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Lee, Tae Geum,Lee, Ju Hoon,Hyun, Min Young,Jang, Seung Pyo,Lee, Hong Gyu,Kim, Cheal,Kim, Sung-Jin,Kim, Youngmee Elsevier 2010 INORGANIC CHEMISTRY COMMUNICATIONS Vol.13 No.12
<P><B>Abstract</B></P><P>Three new Cd(II) complexes containing 3-bpdb ligands with amide moiety as hydrogen-bond capable backbone, formulated as [Cd(3-bpdb)X<SUB>2</SUB>]<SUB>n</SUB> (3-bpdb=N,N′-dipyridin-3-ylpyridine-2,6-dicarboxamide, X=Cl (<B>1</B>), Br (<B>2</B>), and I (<B>3</B>)), have been synthesized. All three compounds show 1-dimensional looped chain structures, and intra- and inter-molecular hydrogen bonding interactions provide 2-dimensional sheets. Among three pausible conformers of ligand 3-bpdb, all three halide compounds show only <I>anti</I><B>–</B><I>anti</I> conformation to provide 1-dimensional looped chains. In addition, emissions of compounds <B>1</B> and <B>2</B> were observed at 424nm and 431nm, respectively, suggesting that they might be a good candidate for a potential hybrid inorganic<B>–</B>organic photoactive material. Moreover, compounds <B>1–3</B> carried out an efficient transesterification of vinyl acetate.</P> <P><B>Graphical Abstract</B></P><P>Three new Cd(II) complexes containing 3-bpdb ligands (3-bpdb=N,N′-dipyridin-3-ylpyridine-2,6-dicarboxamide) were synthesized. All three compounds showed 1-dimensional looped chain structures, and intra- and inter-molecular hydrogen bonding interactions provide 2-dimensional sheets. Their photoluminescence and catalytic reactivity were also studied.<ce:figure id='f0020'></ce:figure></P>
Lee, Seung Goo,SUNG, MOON HEE,Esaki, Nobuyoshi,Hong, Seung Pyo,Kwak, Mi Sun 생화학분자생물학회 2001 BMB Reports Vol.32 No.5
Tyrosine phenol-lyase of thermophilic Symbiobacterium sp. SC-1, which is obligately and symbiotically dependent on thermophilic Bacillus sp. SK-1, was purified and characterized. The enzyme is composed of four identical subunits and contains approximately 1 ㏖ of pyridoxal 5'-phosphate (PLP) per ㏖ subunit as a cofactor. The enzyme showed absorption maxima at 330 and 420 nm, and lost this absorption profile by treatment with phenylhydrazine. The apparent dissociation constant, K'_D, for PLP was determined with the apoenzyme to be about 1.2 μM. The isoelectric point was 4.9. The optimal temperature and pH for the α,β-elimination of z-tyrosine were found to be 80℃ and pH 8.0, respectively. The substrate specificity of the enzyme was very broad: L-amino acids including L-tyrosine, 3,4-dihydroxyphenyl-L-alanine (L-DOPA), L-cysteine, L-serine, S-methyl-L-cysteine, β-chloro-L-alanine, and S-(o-nitrophenyl)-L-cysteine all served as substrates. D-Tyrosine and D-serine were also decomposed into pyruvic acid and ammonia at rates of 7 % and 31 % relative to their corresponding L-enantiomers, respectively. D-Alanine, which was inert as a substrate in α,β-elimination, was the only v-amino acid racemized by the enzyme. The K_m values for L-tyrosine, z-DOPA, S-(o-nitrophenyl)-L-cysteine, β-chloro-L-alanine, and S-methyl-L-cysteine were 0.19, 9.9, 0.36, 12, and 5.5 mM, respectively.
Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus
( Pyo Jam Park ),( Sang Hoon Lee ),( Hee Guk Byun ),( Seo Hyun Kim ),( Se Kwon Kim ) 생화학분자생물학회 2002 BMB Reports Vol.35 No.6
Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and 55℃, respectively. The K_m and V_max of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by Hg^2+, Zn^2+, PMSF, TLCK, and the soybean-trypsin inhibitor.
Development of the Earth Observation Camera of MIRIS
Lee, Dae-Hee,Han, Won-Yong,Park, Young-Sik,Park, Sung-Jun,Moon, Bong-Kon,Ree, Chang-Hee,Pyo, Jeong-Hyun,Jeong, Woong-Seob,Nam, Uk-Won,Lee, Duk-Hang,Park, Kwi-Jong,Bae, Soo-Ho,Rhee, Seung-Wu,Park, Jong 한국우주과학회 2011 Journal of Astronomy and Space Sciences Vol.28 No.3
Sung, Moon-Hee,Lee, Seung-Goo,Hong, Seung-Pyo,Kwak, Mi-Sun,Nobuyoshi Esaki The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.5
Tyrosine phenol-lyase of thermophilic Symbiobacterium sp. SC-1, which is obligately and symbiotically dependent on thermophilic Bacillus sp. SK-1, was purified and characterized. The enzyme is composed of four identical subunits and contains approximately 1 mol of pyridoxal 5'-phosphate (PLP) per mol subunit as a cofactor. The enzyme showed absorption maxima at 330 and 420nm, and lost this absorption profile by treatment with phenylhydrazine. The apparent dissociation constsnt, K'??, for PLP was determined with the apoenzyme to be about 1.2 μM. The isoelectric point was 4.9. The optimal temperature and pH for the α,β-elimination of L-tyrosine were found to be 80℃ and pH 8.0, respectively. The substrate specificity of the enzyme was very broad: L-amino acids including L-tyrosine, 3,4-dihydroxyphenyl-L-alanine (L-DOPA), L-cysteine, L-serine, S-methyl-L-cysteine, β-chloro-S-alanine, and S-(o-nitrophenyl)-L-cysteine all served as substrates. D-Tyrosine and D-serine were also decomposed into pyruvic acid and ammonia at rates of 7% and 31% relative to their corresponding L-enantiomers, respectively. D-Alanine, which was inert as a substrate in α,β-elimination, was the only D-amino acid racemized by the enzyme. The K?? values for L-tyrosine, L-DOPA, S-(o-nitrophenyl)-L-cysteine, β-chloro-L-alanine, and S-methyl-L-cycsteine were 0.19, 9.9, 0.36, 12, and 5.5 mM, respectively.
Lee, Jung Eun,Lee, Ae Sin,Kim, Duk Hoon,Jung, Yu Jin,Lee, Sik,Park, Byung-Hyun,Lee, Sun Hwa,Park, Sung Kwang,Kim, Won,Kang, Kyung Pyo D.A. Spandidos 2012 International journal of molecular medicine Vol.29 No.5
<P>Vascular endothelial cells play an important role in leukocyte trafficking during the inflammatory process. Proinflammatory cytokines activate the expression of cell adhesion molecules in endothelial cells. Janus kinase (JAK) and signal transducer and activator of transcription (STAT) are important intracellular cytokine signaling molecules that are involved in immune responses. The purpose of this study was to investigate the effect of JAK3 inhibition on the expression of tumor necrosis factor (TNF)-α-induced cell adhesion molecules in vascular endothelial cells and to evaluate the therapeutic potential of JAK3 for myocardial vascular permeability in endotoxemic mice. A JAK3 inhibitor, JANEX-1, decreased the TNF-α-induced expression of intercellular adhesion molecule (ICAM)-1, VCAM (vascular cell adhesion molecule)-1 and fractalkine in human umbilical vein endothelial cells (HUVECs). The downregulation of the expression of these cell adhesion molecules by JANEX-1 was mediated via suppression of STAT3 phosphorylation and nuclear factor-κB (NF-κB) activation. In endotoxemic mice, pretreatment with JANEX-1 prevented not only an increase in the cardiac ICAM-1 expression by LPS in the arteriolar and capillary endothelial cells, but also myocardial vascular leakage. These results suggest that inhibition of the JAK/STAT pathway by JANEX-1 ameliorates the expression of TNF-α-induced cell adhesion molecules in HUVECs and improves myocardial vascular permeability.</P>
Lee, Seung-Pyo,Park, Sung-Ji,Kim, Yong-Jin,Chang, Sung-A,Park, Eun-Ah,Kim, Hyung-Kwan,Lee, Whal,Lee, Sang-Chol,Park, Seung Woo,Sohn, Dae-Won,Choe, Yeon-Hyeon BioMed Central 2013 Journal of cardiovascular magnetic resonance Vol.15 No.-
<P><B>Background</B></P><P>Severe aortic stenosis (AS) patients with late gadolinium enhancement (LGE) on cardiovascular magnetic resonance (CMR) or left ventricular (LV) systolic dysfunction are known to have worse outcome. We aimed to investigate whether LGE on CMR would be useful in early detection of subclinical LV structural and functional derangements in AS patients.</P><P><B>Methods</B></P><P>118 patients with moderate to severe AS were prospectively enrolled. Echocardiography and CMR images were taken and the patients were divided into groups according to the presence/absence of LGE and of LV systolic dysfunction (LV ejection fraction (EF) <50%). The stiffness of LV was calculated based on Doppler and CMR measurements.</P><P><B>Results</B></P><P>Patients were grouped into either group 1, no LGE and normal LVEF, group 2, LGE but normal LVEF and group 3, LGE with depressed LVEF. There was a significant trend towards increasing LV volumes, worsening of LV diastolic function (E/e’, diastolic elastance), systolic function (end-systolic elastance) and LV hypertrophy between the three groups, which coincided with worsening functional capacity (all p-value < 0.001 for trend). Also, significant differences in the above parameters were noted between group 1 and 2 (E/e’, 14.6 ± 4.3 (mean ± standard deviation) in group 1 vs. 18.2 ± 9.4 in group 2; end-systolic elastance, 3.24 ± 2.31 in group 1 vs. 2.38 ± 1.16 in group 2, all p-value < 0.05). The amount of myocardial fibrosis on CMR correlated with parameters of diastolic (diastolic elastance, Spearman’s ρ = 0.256, p-value = 0.005) and systolic function (end-systolic elastance, Spearman’s ρ = -0.359, p-value < 0.001).</P><P><B>Conclusions</B></P><P>These findings demonstrate the usefulness of CMR for early detection of subclinical LV structural and functional deterioration in AS patients.</P>
LEE, KYUNG-EUN,SHIN, JI-AE,HONG, IN-SUN,CHO, NAM-PYO,CHO, SUNG-DAE D.A. Spandidos 2013 Experimental and therapeutic medicine Vol.5 No.3
<P><I>Cnidium officinale</I> Makino and <I>Capsella bursa-pastoris</I> are used as traditional herbs with diverse medicinal effects, including the inhibition of inflammation, reduction of blood pressure and as diuretics, however, the anti-cancer effects of <I>C. officinale</I> Makino and <I>C. bursa-pastoris</I> are poorly defined. The aims of this study were to evaluate the effects of methanol extracts of <I>C. officinale</I> Makino (MECO) and methanol extracts of <I>C. bursa-pastoris</I> (MECB) on the cell growth and apoptosis of HSC-2 human oral cancer cells. MECO and MECB caused growth inhibition and the induction of apoptosis in a concentration-dependent manner in HSC-2 cells. A marked reduction in specificity protein 1 (Sp1) expression following treatment with MECO or MECB was also observed. The downregulation of Sp1 by siRNA resulted in growth inhibition and a reduction of total poly (ADP-ribose) polymerase (PARP) expression. In addition, MECO significantly increased Bax expression levels and MECB increased Bak expression levels and decreased Mcl-1 expression levels. These results suggest that MECO and MECB inhibit cell growth and induce apoptosis via the Sp1 protein, indicating that MECO and MECB are useful bioactive materials and attractive drug candidates for oral cancer.</P>
Lee, Jae Woong,Lee, Yong Kyoung,Ban, Jung Ok,Ha, Tae Youl,Yun, Yeo Pyo,Han, Sang Bae,Oh, Ki Wan,Hong, Jin Tae Wistar Institute of Anatomy and Biology 2009 The Journal of nutrition Vol.139 No.10
<P>Alzheimer's disease (AD) is characterized by the extracellular deposition of beta-amyloid peptide (Abeta) in cerebral plaques. Abeta is derived from the beta-amyloid precursor protein (APP) by the enzymes alpha-, beta- and gamma-secretase. Compounds that enhance alpha-secretase, but inhibit beta- or gamma-secretase activity, have therapeutic potential in the treatment of AD. Green tea, or its major polyphenolic compound, has been shown to have neuroprotective effects. In this study, we investigated the possible effects of (-)-epigallocatechin-3-gallate (EGCG) on memory dysfunction caused by Abeta through the change of Abeta-induced secretase activities. Mice were pretreated with EGCG (1.5 or 3 mg/kg body weight in drinking water) for 3 wk before intracerebroventricular administration of 0.5 microg Abeta(1-42). EGCG dose-dependently reduced the Abeta(1-42)-induced memory dysfunction, which was evaluated using passive avoidance and water maze tests. Abeta(1-42) induced a decrease in brain alpha-secretase and increases in both brain beta- and gamma-secretase activities, which were reduced by EGCG. In the cortex and the hippocampus, expression of the metabolic products of the beta- and gamma-secretases from APP, C99, and Abeta also were dose-dependently suppressed by EGCG. Paralleled with the suppression of beta- and gamma-secretases by EGCG, we found that EGCG inhibited the activation of extracellular signal-regulated kinase and nuclear transcription factor-kappaB in the Abeta(1-42)-injected mouse brains. In addition, EGCG inhibited Abeta(1-42)-induced apoptotic neuronal cell death in the brain. To further test the ability of EGCG to affect memory, EGCG (3 mg/kg body weight) was administered in drinking water for 1 wk to genetically developed preseniline 2 (PS2) mutant AD mice. Compared with untreated mutant PS2 AD mice, treatment with EGCG enhanced memory function and brain alpha-secretase activity but reduced brain beta- and gamma-secretase activities as well as Abeta levels. Moreover, EGCG inhibited the fibrillization of Abeta in vitro with a half maximal inhibitory concentration of 7.5 mg/L. These studies suggest that EGCG may be a beneficial agent in the prevention of development or progression of AD.</P>