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Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Lee, Sang-Kyou,Park, Se-Yeon,Jun, Gyo,Hahm, Eun-Ryeong,Lee, Dug-Keun,Yang, Chul-Hak Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 nucleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the coventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Yang, Chul Hak,Jun, Gyo,Lee, Dug Keun,Lee, Sang Kyou,Park, Se Yeon,Hahm, Eun Ryeong 생화학분자생물학회 1998 BMB Reports Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 nucleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the conventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
Quantitative Assay for the Binding of Jun-Fos Dimer and Activator Protein-1 Site
Yang,Chul-Hak,Jun,Gyo,Hahm,Eun-Ryeong,Lee,Sangkyou,Park,Seyeon,Lee,Dug-Keun The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.6
The Jun and Fos families of eukaryotic transcription factors form heterodimers capable of binding to their cognate DNA enhancer elements. We are interested in searching for inhibitors or antagonists of the binding of the Jun-Fos heterodimer to the activator protein-1 (AP-1) site. The basic-region leucine zipper (bZIP) domain of c-Fos was expressed as a fusion protein with glutathione S-transferase, and allowed to form a heterodimer with the bZIP domain of c-Jun. The heterodimer was bound to glutathione-agarose, to which were added radiolabeled AP-1 uncleotides. After thorough washing, the gel-bound radioactivity was counted. The assay is faster than the coventional electrophoretic mobility shift assay because the gel electrophoresis step and the autoradiography step are eliminated. Moreover, the assay is very sensitive, allowing the detection of picomolar quantities of nucleotides, and is not affected by up to 50% dimethylsulfoxide, a solvent for hydrophobic inhibitors. Curcumin and dihydroguaiaretic acid, recently known inhibitors of Jun-Fos-DNA complex formation, were applied to this Jun-GST-fused Fos system and revealed to decrease the dimer-DNA binding.
Eun Ryeong Jun,Sung Hi Kim,Yoon Jeong Cho,Yun-A Kim,Joo Young Lee 대한가정의학회 2019 Korean Journal of Family Medicine Vol.40 No.5
Background: Several studies have shown that negative mental health increases risky health behavior and mortality risk. We investigated the relationship between mental health and health behavior, and the causal association between mental health and mortality risk. Methods: We used data from the 8-year (2006–2014) Korean Longitudinal Study of Aging with a cohort of 10,247 individuals (whom we divided into a younger group aged <65 years and an older group aged ≥65 years). Mental health was assessed with the following factors: depression, social engagement, and satisfaction of life. Health behavior was assessed with smoking, alcohol use, and regular exercise. Mortality risk was calculated using survival status and survival months as of 2014. Multiple logistic regression and Cox proportional hazard analysis were performed. Results: Negative mental health was associated with current smoking and sedentary life style, but not with alcohol consumption. In addition, it was associated with an increase in all-cause mortality risk. The increase in mortality risk in the highest quartile (vs. lowest) was 1.71 times (hazard ratio [HR], 1.71; 95% confidence interval [CI], 1.12– 2.62) and 2.07 times (HR, 2.07; 95% CI, 1.60–2.67) for the younger and older group, respectively. Conclusion: Our results show that mental health affects health behavior and mortality risk. A key inference from this study is that improving mental health can lead to positive changes in health behavior and reduce the risk of mortality.
Jun, Eunsung,Oh, Juyun,Lee, Song,Jun, Hye-Ryeong,Seo, Eun Hye,Jang, Jin-Young,Kim, Song Cheol Neoplasia Press 2018 Translational oncology Vol.11 No.3
<P>Nucleic acid sequencing is frequently used to determine the molecular basis of diseases. Therefore, proper storage of biological specimens is essential to inhibit nucleic acid degradation. RNA isolated from the human pancreas is generally of poor quality because of its high concentration of endogenous RNase. In this study, we optimized the method for extracting high quality RNA from paired tumor and normal pancreatic tissues obtained from eight pancreatic cancer patients post-surgery. RNA integrity number (RIN) was checked to evaluate the integrity of RNA, we tried to extract the RNA with an RIN value of 8 or higher that allows for the latest genetic analysis. The effect of several parameters, including the method used for tissue lysis, RNA<I>later</I> treatment, tissue weight at storage, and the time to storage after surgical resection, on the quantity and quality of RNA extracted was examined. Data showed that the highest quantity of RNA was isolated using a combination of manual and mechanical methods of tissue lysis. Additionally, sectioning the tissues into small pieces (<100 mg) and treating them with RNA<I>later</I> solution prior to storage increased RNA stability. Following these guidelines, high quality RNA was obtained from 100% (8/8) of tumor tissues and 75% (6/8) of normal tissues. High-quality RNA was still stable under repeated freezing and thawing. The application of these results during sample handling and storage in clinical settings will facilitate the genetic diagnosis of diseases and their subsequent treatment.</P>