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A Case of High-degree Atrioventricular Block in a Patient with Ankylosing Spondylitis
( Sang Rok Lee ),( Hyung Wook Park ),( Sang Yub Lim ),( Seo Na Hong ),( Kye Hun Kim ),( Il Suk Sohn ),( Young Joon Hong ),( Ju Han Kim ),( Weon Kim ),( Young Keun Ahn ),( Myung Ho Jeong ),( Jeong Gwan 대한내과학회 2005 대한내과학회 추계학술대회 Vol.69 No.10
Sang Chul Shiim,Chil Hoon Doh,Dong Yub Lee,Jae Goo Shim,Young Zoo Youn,Woo Hyung Park,Li Hong Jiang,Ju Hee Kim Korean Chemical Society 1993 Bulletin of the Korean Chemical Society Vol.14 No.5
Treatment of (dichloromethyl)benzenes with CO (1 atm) in the presence of catalytic amount of $Co_2(CO)_8,\;Fe(CO)_5$ and BTEAC under two phase systems with NaOH(_{aq}) and $PhCH_3$ containing small amount of alcohol for 20 hours at 80$^{\circ}$C gives phenylacetic acids in moderate yields.
Sung Chul Kwon(권성철),Yoon-yub Park(박윤엽),Young Man Lee(이영만) 한국생명과학회 2010 생명과학회지 Vol.20 No.4
흰쥐에서 Interleukin-1 (IL-1)으로 유도된 급성폐손상에서의 group Ⅱ phospholipase A₂ (PLA₂) 억제제인 rutin의 효과를 알아보기 위하여 본 연구를 시행하였다. Rutin은 IL-1에 의해 증가한 폐장내의 myeloperoxidase의 활성도를 감소시키지는 못하였으나 폐포세척액 내의 호중구의 수 및 모세혈관의 손상지표로 알려져 있는 폐장 모세혈관에서의 단백짙 누출양음 감소시켰다. 동시에 rutin은 IL-1에 의하여 증가한 폐장의 염증조절효소인 PLA₂의 활성도를 감소시키고 결과적으로 호중구에서의 산소기의 생성을 감소시켰다. Rutin 뿐만 아니라 manoalide, scalaradial 같은 group Ⅱ PLA₂의 억제제도 호중구의 respiratory burst를 감소시킴을 확인하였다. IL-1에 의하여 증가한 폐포세척액 내에서의 cytokine induced neutrophil chemoattractant의 농도는 rutin에 의해 영향을 받지 않았다. 형태학적으로는 IL-1에 의한 폐장조직에서의 산소기의 형성이 관찰되었고 rutin은 이러한 산소기의 생성을 현저히 감소시켰다. 이러한 결과로 미루어 group Ⅱ PLA₂ 억제제인 rutin은 호중구에서의 활성 산소기의 생성을 효과적으로 억제함으로써 IL-1에 의한 급성폐손상의 감소를 가져 오는 것으로 결론지을 수 있다. Rutin, a group Ⅱ phospholipase A₂ (PLA₂) inhibitor, was tested on interleukin-1 (IL-1) induced acute lung injury (ALI) in male Sprague-Dawley rats. Rutin did not alter the increased lung myeloperoxidase activity by IL-1. However, the number of neutrophils in bronchoalveolar lavage fluid (BALF) and IL-1 induced lung leak were decreased by rutin (p<0.001). Simultaneously, rutin decreased lung PLA₂ activity, which was increased by IL-I (p<0.001). The reduction of neutrophilic respiratory burst by the inhibition of PLA₂ was confirmed by group Ⅱ PLA₂ inhibitors such as rutin, manoalide and scalaradial. The increased level of cytokine-induced neutrophilic chemoattractant (CINC) in BALF by IL-I was not affected by rutin. Ultrastructural changes of ALI and increased generation of free radicals in the lung by IL-I were found, and rutin ameliorated these pathological findings. Taken together, rutin seems to be effective in decreasing IL-I induced ALI through inhibition of group Ⅱ PLA₂.
Bisphenol A exerts estrogenic effects by modulating CDK1/2 and p38 MAP kinase activity.
Lee, Hee-Seok,Park, Eun-Jung,Oh, Jae-Ho,Moon, Guiim,Hwang, Myung-Sil,Kim, Sang-Yub,Shin, Min-Ki,Koh, Young-Ho,Suh, Jin-Hyang,Kang, Hui-Seung,Jeon, Ju-Hong,Rhee, Gyu-Seek,Hong, Jin-Hwan Japan Society for Bioscience, Biotechnology, and A 2014 Bioscience, Biotechnology, and Biochemistry Vol.78 No.8
<P>Bisphenol A (BPA) is considered to be an endocrine disruptor, but the mechanisms by which it disrupts endocrine functions are poorly understood. Here, we have shown that BPA binds both estrogen receptor (ER)-α and ER-beta (ER-β) using a fluorescence polarization competitive binding assay. In addition, we found that BPA induced cell proliferation by modulating cell cycle-related genes in the MCF-7 human mammary cancer cell line. Moreover, using a BG1 luciferase ER transactivation assay, we found that BPA has estrogenic activity. Modulating the MAPK pathway by using an ERK inhibitor (PD98059) or a JNK inhibitor (SP600125) had no effect on the ability of BPA to induce estrogenic activity. However, the antiestrogen, ICI 182,780, and the p38 inhibitor, PD 169316 successfully blocked BPA-induced estrogenic activity. Our findings suggest that BPA mimics ER-dependent estrogenic activity by targeting proteins that regulate the cell cycle and p38 MAPK.</P>
Lee, Hyun Jik,Ryu, Jung Min,Jung, Young Hyun,Oh, Sang Yub,Lee, Sei-Jung,Han, Ho Jae AlphaMed Press 2015 Stem Cells Vol.33 No.7
<P>The control of stem cells by oxygen signaling is an important way to improve various stem cell physiological functions and metabolic nutrient alteration. Lipid metabolism alteration via hypoxia is thought to be a key factor in controlling stem cell fate and function. However, the interaction between hypoxia and the metabolic and functional changes to stem cells is incompletely described. This study aimed to identify hypoxia-inducible lipid metabolic enzymes that can regulate umbilical cord blood (UCB)-derived human mesenchymal stem cell (hMSC) proliferation and migration and to demonstrate the signaling pathway that controls functional change in UCB-hMSCs. Our results indicate that hypoxia treatment stimulates UCB-hMSC proliferation, and expression of two lipogenic enzymes: fatty acid synthase (FASN) and stearoyl-CoA desaturase-1 (SCD1). FASN but not SCD1 is a key enzyme for regulation of UCB-hMSC proliferation and migration. Hypoxia-induced FASN expression was controlled by the hypoxia-inducible factor-1 alpha (HIF-1)/SCAP/SREBP1 pathway. Mammalian target of rapamycin (mTOR) was phosphorylated by hypoxia, whereas inhibition of FASN by cerulenin suppressed hypoxia-induced mTOR phosphorylation as well as UCB-hMSC proliferation and migration. RAPTOR small interfering RNA transfection significantly inhibited hypoxia-induced proliferation and migration. Hypoxia-induced mTOR also regulated CDK2, CDK4, cyclin D1, cyclin E, and F-actin expression as well as that of c-myc, p-cofilin, profilin, and Rho GTPase. Taken together, the results suggest that mTORC1 mainly regulates UCB-hMSC proliferation and migration under hypoxia conditions via control of cell cycle and F-actin organization modulating factors. In conclusion, the HIF-1/FASN/mTORC1 axis is a key pathway linking hypoxia-induced lipid metabolism with proliferation and migration in UCB-hMSCs. Stem Cells 2015;33:2182-2195</P>