• Title/Summary/Keyword: $5{\alpha}H,\

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Apigenin Inhibits Tumor Necrosis Factor-α-Induced Production and Gene Expression of Mucin through Regulating Nuclear Factor-Kappa B Signaling Pathway in Airway Epithelial Cells

  • Seo, Hyo-Seok;Sikder, Mohamed Asaduzzaman;Lee, Hyun Jae;Ryu, Jiho;Lee, Choong Jae
    • Biomolecules & Therapeutics
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    • v.22 no.6
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    • pp.525-531
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    • 2014
  • In the present study, we investigated whether apigenin significantly affects tumor necrosis factor-${\alpha}$ (TNF-${\alpha}$)-induced production and gene expression of MUC5AC mucin in airway epithelial cells. Confluent NCI-H292 cells were pretreated with apigenin for 30 min and then stimulated with TNF-${\alpha}$ for 24 h or the indicated periods. The MUC5AC mucin gene expression and mucin protein production were measured by reverse transcription - polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay (ELISA), respectively. Apigenin significantly inhibited MUC5AC mucin production and down-regulated MUC5AC gene expression induced by TNF-${\alpha}$ in NCI-H292 cells. To elucidate the action mechanism of apigenin, effect of apigenin on TNF-${\alpha}$-induced nuclear factor kappa B (NF-${\kappa}B$) signaling pathway was also investigated by western blot analysis. Apigenin inhibited NF-${\kappa}B$ activation induced by TNF-${\alpha}$. Inhibition of inhibitory kappa B kinase (IKK) by apigenin led to the suppression of inhibitory kappa B alpha ($I{\kappa}B{\alpha}$) phosphorylation and degradation, p65 nuclear translocation. This, in turn, led to the down-regulation of MUC5AC protein production in NCI-H292 cells. Apigenin also has an influence on upstream signaling of IKK because it inhibited the expression of adaptor protein, receptor interacting protein 1 (RIP1). These results suggest that apigenin can regulate the production and gene expression of mucin through regulating NF-${\kappa}B$ signaling pathway in airway epithelial cells.

Mossbauer studies of LiFeO2 powders by sol-gel process (졸겔 합성에 의한 LiFeO2분말의 Mossbauer 연구)

  • An, Sung-Yong;Kim, Chul-Sung
    • Journal of the Korean Magnetics Society
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    • v.14 no.2
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    • pp.71-75
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    • 2004
  • $\alpha$-LiFe $O_2$ powders have been prepared by a sol-gel method. The crystallographic and magnetic properties were characterized with a x-ray diffractometry, Mossbauer spectroscopy, and vibrating Samples magnetometry. The ${\gamma}$-LiFe $O_2$+LiFe$_{5}$ $O_{8}$ phase is observed in the Samples annealed at $600^{\circ}C$ for 3h in air and $\alpha$-LiFe $O_2$ phase is observed in the Samples annealed at $600^{\circ}C$ for 3 h in $H_2$(5%)/Ar(Bal.) gas atmosphere. The crystal structure of $\alpha$-LiFe $O_2$ is found to be cubic with a lattice a=4.193$\pm$0.0005 $\AA$. The Neel temperature of $\alpha$-LiFe $O_2$ is found to be 130$\pm$3 K.

Production and Characterization of New Structured-oligosaccharides from Mixed-enzyme of Dextransucrase and ${\alpha}$-amylase (Dextrnasucrase와 ${\alpha}$-amylase의 혼합효소를 이용한 새로운 구조의 올리고당 생산 및 특성 연구)

  • Lee, In-Su;Kim, Do-Man;Chang, Pahn-Shick
    • KSBB Journal
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    • v.14 no.6
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    • pp.707-712
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    • 1999
  • We have produced new-structured oligosaccharides using mixed-enzyme reactor of dextransucrase from Leuconostoc mesenterides B-512FMCM and ${\alpha}$-amylase. When the concentrations of sucrose and starch were 10%(w/v) and 5%(w/v), respectively, the maximum yield of oligosaccharides with both dextransucrase(100U) and ${\alpha}$-amylase(1000U) was 66.4%. The activity of dextransucrase in mixed-enzyme reactor was increased about 2.5 times by acceptor reaction with starch hydrolyzates. As the activities of dextransucrase:${\alpha}$-amylase were increased from 20U:200U to 500U:5000U, the amount of polymer was increased and the yield of oligosaccharides was decreased. By the addition of sucrose into mixed-enzyme reactor following the prehydrolysis of starch with ${\alpha}$-amylase, the yield was increased up to 12% compared with that of mixed-enzyme reactor without the addition of starch hydrolyzate. New structured-oligosaccharides showed heat resistance up to 140$^{\circ}C$ and was stable in acidic condition at pH 3~6.

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Studies on Synthesis and Heterocyclisation Reactions of Michael Products and Formation of New 1, 4-Thiazine Quinoxaline Derivatives

  • Mahgoub, S.A.
    • Archives of Pharmacal Research
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    • v.13 no.4
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    • pp.319-324
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    • 1990
  • Synthesis of $\alpha$-piperidino and $\alpha$-morphelino styryl quinoxalinone 2f, 2g respectively by facile one step method is reported. The Michael adducts (3a-d) obtained by the interaction of 2-styryl-2 (1H) quinoxalinone (2) and ethylacetoacetate have been treated with resorcino and hydroxylamine separately. With resorcinol the chromones (4) are obtained whereas with ydroxylamine isoxazoles (6) are the products. Michael addition of acetylacetone to 2 leads to 3-[1'-aryl-2'-(2'-hydroxy-3'-quinoxalinyl)ethyl]-2, 4-pentanediones (5) which undergo cyclisation with hydroxylamine to give isoxazoles (7). Addition of thiopenol and thioglycolic acid to 2 gives 3-$\alpha$[$\beta$-(phenyl)-$\beta$-(plenylthio)]ethyl-2(1H)-quinoxalinone (8) and 3-$\alpha$-[$\beta$-phenyl)-$\beta$-(hydroxycarbonylmethylithio)]-ethyl-2(1H)-qui noxalinone (9) respectively. 2-Bromomethyl-2(1H)-quinoxalinone (1b) reacts with thioglycolic acid to gives S-[2 (1H)-oxoquionoxaline-3-yl-methyl] mercaptoacetic acid (10) which on cyclisation with acetic anhydride/pyridine affords 1, 2, 5, 6-tetrahydro [1, 4]thiazino[4, 3-a] quinoxaline-1, 6-dione (11).

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Isolation of Thermostable ${\alpha}$-Amylase Hyperproducing Bacillus sp. No. 32H417 and Some Properties of the Enzyme (耐熱性 ${\alpha}$-Amylase 高 生産性 Bacillus sp. No. 32H417의 分離 및 酵素 特性)

  • Kim, Moo-Sung;O, Pyong-Su
    • Microbiology and Biotechnology Letters
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    • v.19 no.2
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    • pp.122-127
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    • 1991
  • A bacterial strain NO. 32 which produced thermostable ${\alpha}$-amylase was isolated from soil and identified to genus of Bacillus. To enhance ${\alpha}$-amylase productivity, a successive mutation of Bacillus sp. No. 32 was attempted with treatment of N-methyl-N'-nitro-N-nitrosoguanidine (NTG). The resulting mutant, Bacillus sp. No. 32H417, which is risistant to refampicin and deficient in spore formation, produced about 90-fold high level of ${\alpha}$-amylase when compared with parental strain. The properties of the enzyme for thermostability were investigated. The optimal temperature and pH for enzyme reaction were 95$^{\circ}C$ and pH6.5, respectively, in the presence of 0.3mM $Ca^{2+}$ as an effective stabilizer.

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Preparation and Maghemite Using Waste Pickling Acid (산세폐액을 이용한 Maghemite의 제조)

  • 변태봉;이재영;김대영;손진군;권순주
    • Journal of the Korean Ceramic Society
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    • v.28 no.12
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    • pp.996-1004
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    • 1991
  • In this study, we tried to synthesis iron hydroxide suitable for longitudinal magnetic recording media from waste acid, which is a by-product of an iron works factory. Effects of initial pH of reactants, reaction temperature, reaction time for the synthesis of acicular iron hydroxide were studied in relation to particle properties of iron hydroxide and magnetic properties of maghemite powders. As the pH in reactant solution increased, $\beta$-FeOOH(pH=4.5), mixture of $\beta$-FeOOH and $\alpha$-FeOOH(4.5$\alpha$-FeOOH and Fe3O4(6.4$\alpha$-FeOOH (pH>13) was found to from in order. Especially, $\alpha$-FeOOH formed above pH 13 was single phase with superior acicularity. The temperature range over which the single-phase goethite can be formed increased as the initial pH of reactants increased (pH 13:10~5$0^{\circ}C$, pH 13.2:10~7$0^{\circ}C$, pH 13.5:0~8$0^{\circ}C$). The goethite formed between 40~6$0^{\circ}C$ has superior characteristics because the acicularity increased with increasing temperature but at high temperature (>6$0^{\circ}C$) Fe3O4 (pH=13) was found to start to form. Generally, single phase of goethite was found to form after one hour when an optimized condition. The particle size of goethite did not change as the reaction time increased over one hour. Accordingly, the magnetic properties of ${\gamma}$-Fe2O3 produced from goethite were not altered.

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Isozyme Variants in Genus Pinus by Simulated Acidic Rain (인공 산성비가 소나무속의 동위효소 양상에 미치는 영향)

  • EuiSooYoon
    • Korean Journal of Plant Resources
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    • v.10 no.4
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    • pp.305-313
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    • 1997
  • The effect of acid rain on plant isozyme response was studied with the treatment of simulated acid rain to Pinus densiflora, P. nigida and P. koraiensis for 9 months. The isozyme pattern of $\alpha$-Esterase($\alpha$-Est), Peroxidase(POD) and Glutamate dehydrogenase(GDH) were observed in the control (pH 5.6) and simulated acid rain (pH 3.5) treatment. No changes of isozyme pattern in $\alpha$-Est was observed in P. densiflora after 9 month treatment of simulated acid rain, but, two new isozymes were activated in P. nigida in the same treatment. In P. koraiensis, two new isozyme were activated but five isozymes were not activated. P. densiflora did not show any difference in POD and GDH after the treatment of simulated acid rain. P. nigida showed activation of eight and two isozymes in POD and GDH, respectively. P. koraiensis showed inactivation of 4 isozymes in POD but showed no changes In GDH.

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Characteristics and Action Pattern of ${\alpha}-galactosidase$ from Scopulariopsis brevicaulis in Korean Traditional Meju (한국 재래 간장에서 분리한 Scopulariopsis brevicaulis가 생성하는 ${\alpha}-galactosidase$의 특성 및 작용양상)

  • Choi, Kwang-Soo;Lee, Seon-Ho;Hong, Seung-Pyo;Lee, Hee-Duck;Bae, Du-Kyung;Choi, Cheong
    • Applied Biological Chemistry
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    • v.41 no.7
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    • pp.489-495
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    • 1998
  • The optimum culture condition of Scopulariopsis brevicaulis for the production of ${\alpha}$-galactosidase was as follows: Tryptone 1.5%, $NH_4NO_3$ 0.2%, Raffinose 2.5%, $KH_2PO_4$ 0.5%, yeast extract 0.5%, pH 7.0, $27^{\circ}C$. The optimum pH and temperature for the enzyme activity of ${\alpha}$-galactosidase producing Scopulariopsis brevicaulis were pH 7.0 and $27^{\circ}C$, respectively. The enzyme was relatively stable at $pH\;6.0{\sim}8.0$ and at temperature below $40^{\circ}C$. The activity of the enzyme was inhibited by $Ag^{2+},\;Hg^{2+},\;Cu^{2+}$, p-chloromercuribenzoic acid and Iodine. These results would indicate the presence of -SH groups in the catalytic site of the enzyme. Km value was 1.9 mM for $p-nitrophenyl-{\alpha}-D-galactopyranoside$ and Vmax value was $9.66{\times}10^2\;{\mu}M/min$. Sugar constituents of culture broth were identified by HPLC that the enzyme liberated sucrose, glucose and fructose from raffinose and raffinose was significantly decreased.

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Purification and Biochemical Characterization of Carboxylesterase-III from Plodia interpunctella Hubner (화랑곡나방(Plodia interpunctella Hubner) Carboxylesterase-III의 정제 및 생화학적 특성)

  • 박희윤;유종명
    • Journal of the Korean Society of Tobacco Science
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    • v.21 no.2
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    • pp.160-170
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    • 1999
  • Purification and biochemical experiments on the carboxylesterases-III (CE-III) from the indian meal moth, Plodia interpunctella (Hubner) were carried out to understand their enzymemological characteristics. The CE-III from the fifth instar larvae was purified by means of ammonium sulfate fractionation, gel permeation choromatography and ion exchange choromatography. The optimal temperature for the reaction of the CE-III on the 4 substrates ($\alpha$-Na, $\alpha$-Nb, $\beta$-Na and $\beta$-Nb) was confirmed at 4$0^{\circ}C$. The optimal pH for the reactions on the substrates $\alpha$-Na and $\alpha$-Nb was 7.5. But the optimal pH on the substrate $\beta$-Na and $\beta$-Nb was 8.0. The optimal substrate concentration for the reactions of the CE-III was 3.16 X 10$^{-3}$ M in $\alpha$-Na and $\beta$-Nb. On the substrate $\beta$-Na and $\alpha$-Nb, the optimal substrate concentration was 1.0 X 10$^{-3}$ M for CE-III. The $V_{max}$ and $K_{m}$ values of the carboxylesterases were varied by the substrates as followings: the $V_{max}$ of CE-III was 45.9 for $\alpha$-Na, 52.6 for $\beta$-Na, 36.4 for $\alpha$-Nb, and 83.3 ($\mu$ mol/min/mg protein) for $\beta$-Nb. The $K_{m}$ of CE-III was 1.43 X 10$^{-4}$ M for $\alpha$-Na, 3.57 x 10$^{-5}$ M for $\beta$-Na, 9.17 X 10$^{-5}$ M for $\alpha$-Nb, and 7.14 X 10$^{-5}$ M for $\beta$ -Nb, respectively. The CE-III seemed to have somewhat high thermostability considering that the temperature for effective denaturation on activity was about 5$0^{\circ}C$ ~ 6$0^{\circ}C$.EX>.EX>.

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Studies on the Production of Enzymes by Thermophilic Actinomycetes Part I. Isolation and Culture Conditions of Thermostable $\alpha$-Amylase Producing Actinomycete (고온성 방선균에 의한 효소생산에 관한 연구 제 1보 $\alpha$-Amylase생산균의 분이 및 효소생산 조건)

  • 양한철;금범환;최용진
    • Microbiology and Biotechnology Letters
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    • v.3 no.2
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    • pp.73-82
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    • 1975
  • In the course of studies on the production of thermostable amylases by thermophilic actinomycetes isolated from soils the investigation was carried out on the production of $\alpha$-amylase by G-1011 strain which had presented the most remarkable $\alpha$-amylase formation ability among 128 amylolytic isolates. The results were as follows : 1. Characteristics of G-1011 strain were compared with those descriptions of thermophilic actinomycetes given in Bergey's Manual. The strain was identical to these species of actinomycetes. The details of physiological properties of the strain luould he published in near future. 2. The optimum temperature for incubation of the cell growth of G-1011 strain and $\alpha$-amylase production by the strain was revealed to 5$0^{\circ}C$. 3. The effective medium for $\alpha$-amylase formation by the strain was consisted of 3.0%, soluble starch, 1.0%, peptone, 0.5%, yeast extract, 0.5%, NaCl, 0.1%, MgSO$_4$ㆍ7$H_2O$ 0.02%, $K_2$MPO$_4$and 0.002% FeSO$_4$ㆍ7$H_2O$. The pH of the medium was ajusted to 7.0 with phosphate buffer solution. 4. The maximum production of $\alpha$-amylase (3420 D. U/ml) by G-1011 strain resulted when it was grown for 16 hours with the culture of reciprocal shaking.

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