Low Temperature Oligomerization of Ethylene over Ni/Al-KIT-6 Catalysts

Hwang, A.,Kim, S.,Kwak, G.,Kim, S. K.,Park, H. G.,Kang, S. C.,Jun, K. W.,Kim, Y. T. Springer Science + Business Media 2017 Catalysis letters Vol.147 No.6

<P>In this paper, we have studied the oligomerization of ethylene with a liquid heptane solvent over bifunctional Ni catalysts in a continuous flow reactor. We have prepared an Al-containing KIT-6 silica that was used as a support after calcination in the temperature range of 300-900 A degrees C. The Ni/Al-KIT-6 catalysts had uniform mesopores with diameters in the range of 5.4-6.3 nm, excepting Ni/Al-KIT-6 (900). The calcination temperature of Al-KIT-6 support changed the surface acidity as well as the interaction of Ni2+ and acid sites for the Ni catalysts, as determined by temperature-programmed desorption of ammonia, temperature-programmed reduction, infrared spectroscopy after the adsorption of pyridine, solid-state Al-27 magic-angle spinning nuclear magnetic resonance spectroscopy, and X-ray adsorption spectroscopy. Among the tested catalysts, the Ni/Al-KIT-6 (300) showed the highest ethylene conversion because of the increased intimate contact between Ni2+ and acid sites. The strong interaction of Ni2+ species and the support is not effective in increasing active sites for ethylene conversion. The Ni/Al-KIT-6 catalysts produced internal linear C4 and C6 olefins with high selectivity. The Ni/Al-KIT-6 (300) had 2.2-6.1 times lower selectivities toward 2-ethyl-1-butene than other catalysts at similar ethylene conversions. The reaction product mixture showed that the Ni/Al-KIT-6 catalysts shifted the product distribution towards acid-catalyzed oligomerization/cracking/realkylation products (i.e. C3, C7, C7, and C8+ olefins) as the concentration of Bronsted acid sites increased. Among the tested catalysts, the Ni/Al-KIT-6 (300) showed the highest yield of C4 and C6 olefins (78.3%).</P>

A peroxisome proliferator-activated receptor gamma agonist attenuates neurological deficits following spinal cord ischemia in rats

Kim, H.,Hwang, J.,Park, S.,Nahm, S.F.,Min, S.,Lim, C.,Park, K.,Han, S. C.V. Mosby Co 2014 Journal of Vascular Surgery Vol.59 No.4

Objective: Neuroprotective effects of the peroxisome proliferator-activated receptor gamma (PPARγ) agonist in cerebral ischemia have been reported, but the effect of a PPARγ agonist on spinal cord ischemia has not been investigated. The objective of this study was to investigate the effect of a PPARγ agonist on spinal cord ischemia. Pioglitazone, a PPARγ agonist, was administered in a rat model of spinal cord ischemia, and the extent of neurological damage and histological alterations were assessed. Methods: Forty-five rats were randomly enrolled into one of the three groups: (1) pioglitazone group (group PIO): rats were treated with pioglitazone 24 hours before ischemia; (2) control group (group C): rats were treated with the same volume of saline 24 hours before ischemia; and (3) sham group (group sham): rats were treated with the same volume of saline 24 hours before the sham surgery. Spinal cord ischemia was induced using a balloon-tipped catheter placed on the proximal descending aorta. Neurologic function was assessed using the motor deficit index (0 = normal, 6 = complete paralysis) during the 48 hours after reperfusion. Histological and biochemical evaluations were then performed. Results: Compared with group C, group PIO presented with lower motor deficit index 48 hours after reperfusion (5.0 [4.0-6.0] vs 3.0 [2.0-3.0]; group C vs group PIO, respectively; P < .001). Group PIO presented with a higher number of normal motor neurons (10.7 [8.1-11.9] vs 14.7 [14.0-15.3]; group C vs group PIO, respectively; P = .009) and a smaller area of infarcts (48.4% [46.3%-54.0%] vs 16.8% [11.5%-18.3%]; group C vs group PIO, respectively; P = .009) when compared with group C. The degree of inflammatory reactions, assessed by microglia activities, was significantly reduced in group PIO. Oxidative stress level, assessed using malonydialdehyde assay, was significantly reduced in group PIO relative to group C (192.21% [173.5%-206.4%] of sham vs 141.1% [131.7%-152.1%] of sham; group C vs group PIO, respectively; P = .007). The sham group exhibited no abnormality upon neurological or histological examination. Conclusions: PPARγ agonist pioglitazone pretreatment significantly reduces infarct volume and attenuates neurological deficits following spinal cord ischemia. The possible mechanism of neuroprotection by PPARγ agonist may involve modulation of inflammatory reaction and oxidative stress.

<i>Rhodococcus aerolatus</i> sp. nov., isolated from subarctic rainwater

Hwang, C. Y.,Lee, I.,Cho, Y.,Lee, Y. M.,Baek, K.,Jung, Y.-J.,Yang, Y. Y.,Lee, T.,Rhee, T. S.,Lee, H. K. International Union of Microbiological Societies 2015 International journal of systematic and evolutiona Vol.65 No.2

<P>A Gram-stain-positive, rod-shaped and non-motile strain, designated PAMC 27367<SUP>T</SUP>, was isolated from rainwater collected on the Bering Sea. Analysis of the 16S rRNA gene sequence of the strain showed an affiliation with the genus <I>Rhodococcus</I>. Phylogenetic analyses revealed that strain PAMC 27367<SUP>T</SUP> formed a robust clade with the type strains of <I>Rhodococcus rhodnii</I>, <I>Rhodococcus aetherivorans</I> and <I>Rhodococcus ruber</I> with 16S rRNA gene sequence similarities of 96.3 %, 95.8 % and 95.5 %, respectively. Cells of the strain grew optimally at 25 °C and at pH 6.5–7.0 in the presence of 0–2 % (w/v) sea salts. The major polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylethanolamine, phosphatidylinositol, phosphatidylinositol mannoside and three unknown phospholipids. The major cellular fatty acids (>10 %) were iso-C<SUB>16 : 0</SUB>, C<SUB>17 : 1</SUB>ω8<I>c</I> and 10-methyl C<SUB>17 : 0</SUB>. Cell wall analysis showed that strain PAMC 27367<SUP>T</SUP> contained <I>meso</I>-diaminopimelic acid. The genomic DNA G+C content was 77.1 mol%. Based on the phylogenetic, chemotaxonomic and phenotypic data presented here, we propose a novel species with the name <I>Rhodococcus</I> <I>aerolatus</I> sp. nov., with PAMC 27367<SUP>T</SUP> ( = KCTC 29240<SUP>T</SUP> = JCM 19485<SUP>T</SUP>) as the type strain.</P>

Effective suppression of C5a-induced proinflammatory response using anti-human C5a repebody

Hwang, D.E.,Choi, J.M.,Yang, C.S.,Lee, J.j.,Heu, W.,Jo, E.K.,Kim, H.S. Academic Press 2016 Biochemical and biophysical research communication Vol.477 No.4

The strongest anaphylatoxin, C5a, plays a critical role in the proinflammatory responses, causing the pathogenesis of a number of inflammatory diseases including sepsis, asthma, and rheumatoid arthritis. Inhibitors of C5a thus have great potential as therapeutics for various inflammatory disorders. Herein, we present the development of a high-affinity repebody against human C5a (hC5a), which effectively suppresses the proinflammatory response. A repebody scaffold composed of leucine-rich repeat (LRR) modules was previously developed as an alternative protein scaffold. A repebody specifically binding to hC5a was selected through a phage display, and its affinity was increased up to 5 nM using modular engineering. The repebody was shown to effectively inhibit the production of C5a-induced proinflammatory cytokines by human monocytes. To obtain insight into a mode of action by the repebody, we determined its crystal structure in complex with hC5a. A structural analysis revealed that the repebody binds to the D1 and D3 regions of hC5a, overlapping several epitope residues with the hC5a receptor (hC5aR). It is thus likely that the repebody suppresses the hC5a-mediated immune response in monocytes by blocking the binding of hC5a to its receptor. The anti-hC5a repebody can be developed as a potential therapeutic for C5a-involved inflammatory diseases.

O-free polyacrylonitrile doping to improve the J_c(B) and H_c2 of MgB₂ wires

Hwang, S.M.,Sung, K.,Choi, J.H.,Kim, W.,Joo, J.,Lim, J.H.,Kim, C.J.,Park, Y.S.,Kim, D.H. North-Holland 2010 Physica. C, Superconductivity Vol.470 No.20

We selected polyacrylonitrile (PAN, -[C<SUB>3</SUB>H<SUB>3</SUB>N]-) as an O-free organic dopant and fabricated C-doped MgB<SUB>2</SUB> wires by in situ and powder-in-tube techniques. 0-5 wt.% PAN powders were uniformly mixed with B powder using a liquid mixing method. The precursor powders were mixed with Mg powder, filled into Fe tubes, and then drawn into wires. Sintering was performed at 900<SUP>o</SUP>C for 1h in a flowing Ar gas. The PAN doping decreased the critical temperature (T<SUB>c</SUB>) and a-axis lattice parameter, but significantly improved the critical current density (J<SUB>c</SUB>) in high fields, upper critical field (H<SUB>c2</SUB>), and irreversibility field (H<SUB>irr</SUB>) performances. These results are attributed to the replacement of B sites with C by the PAN doping. Furthermore, as expected, the MgO amount did not increase as the doping content increased. The J<SUB>c</SUB> of the PAN-doped MgB<SUB>2</SUB> wires was more than one order of magnitude higher than that of the undoped MgB<SUB>2</SUB> wire at 5K and 6.6T (1.46-3.82kA/cm<SUP>2</SUP> vs. 0.11kA/cm<SUP>2</SUP>).

Solubility of oxcarbazepine in eight solvents within the temperature range T=(288.15-308.15)K

Nam, K.,Ha, E.S.,Kim, J.S.,Kuk, D.H.,Ha, D.H.,Kim, M.S.,Cho, C.W.,Hwang, S.J. Academic Press 2017 The Journal of chemical thermodynamics Vol.104 No.-

In this study, the solubility of oxcarbazepine in pure methanol, ethanol, 1-propanol, 2-propanol, 1-butanol, acetone, acetonitrile, and tetrahydrofuran was analysed across the temperature range of 288.15-308.15K under atmospheric pressure by using a solid-liquid equilibrium method. The experimental values obtained data were correlated using the modified Apelblat model at each temperature. The mole fraction solubility of oxcarbazepine in all eight pure solvents increased gradually in a temperature-dependent manner. The highest mole fraction solubility of 3.08x10<SUP>-3</SUP> at 308.15K was observed for tetrahydrofuran, followed by acetone (1.82x10<SUP>-3</SUP> at 308.15K), acetonitrile (1.22x10<SUP>-3</SUP> at 308.15K), methanol (1.11x10<SUP>-3</SUP> at 308.15K), ethanol (6.17x10<SUP>-4</SUP> at 308.15K), 1-butanol (6.17x10<SUP>-4</SUP> at 308.15K), 1-propanol (6.16x10<SUP>-4</SUP> at 308.15K), and 2-propanol (4.13x10<SUP>-4</SUP> at 308.15K). The experimental solubility in all solvents correlated well with that calculated using the modified Apelblat equation across the temperature range of (288.15-308.15)K. Therefore, the experimental solubility and correlation equations established in this study could be useful during the crystallization/purification, pre-formulation, and formulation stages of oxcarbazepine production in laboratories and related industries.

Novel dentin phosphoprotein frameshift mutations in dentinogenesis imperfecta type II

Lee, K‐,E,Kang, H‐,Y,Lee, S‐,K,Yoo, S‐,H,Lee, J‐,C,Hwang, Y‐,H,Nam, KH,Kim, J‐,S,Park, J‐,C,Kim, J‐,W Blackwell Publishing Ltd 2011 Clinical genetics Vol.79 No.4

<P>Lee K‐E, Kang H‐Y, Lee S‐K, Yoo S‐H, Lee J‐C, Hwang Y‐H, Nam KH, Kim J‐S, Park J‐C, Kim J‐W. Novel dentin phosphoprotein frameshift mutations in dentinogenesis imperfecta type II.</P><P>The dentin sialophosphoprotein (<I>DSPP</I>) gene encodes the most abundant non‐collagenous protein in tooth dentin and DSPP protein is cleaved into several segments including the highly phosphorylated dentin phosphoprotein (DPP). Mutations in the <I>DSPP</I> gene have been solely related to non‐syndromic form of hereditary dentin defects. We recruited three Korean families with dentinogenesis imperfecta (DGI) type II and sequenced the exons and exon–intron boundaries of the <I>DSPP</I> gene based on the candidate gene approach. Direct sequencing of PCR products and allele‐specific cloning of the highly repetitive exon 5 revealed novel single base pair (bp) deletional mutations (c.2688delT and c.3560delG) introducing hydrophobic amino acids in the hydrophilic repeat domain of the DPP coding region. All affected members of the three families showed exceptionally rapid pulp chambers obliteration, even before tooth eruption. Individuals with the c.3560delG mutation showed only mild, yellowish tooth discoloration, in contrast to the affected individuals from two families with c.2688delT mutation. We believe that these results will help us to understand the molecular pathogenesis of DGI type II as well as the normal process of dentin biomineralization.</P>

2, 4-Thiazolidindion Induced Plasticity of Myoblast (C2C12) and Satellite Cells (Porcine) - A Comparative Study

Singh, N.K.,Chae, H.S.,Hwang, I.H.,Yoo, Y.M.,Ahn, C.N.,Lee, H.J.,Park, H.J.,Chung, H.Y. Asian Australasian Association of Animal Productio 2007 Animal Bioscience Vol.20 No.7

This study was conducted to determine the difference between satellite cells (porcine) and myoblasts (C2C12) in their differentiation under the influence of 2, 4-thiazolidindion. C2C12 myoblast cells and porcine satellite cells (isolated from 10 d old $Landrace{\times}Duroc$ piglets) were grown to absolute confluency. Post confluent cells (day 0) were further exposed to adipogenic induction medium along with 2, 4-thiazolidindion ($8{\mu}M$) for 2 d. Thereafter, cells were exposed to 2, 4-thiazolidindion alone every 2 d till day 10 and analysed. The control was cultured in differentiation medium without any treatment. Increased (p<0.05) expression of transcriptional factors i.e. C/EBP-${\alpha}$ and PPAR-${\gamma}$ and transition of cells to adipocyte morphology was noticed from 2 d and 4 d onwards in satellite cells (Porcine) and myoblasts (C2C12) respectively. Myogenesis was observed to be suppressed completely in case of satellite cells compared to myoblasts in response to 2, 4-thiazolidindion. Pax-7 (transcriptional factor) appeared as a sole entity to satellite cells only, as it was not identified in case of myoblasts. Although both the cells were converting to adipoblasts, the degree of their conversion was different in response to 2, 4-thiazolidindion. Therefore, the hypothesis that satellite cells contribute various domains to the growing myoblasts appeared obscured and found to be dependent on the proliferative energy/or degree of fusion. However, it revealed satellite cells as currency to myoblasts/muscle.

Conversion of C2C12 Myoblast into Adipoblast with Thiazolidinediones - A Possible Basis for Intramuscular Fat Generation in Meat Animals

Singh, N.K.,Chae, H.S.,Hwang, I.H.,Yoo, Y.M.,Ahn, C.N.,Lee, H.J.,Park, H.J.,Chung, H.Y. Asian Australasian Association of Animal Productio 2007 Animal Bioscience Vol.20 No.3

Thiazolidinediones (TZDs) act as potent activators of the adipose differentiation program in established preadipose cell lines. TZD's have also been investigated in diabetic patients and reported to act as PPAR-${\gamma}$ ligands. In this report, the effects of TZDs on the differentiation pathway of myoblasts have been investigated. C2C12 mouse myoblasts were grown in Dulbecco's Modified Eagles medium for 4-5 days until they reached almost 100% confluency. Post-confluent cells (day 0) were further exposed to adipogenic induction medium along with TZDs for 48 hours. Thereafter, cells were exposed only to TZDs every 48 h until day 10. The control was provided with differentiation medium without any treatment. Alterations in the cells during the differentiation programme were analyzed on the basis of fusion index, oil-red-o staining, adipocyte index, adipocyte stain uptake measurement, immuno-histochemistry and western blotting. Exposure of C2C12 mouse myoblasts to TZDs prevented the expression of myosin heavy chain with parallel increase in the expression of C/EBP-${\alpha}$ and PPAR-${\gamma}$ and acquisition of adipocyte morphology, thus abolishing the formation of multinucleated myotubes. TZDs exert their adipogenic effects only in non-terminally differentiated myoblasts; myotubes were insensitive to the compound. Continuous exposure (at least 4-5 doses) to inducers after the growth arrest was essential to provide a sustained environment to the cells converting to fully matured adipoctyes. The results indicate that TZDs specifically converted the differentiation pathway of myoblasts into that of adipoblasts.

FAM83H mutations cause ADHCAI and alter intracellular protein localization.

Lee, S-K,Lee, K-E,Jeong, T-S,Hwang, Y-H,Kim, S,Hu, J C-C,Simmer, J P,Kim, J-W Journal of Dental Research, Inc 2011 Journal of dental research Vol.90 No.3

<P>Mutations in a family with sequence similarity 83 member H (FAM83H) cause autosomal-dominant hypocalcification amelogenesis imperfecta (ADH CAI). All FAM83H ADHCAI-causing mutations terminate translation or shift the reading frame within the specific exon 5 segment that encodes from Ser(287) to Glu(694). Mutations near Glu(694) cause a milder, more localized phenotype. We identified disease-causing FAM83H mutations in two families with ADHCAI: family 1 (g.3115C>T, c.1993 C>T, p.Q665X) and family 2 (g.3151C>T, c.2029 C>T, p.Q677X). We also tested the hypothesis that truncation mutations alter the intracellular localization of FAM83H. Wild-type FAM83H and p.E694X mutant FAM83H fused to green fluorescent protein (GFP) localized in the cytoplasm of HEK293T cells, but the mutant FAM83H proteins (p.R325X, p.W460X, and p.Q677X) fused to GFP localized mainly in the nucleus with slight expression in the cytoplasm. We conclude that nuclear targeting of the truncated FAM83H protein contributes to the severe, generalized enamel phenotype.</P>