every subject was asked to complete a questionnaire concerning their smoking habits and their environmental exposure to PAHs. The genotypes of the GPX1 and 8-oxoguanine glycosylase 1 (hOGG1) genes were examined and the concentrations of urinary hydroxypyrene (1-OHP), 2-naphthol and 8-hydroxydeoxyguanosine (8-OH-dG) were measured. Results : Cigarette smoking was a significant risk factor for lung cancer. The levels of urinary 8-OH-dG were higher in the patients (p<0.001), whereas the urinary 1-OHP and 2-naphthol levels were higher in the controls. The GPX1 codon 198 polymorphism was associated with an increased risk of lung cancer. Individuals carrying the Pro/Leu or Leu/Leu genotype of GPX1 were at a higher risk for lung cancer (adjusted OR=2.29). In addition, these individuals were shown to have high urinary 8-OH-dG concentrations compared to the individuals with the GPX1 Pro/Pro genotype. On the other hand, the polymorphism of the hOGG1 gene did not affect the lung cancer risk and the oxidative DNA damage. Conclusions : These results lead to a conclusion that individuals with the GPX1 Pro/Leu or Leu/Leu genotype would be more susceptible to the lung cancer induced by oxidative stress than those individuals with the Pro/Pro genotype.
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강일준,이철호 ( Il Jun Kang,Cherl Ho Lee ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.1
The changes in the hydrophobicity of model proteins (bovine serum albumin, ovalbumin, bovine globulins) were measured by heptane binding method, phenyl -Sepharose CL-4B gel column chromatography, critical micelle concentration and surface tension. The heptane binding capacity and retention time in phenyl-Sepharose CL-4B gel column increased and the critical micelle concentration and surface tension of protein solution decreased as the hydrophobicity of proteins increased. When protein solutions (1% w/v, pH 6.8) were heated upto 90℃, the PAG electrophoresis pattern of each protein suddenly changes at a specific temperature indicating thermal aggregation, i.e. 60℃ for BSA, 60-70℃ for BGs and 80℃ for OA. The hydrophobicity of proteins increased up to the thermal aggregation temperature and then rapidly decreased. It demonstrates the exposure of hydrophobic domain of proteins by heating and subsequent enclosure during aggregation.
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강일준,이철호,Kang, Il-Jun,Lee, Cherl-Ho 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.1
Bovine serum albumin (BSA), ovalbumin (OA), bovine globulins (BGs) 등의 모델단백질을 사용하여 열 처리에 따른 단백질의 변성과 소수성의 변화를 측정할 수 있는 여러 변수를 관찰하였다. 단백질 용액(1% w/v, pH 6.8)을 $20^{\circ}C$부터 $90^{\circ}C$까지 $10^{\circ}C$ 간격으로 10분간씩 열 처리 한 후 전기영동 분석결과 BSA는 $60^{\circ}C$ OA는 $80^{\circ}C$, BGs의 경우 $60^{\circ}C{\sim}70^{\circ}C$사이에서 급격한 열 변성을 일으켰다. 또한 열변성이 일어나기 전까지의 온도에서는 단백질이 부분적으로 변성되면서 heptane결합능력이 커지고 표면장력이 낮아지며, phenyl Sepharose CL-4B gel column에서 지연시간이 걸어졌다. 그러나 단백질 용액의 현탁도가 증가되면서 이들 소수성 측정치는 급격히 감소되었다. 이것은 단백질의 열 처리 과정에서 침전현상이 일어나기 전까지는 소수성 영역이 노출되어 소수성이 증가하는 현상을 간접적으로 시사하는 것이다. The changes in the hydrophobicity of model proteins (bovine serum albumin, ovalbumin, bovine globulins) were measured by heptane binding method, phenyl-Sepharose CL-4B gel column chromatography, critical micelle concentration and surface tension. The heptane binding capacity and retention time in phenyl-Sepharose CL-4B gel column in creased and the critical micelle concentration and surface tension of protein solution decreased as the hydrophobicity of proteins increased. When protein solutions (1% w/v, pH 6.8) were heated upto $90^{\circ}C$, the PAG electrophoresis pattern of each protein suddenly changes at a specific temperature indicating thermal aggregation, i.e. $60^{\circ}C$ for BSA, $60-70^{\circ}C$ for BGs and $80^{\circ}C$ for OA. The hydrophobicity of proteins increased up to the thermal aggregation temperature and thenrapidly decreased. It demonstrates the exposure of hydrophobic domain of proteins by heating and subsequent enclosure during aggregation.
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최인혁,이동일,이철호,강병규,이원교,박준호,Choi, In-Hyuk,Lee, Dong-Il,Lee, Chul-Ho,Kang, Byoung-Kyu,Lee, Won-Kyo,Park, Jun-Ho 한국전기전자재료학회 2007 전기전자재료학회논문지 Vol.20 No.9
To understand the effects of forest fires on polymer insulators for transmission lines, the forest fire simulation tests were performed with polymer and porcelain insulators at Gochang testing center. These tests consisted of energizing 90 kV at line-to-ground voltage of 154 kV lines and open flame rising up to $600-630^{\circ}C$ as being measured at insulator surface. Mechanical and electrical characteristics such as specific mechanical load, leakage current, low frequency dry flashover voltage and impulse flashover voltage were analyzed for the polymer insulators before, during and after simulation tests compared with porcelain insulators. At the end of fire simulation tests, there was no detrimental deterioration of any insulators. All insulators passed the criteria of KEPCO specification. This study showed that forest fire simulation had no impact on polymer insulators.
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