34 research outputs found

    Proinflammatory cytokines changes among the control, HF, and HF+GTP groups.

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    <p>Results are expressed as mean±SE. # P<0.05 between the HF and HF+GTP groups.</p

    Western blot analyses of protein expression in the control, HF, and HF+GTP groups.

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    <p>(A) Effects of HF and HF+GTP treatment on the protein expression of SOD1. (B) Effects of HF and HF+GTP treatment on the protein expression of COMT. Blots were also probed for α-tubulin to confirm equal protein loading. The relative protein intensities of SOD1 and COMT were compared with the intensity of α-tubulin. The intensity of each band was quantified using Quantity One software. Data are means±SE, n = 3. The experiments were conducted in triplicate. * P<0.05 between the control and HF groups; ** P<0.01 between the control and HF groups; ## P<0.01 between HF and HF+GTP; ∧∧P<0.01 between the control and HF+GTP groups.</p

    The symbol and description of genes in the PCR array.

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    <p>The symbol and description of genes in the PCR array.</p

    Body weight in female rats supplemented with green tea polyphenols (GTP) in drinking water for 4 months.

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    <p>Body weight (g) of the control, HF, and HF+GTP treated rats at 0–8 months. Values are mean (n = 10–12) with their standard error (SE) represented by vertical bars. * P<0.05 between the control and HF groups; # P<0.05 between the HF and HF+GTP groups; ∧P<0.01 between the control and HF+GTP groups.</p

    The changes of obesity-related genes among the control, HF, and HF+GTP groups.

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    <p>(A) Representative PCR array gene tables of undetected genes and detected genes. (B) The heat map demonstrating fold regulation expression data between the HF group and the control group. Genes with significant differences between two groups are shown in the histogram. (C) The heat map demonstrating fold regulation expression data between the HF+GTP group and the HF group. Genes with significant differences between two groups are shown in the histogram. (D) The heat map demonstrating fold regulation expression data between the HF+GTP group and the control group. Genes with significant differences between two groups are shown in the histogram.</p

    Rat obesity PCR Array.

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    <p>(A) Functional gene grouping in 3 colors: orexigenic genes in red, anorectic genes in yellow, and genes involved in energy expenditure in green. (B) The C<sub>T</sub> value of quality control used rat genomic DNA.</p

    Nuclear proteome profiling in A549 cells after DOX and/or LMB treatment.

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    <p>A, Western blot of nuclear and cytoplasmic protein extractions from A549; α-tubulin served as an internal control for cytoplasmic proteins, and histone 3 served as a control for nuclear proteins. B, 2D-DIGE analyses of nuclear proteins in A549 cells and 3D views of SQSTM1 in A549 cell with vehicle control or LMB treatment. Nuclear proteins treated with LMB or vehicle control were labeled with Cy3 (green channel) and Cy5 (red channel), respectively. Nuclear proteins were separated based on isoelectric point (PI, horizontal axis) and molecular weight (MW, vertical axis). Approximately 1,000 protein spots were detected in nuclear extractions of A549 cells. Spots labeled with red color indicate decreased expression after LMB treatment, while spots labeled with green color indicate increased expression after LMB treatment (left panel). Magnification of 5 protein spots (right upper panel) and 3D view of vehicle control and LMB treated (right bottom panel) (identified by LC/MS/MS as sequestosome 1 (SQSTM1/p62)). C, Protein sequence and tandem mass spectrometry identification of SQSTM1. The MS/MS fragmentation spectrum (obtained after trypsin digestion) of AYLLGKEDAAR for SQSTM1 is shown. The resultant MS/MS data were processed using Mascot. D, Western blot analysis of SQSTM1 in cytoplasm and nucleus of A549 cells after LMB treatment. E, Effects of LMB alone or pre-DOX+LMB treatment on protein expression of SQSTM1 in A549 cells. The relative protein intensity of SQSTM1 was compared with the intensity of corresponding α-tubulin. The intensity of each band was quantified using Quantity One software. Data are means ± SD. Experiments were conducted in triplicate. LMB1: 1 nM LMB; LMB5: 5 nM LMB; **, <i>P</i><0.001 compared to control.</p

    Novel Ultrathin Nanoflake Assembled Porous MnO<sub>2</sub>/Carbon Strip Microspheres for Superior Pseudocapacitors

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    A novel hierarchical MnO<sub>2</sub>/carbon strip (MnO<sub>2</sub>/C) microsphere is synthesized via galvanostatic charge–discharge of a MnO@C matrix precursor where the carbon is from a low-cost citric acid. This hierarchical structure is composed of manganese oxides nanoflakes and inlaid carbon strips. The ultrathin nanoflakes assemble to form porous microspheres with a rippled surface superstructure. Due to its improved conductivity and remarkable increased phase contact area, this novel structure exhibits an excellent electrochemical performance with a specific capacitance of 485.6 F g<sup>–1</sup> at a current density of 0.5 A g<sup>–1</sup> and an area capacitance as high as 4.23 F cm<sup>–2</sup> at a mass loading of 8.7 mg cm<sup>–2</sup>. It also shows an excellent cycling stability with 88.9% capacity retention after 1000 cycles. It is speculated that the present low-cost novel hierarchical porous microspheres can serve as a promising electrode material for pseudocapacitors

    Effects of DOX and LMB on cell cycle and apoptosis of A549 cells.

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    *<p><i>P</i><0.05 in comparison to control;</p>**<p><i>P</i><0.01 in comparison to control.</p>#<p><i>P</i><0.05 in comparison to LMB alone;</p>##<p><i>P</i><0.01 in comparison to LMB alone.</p

    Western blot analyses of protein expression in A549 cells after DOX and LMB treatment.

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    <p>A, Effects of pre-DOX+LMB treatment on the protein expression of p53, phospho-p53 (Ser15), phospho-p53 (Thr55), p21, and survivin in A549. Cells were treated with 0.5 µM DOX 24 h before treatment with LMB (1 nM or 5 nM). After 48 h LMB treatment, cells were harvested for Western blot analysis to determine protein levels. Blots were also probed for α-tubulin to confirm equal protein loading. B, The relative protein intensities of p53, phospho-p53 (Ser15), phospho-p53 (Thr55), p21, and survivin as compared with the intensity of α-tubulin. The intensity of each band was quantified using Quantity One software. Data are means ± SD, n = 3. The experiments were conducted in triplicate. LMB1: 1 nM LMB; LMB5: 5 nM LMB; *, <i>P</i><0.05 compared to control; **, <i>P</i><0.01 compared to control; #, <i>P</i><0.05, compared to LMB5; ##, <i>P</i><0.01, compared to LMB5.</p
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