10 research outputs found

    Facile Method to Prepare for the Ni<sub>2</sub>P Nanostructures with Controlled Crystallinity and Morphology as Anode Materials of Lithium-Ion Batteries

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    Conversion reaction materials (transition metal oxides, sulfides, phosphides, etc.) are attractive in the field of lithium-ion batteries because of their high theoretical capacity and low cost. However, the realization of these materials in lithium-ion batteries is impeded by large voltage hysteresis, high polarization, inferior cycle stability, rate capability, irreversible capacity loss in first cycling, and dramatic volume change during redox reactions. One method to overcome these problems is the introduction of amorphous materials. This work introduces a facile method to synthesize amorphous and crystalline dinickel phosphide (Ni<sub>2</sub>P) nanoparticle clusters with identical morphology and presents a direct comparison of the two materials as anode materials for rechargeable lithium-ion batteries. To assess the effect of crystallinity and hierarchical structure of nanomaterials, it is crucial to conserve other factors including size, morphology, and ligand of nanoparticles. Although it is rarely studied about synthetic methods of well-controlled Ni<sub>2</sub>P nanomaterials to meet the above criteria, we synthesized amorphous, crystalline Ni<sub>2</sub>P, and self-assembled Ni<sub>2</sub>P nanoparticle clusters via thermal decomposition of nickelā€“surfactant complex. Interestingly, simple modulation of the quantity of nickel acetylacetonate produced amorphous, crystalline, and self-assembled Ni<sub>2</sub>P nanoparticles. A 0.357 M nickelā€“trioctylphosphine (TOP) solution leads to a reaction temperature limitation (āˆ¼315 Ā°C) by the nickel precursor, and crystalline Ni<sub>2</sub>P (c-Ni<sub>2</sub>P) nanoparticles clusters are generated. On the contrary, a lower concentration (0.1 M) does not accompany a temperature limitation and hence high reaction temperature (330 Ā°C) can be exploited for the self-assembly of Ni<sub>2</sub>P (s-Ni<sub>2</sub>P) nanoparticle clusters. Amorphous Ni<sub>2</sub>P (a-Ni<sub>2</sub>P) nanoparticle clusters are generated with a high concentration (0.714 M) of nickelā€“TOP solution and a temperature limitation (āˆ¼290 Ā°C). The a-Ni<sub>2</sub>P nanoparticle cluster electrode exhibits higher capacities and Coulombic efficiency than the electrode based on c-Ni<sub>2</sub>P nanoparticle clusters. In addition, the amorphous structure of Ni<sub>2</sub>P can reduce irreversible capacity and voltage hysteresis upon cycling. The amorphous morphology of Ni<sub>2</sub>P also improves the rate capability, resulting in superior performance to those of c-Ni<sub>2</sub>P nanoparticle clusters in terms of electrode performance

    Orphan nuclear receptor ERRĪ³ is a key regulator of human fibrinogen gene expression

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    <div><p>Fibrinogen, 1 of 13 coagulation factors responsible for normal blood clotting, is synthesized by hepatocytes. Detailed roles of the orphan nuclear receptors regulating fibrinogen gene expression have not yet been fully elucidated. Here, we identified estrogen-related receptor gamma (ERRĪ³) as a novel transcriptional regulator of human fibrinogen gene expression. Overexpression of ERRĪ³ specially increased fibrinogen expression in human hepatoma cell line. Cannabinoid receptor types 1(CB1R) agonist arachidonyl-2'-chloroethylamide (ACEA) up-regulated transcription of fibrinogen via induction of ERRĪ³, whereas knockdown of ERRĪ³ attenuated fibrinogen expression. Deletion analyses of the fibrinogen Ī³ (FGG) gene promoter and ChIP assays revealed binding sites of ERRĪ³ on human fibrinogen Ī³ gene promoter. Moreover, overexpression of ERRĪ³ was sufficient to increase fibrinogen gene expression, whereas treatment with GSK5182, a selective inverse agonist of ERRĪ³ led to its attenuation in cell culture. Finally, fibrinogen and ERRĪ³ gene expression were elevated in liver tissue of obese patients suggesting a conservation of this mechanism. Overall, this study elucidates a molecular mechanism linking CB1R signaling, ERRĪ³ expression and fibrinogen gene transcription. GSK5182 may have therapeutic potential to treat hyperfibrinogenemia.</p></div

    Patients with NAFLD/NASH exhibit elevated ERRĪ³ and fibrinogen expression in the liver.

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    <p><b>(A)</b> Left: representative immunohistochemistry results for ERRĪ³ expression in liver tissue, as identically found in all three analysed patients with NASH. Right: serial sections of steatotic liver tissue showing colocalization of ERRĪ³ and Fibrinogen staining. <b>(B)</b> Fibrinogen levels in blood of healthy controls and overweight patients. <b>(C)</b> qPCR analysis showing mRNA levels of hepatic fibrinogen gamma and ERRĪ³ in liver tissue of healthy controls and patients with NAFLD. * <i>p</i><0.05, ** <i>p</i><0.01. <b>(D)</b> Proposed model for CB1 receptorā€“mediated induction of fibrinogen gene expression via ERRĪ³. Activation of hepatic CB1 receptor increases ERRĪ³ gene expression, which in turn leads to fibrinogen expression causing hyperfibrinogenemia. GSK5182, an ERRĪ³ inverse agonist, inhibits CB1 receptorā€“mediated fibrinogen gene expression.</p

    Inverse agonist of ERRĪ³ inhibits ACEA-mediated fibrinogen gene expression in Huh7 cells.

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    <p><b>(A)</b> GSK5182 decreased ACEA-mediated FGG promoter activity. Huh7 cells were transfected with vectors expression hFGG-luc, and then treated with ACEA (10 Ī¼M) and/or GSK5182 (10 Ī¼M). <b>(B-E)</b> GSK5182 inhibited ACEA-mediated fibrinogen expression and secretion in human hepatoma cell line. Huh7 and HepG2 cells were treated with ACEA (10 Ī¼M) for 12 h. The cell culture medium was replaced, and GSK5182 (10 Ī¼M) was added for the final 24 h. Total mRNA and protein were extracted for qPCR (B-C) and western blot analyses (D). Cell culture media were collected to determine fibrinogen levels in Huh7 cells (E). <b>(F)</b> GSK5182 specifically inhibits ERRĪ³ transcriptional activity. Huh7 cells were infected with Ad-GFP, Ad-ERRĪ³, or Ad-ERRĪ³ Y326A and then treated with GSK5182 (10 Ī¼M) for 24 h. Fibrinogen mRNA levels were analyzed by qPCR. * <i>p</i><0.05, ** <i>p</i><0.01. All data are representative of at least three independent experiments. Western blot images were cropped with a black cropping line. All gels for Western blot analysis were run under the same experimental conditions. Full uncropped blots are available as <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0182141#pone.0182141.s004" target="_blank">S2 Fig</a>. Error bars show SEM.</p

    Knockdown of ERRĪ³ attenuates ACEA-mediated induction of fibrinogen.

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    <p><b>(A)</b> ACEA-mediated induction of fibrinogen expression. Huh7 cells were treated with ACEA (10 Ī¼M) for the indicated time periods. Total RNAs were extracted for qPCR analyses. <b>(B-C)</b> Huh7 cells were treated with ACEA (10 Ī¼M) for 24 h. Total protein was extracted for western blotting (B). Cell culture media were collected to determine fibrinogen levels (C). * <i>p</i><0.05, ** <i>p</i><0.01. All data are representative of at least three independent experiments. Error bars show SEM. <b>(D)</b> Huh7 cells were treatment with ACEA in the continued presence or absence of AM251 for 24 h. qPCR were performed to measure mRNA levels. * <i>p</i><0.05. ** <i>p</i><0.01. <b>(E-G)</b> qPCR (E) and western blot (F) analysis showing mRNA and protein levels of ERRĪ³, FGA, FGB, and FGG in Huh7 cells. Huh7 cells were infected with Ad-Usi or Ad-shERRĪ³ for 48 h, followed by treatment with ACEA (10 Ī¼M). Cell culture media were collected to determine fibrinogen levels (G).Western blot images were cropped with a black cropping line. All gels for Western blot analysis were run under the same experimental conditions. Full uncropped blots are available as <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0182141#pone.0182141.s003" target="_blank">S1</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0182141#pone.0182141.s004" target="_blank">S2</a> Figs.</p

    ACEA induces <i>FGF21</i> gene expression.

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    <p>(Aā€“C) HepG2 cells, rat primary hepatocytes (RPH), and AML12 cells were treated with ACEA (10 Ī¼M) for the indicated time periods. (D) Wild-type or CB1<sup>-/-</sup> mouse primary hepatocytes (MPH) were treated with ACEA (10 Ī¼M) for 3 h. (E) Mice were treated with ACEA (10 mg/kg) for the indicated number of days. Livers were harvested for mRNA analysis. (Aā€“E) <i>FGF21</i> and <i>ERRĪ³</i> mRNA levels were measured by quantitative qPCR analysis and normalized to <i>actin</i> mRNA levels. All data are the means Ā± standard errors of at least three independent experiments. *p < 0.05; **p < 0.01; ***p < 0.001 by one-way ANOVA.</p

    ERRĪ³ directly regulates fibrinogen gene transcription.

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    <p><b>(A)</b> ERRĪ³-specific induction of human FGG promoter activity. 293T cells were transfected with vectors expressing human FGG-luc and ERRĪ±, ERRĪ², and ERRĪ³. <b>(B)</b> ERRĪ³ induced human <i>FGA</i> and <i>FGB</i> promoters. 293T cells were transfected with vectors expressing human FGA-luc or FGB-luc and ERRĪ³. <b>(C)</b> Mapping of the human <i>FGG</i> promoter. 293T cells were transfected with deletion constructs of hFGG-luc and ERRĪ³. <b>(D)</b> ERRE-dependent activation of the human <i>FGG</i> promoter. 293T cells were transiently transfected with pCDNA3-FLAG-ERRĪ³, hFGG-luc (WT), hFGG-Luc (MT ERRE). <b>(E)</b> ERRE is required for ACEA-mediated activation of the human <i>FGG</i> promoter. Huh7 cells were transfected with vectors expressing hFGG-luc (WT) or hFGG-luc (MT ERRE) and treated with ACEA (10 Ī¼M) at 36 h post transfection. Experiments in <b>A-E</b> were conducted in triplicate, and data are expressed as fold activation relative to the control. * <i>p</i><0.05, ** <i>p</i><0.01, *** <i>p</i><0.001. <b>(F)</b> ChIP assay showing occupancy of the ERRE from the human <i>FGG</i> promoter by ERRĪ³. Huh7 cells were infected with Ad-GFP or Ad-ERRĪ³ for 48 h. Input represents 10% of purified DNA in each sample. Cell extracts were immunoprecipitated with IgG or ERRĪ³ antibody, and purified DNA samples were employed for PCR with primers encompassing the ERRE (-1.0 kb to -0.8 kb) and a distal site (-1.9 kb to -1.7 kb) of the <i>FGG</i> gene promoter. Error bars show SEM. The gel images were cropped with a black cropping line. Full uncropped gels are available as <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0182141#pone.0182141.s005" target="_blank">S3 Fig</a>. All gels for ChIP analysis were run under the same experimental conditions.</p

    GSK5182 inhibits ACEA-mediated induction of <i>FGF21</i> gene expression.

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    <p>(A) AML12 cells were transfected with mFGF21-Luc and treated with ACEA (10 Ī¼M) for 3 h with or without GSK5182 (10 Ī¼M). (Bā€“D) HepG2 cells, AML12 cells, and mouse primary hepatocytes (MPH) were treated with ACEA (10 Ī¼M) for 3 h with or without GSK5182 (10 Ī¼M). (E and G) GSK5182 (40 mg/kg) was administrated to male C57BL/6J mice (n = 3ā€“4 per group) daily by intraperitoneal injection for 4 days. ACEA (10 mg/kg) was also given by intraperitoneal injection daily during the final 3 days. (Aā€“D) <i>FGF21</i> and <i>ERRĪ³</i> mRNA levels were measured by qPCR analysis and normalized to <i>actin</i> mRNA levels. (F) AML12 cells were treated with ACEA (10 Ī¼M) for 3 h with or without GSK5182 (10 Ī¼M). Culture media was recovered for FGF21 secretion analysis. (G) Male C57BL/6J mice (n = 3) were treated with ACEA (10 mg/kg) with and without GSK5182 (40 mg/kg) daily for 3 days. Serum was analyzed for FGF21 secretion. (H) Male C57BL/6J mice (n = 5 per group) were fed an alcohol-containing diet for 4 weeks and GSK5182 (40mg/kg once daily) was given by oral gavage for the final 2 weeks of alcohol feeding. (I) Schematic diagram of ERRĪ³-mediated <i>FGF21</i> gene expression. GSK5182 inhibits activation of <i>FGF21</i> gene expression and FGF21 secretion mediated by increased ERRĪ³ caused by activation of the hepatic CB1 receptor. All data are the means Ā± standard errors for at least three independent experiments. *p < 0.05; **p < 0.01; ***p < 0.001 by one-way ANOVA.</p

    ERRĪ³ overexpression induces <i>FGF21</i> gene expression.

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    <p>(Aā€“C) HepG2 cells, AML12 cells, and mouse primary hepatocytes (MPH) were infected with Ad-GFP and Ad-ERRĪ³. (D) Ad-GFP or Ad-ERRĪ³ was injected into male C57BL/6J mice via the tail vein. Mice were sacrificed at 5 days after injection. (Aā€“D) <i>FGF21</i> and <i>ERRĪ³</i> mRNA levels were measured by quantitative qPCR analysis and normalized to <i>actin</i> mRNA levels. (E) Culture media of adenovirus-infected AML12 cells was obtained for FGF21 secretion analysis. (F) Ad-GFP or Ad-ERRĪ³ was injected via the tail vein into male C57BL/6J mice. Serum from these mice was analyzed for FGF21 secretion. All data are the means Ā± standard errors of at least three independent experiments. ***p < 0.001 by Studentā€™s t-test.</p

    ACEA increases FGF21 protein levels.

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    <p>(Aā€“C) Whole cell lysates of ACEA-treated HepG2 cells and AML12 cells and livers of ACEA-treated intact mice were harvested for western blot analysis. (Dā€“E) AML12 cells and rat primary hepatocytes were treated with ACEA (10 Ī¼M) for the indicated time periods. Culture media were collected for FGF21 secretion analysis. (F) Mice were treated with ACEA (10 mg/kg) for the indicated number of days. Serum was obtained for FGF21 secretion analysis. All data are the means Ā± standard errors of at least three independent experiments. **p < 0.01; ***p < 0.001 by one-way ANOVA.</p
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