182 research outputs found

    Summary of adult lifespan assays after RNAi-mediated gene inactivation.

    No full text
    <p>RNAi treatments, initiated at L1 stage, were continued throughout the assay time. Lifespan assays were performed at 20°C. Each experiment was individually grouped and statistical analyses of the data sets were carried out using the vector (L4440) control as the reference in each group (P value). In Set #3, the second set of statistical analyses was carried out for all the survivor data derived from the <i>asm-3(ok1744);rrf-3(pk1426)</i> strain, using the corresponding vector (L4440) control in this strain (marked as *) as the reference for this subgroup (*P values). Each set of the lifespan experiments was repeated at least two independent times and similar results were obtained. Data from representative sets of experiments are shown. Greater than 50 worms were counted for each RNAi-inducing condition in each experiment.</p

    Effects of <i>asm-3</i> on lifespan regulation in various mutants defective in the <i>daf-2</i> signaling.

    No full text
    <p>(A) Loss of <i>asm-3</i> did not further increase the lifespan of <i>daf-2(e1370)</i> mutants (P = 0.463). (B) <i>asm-3(ok1744)</i> mutation enhanced the mean lifespan of the longer-lived <i>age-1(mg305)</i> mutants by 67% (P<0.0001). (C) Silencing of <i>asm-3</i> in the <i>aap-1(m889)</i> mutant background further extended the mean lifespan by 21% compared to control (L4440) RNAi (P<0.0001). (D) <i>asm-3</i> mutation did not affect lifespan of <i>pdk-1(sa709)</i> mutant animals (P = 0.8404). (E) Effects of <i>asm-3(ok1744), akt-1(mg306),</i> and <i>asm-3(ok1744);akt-1(mg306)</i> mutations on lifespan regulation. <i>asm-3</i> mutation inhibited the lifespan extension of <i>akt-1(mg306)</i> mutant (P<0.0001), but <i>akt-1</i> mutation did not seem to affect the lifespan extension of <i>asm-3(ok1744)</i> mutant (P = 0.064). Mean lifespan, P values and other details for these experiments are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone-0045890-t001" target="_blank">Table 1</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone-0045890-t002" target="_blank">Table 2</a>.</p

    Loss of <i>asm</i> gene activities extends animal lifespan in a <i>daf-16</i> or <i>daf-18</i> dependent manner.

    No full text
    <p>For RNAi experiments, the vector alone (L4440) was used as a control. (A) <i>asm-3</i> RNAi extended animal lifespan with the mean lifespan 19% greater than that of the control in the <i>rrf-3(pk1426)</i> background (P<0.0001). (B) <i>asm-3(ok1744)</i> mutants had 14% longer lifespan than wild-type (N2) animals (P = 0.0141). (C) Knockdown of <i>asm-1</i>, <i>asm-2</i> or <i>asm-3</i> by RNAi each extended lifespan with the mean lifespan 12%, 10% or 19% greater than that of the vector control in the <i>rrf-3(pk1426)</i> background, respectively (P = 0.0068 for <i>asm-1</i> RNAi, P = 0.0258 for <i>asm-2</i> RNAi and P<0.0001 for <i>asm-3</i> RNAi). (D) Experiments were carried out in the <i>asm-3(+);rrf-3(pk1426)</i> or <i>asm-3(ok1744);rrf-3(pk1426)</i> background. <i>asm-3(ok1744</i>) mutation extended lifespan with the mean lifespan 15% greater than that of the control (P = 0.0018), and the lifespan of <i>asm-3(ok1744)</i> mutant was further enhanced by RNAi of <i>asm-1</i> or <i>asm-2</i> with the mean lifespan 30% or 28% greater than that of the control (P<0.0001 for <i>asm-1</i> RNAi or <i>asm-2</i> RNAi). Lifespan extension produced by <i>asm-3</i> mutation was inhibited by <i>daf-16</i> RNAi (P<0.0001). (E) <i>daf-16(mgDf47)</i> null mutation completely abolished lifespan extension phenotype of <i>asm-3</i> mutants. (F) Lifespan extension phenotype by <i>asm-1</i>, <i>asm-2</i> or <i>asm-3</i> RNAi shown in (C) was completely abolished by <i>daf-18(nr2037)</i> null mutation in the <i>rrf-3(pk1426);daf-18(nr2037)</i> background. Mean lifespan, P values and other details for these experiments are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone-0045890-t001" target="_blank">Table 1</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone-0045890-t002" target="_blank">Table 2</a>.</p

    Electronic Structure and Comparative Properties of LiNi<sub><i>x</i></sub>Mn<sub><i>y</i></sub>Co<sub><i>z</i></sub>O<sub>2</sub> Cathode Materials

    No full text
    We study the electronic structure and valence states in LiNi<sub><i>x</i></sub>Mn<sub><i>y</i></sub>Co<sub><i>z</i></sub>O<sub>2</sub> (NMC) materials and compare the resulting electronic, structural, mechanical, and thermal properties of a class of NMC compositions. The Jahn–Teller distortion in the transition metal (TM) octahedral complex allows us to determine the ionic states of the TM elements. The variation of Ni<sup>2+</sup>/Ni<sup>3+</sup> and Co<sup>2+</sup>/Co<sup>3+</sup> as the NMC composition changes alters the structural stability, electrical conductivity, lattice parameters, elastic modulus, and thermal stability. The theoretical predictions are in excellent agreement with the experimental results. Through intensive computational screening, we further show that long-range atomic ordering is absent in the NMC lattice due to the mixture of the ionic states and similar ionic radii of the TM elements. The first-principles modeling provides a theoretical foundation on a complete understanding of the physicochemical properties of NMC at the level of electronic structures

    Effects of drug treatment on animal lifespan.

    No full text
    <p>N2 (wild-type) or <i>daf-16(mgDf47)</i> mutant animals were assayed on plates either containing desipramine (30 µM), clomipramine (5 µM), or no drug control (0 µM). All the lifespan assays were carried out at 20°C. Mean lifespan, relative mean lifespan and statistical analyses (P values) for each assay were listed. Standard error of the mean, SEM, is included in parenthesis. Each set of the lifespan experiments was repeated at least three independent times and similar results were obtained. Data from representative sets of experiments are shown. Greater than 50 worms were counted for each condition in each experiment.</p

    Loss of <i>asm</i> induces the nuclear localization of DAF-16::GFP fusion protein and affects the DAF-16 protein levels.

    No full text
    <p>(A) and (B) DAF-16::GFP cellular distributions were examined by fluorescence microscopy and tail regions of animals were shown here. For images on the body and head regions of the animals, see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone.0045890.s005" target="_blank">Figure S5</a>. Animals were examined on adult day 1 (A) or day 4 (B). (A) In the <i>rrf-3(pk1426);daf-16::gfp</i> mutant background, vector control (L4440) RNAi showed that DAF-16::GFP diffusely localized in the cytoplasm, while <i>asm-3</i>, <i>asm-1</i> or <i>asm-2</i> RNAi each induced the nuclear localization of DAF-16::GFP. RNAi inactivation of <i>daf-2</i> and <i>age-1</i> (positive controls) and RNAi inactivation of <i>daf-16</i> and <i>daf-18</i> (negative controls) were carried out in parallel. (B) In the <i>asm-3(ok1744);rrf-3(pk1426);daf-16::gfp</i> mutant background, RNAi knockdown of <i>asm-1</i>, <i>asm-2</i> or <i>asm-1/asm-2</i> (double RNAi of <i>asm-1</i> and <i>asm-2</i>) further induced the nuclear localization of DAF-16::GFP protein. (C) and (D) western blot analysis of endogenous DAF-16 protein levels. (C) Increased DAF-16 protein levels were observed in the <i>asm-3(ok1744)</i> and <i>daf-2(e1370)</i> mutants as compared with that of wild-type control. Lysates were prepared from adult day 1 animals. (D) RNAi knockdown of <i>asm-3</i> or <i>daf-2</i> each elevated DAF-16 protein level as compared with that of vector control (L4440) RNAi. The specificity of the immunodetection was verified by the disappearance of DAF-16 protein in the <i>daf-16(mgDf47)</i> null mutants or in animals treated with <i>daf-16</i> RNAi. Lysates were prepared from RNAi-treated, adult day 2 animals. In (C) and (D), quantification of the relative abundance of DAF-16 proteins was shown with the DAF-16 protein levels being normalized against the beta-actin protein levels using the ImageJ software.</p

    qRT-PCR for DAF-16/FOXO transcriptional activity and <i>sod-3p::gfp</i> reporter.

    No full text
    <p>(A) By qRT-PCR, mRNA expression of endogenous <i>sod-3</i> gene was increased about 3-fold in the <i>asm-3(ok1744)</i> mutant animals as compared to the wild-type (N2) animals (T-test *P<0.05 for <i>asm-3(ok1744)</i> vs. wild-type; T-test **P<0.001 for <i>daf-2(e1370)</i> vs. wild-type). RNA samples were prepared from young adults (adult day 1). (B) By qRT-PCR, mRNA expression of endogenous <i>mtl-1</i> gene was modestly increased in the <i>asm-3(ok1744)</i> mutant animals as compared to the wild-type (N2) animals (T-test *P<0.05 for <i>asm-3(ok1744)</i> vs wild-type; T-test **P<0.001, <i>daf-2(e1370)</i> vs. wild-type). In (A) and (B), RNA samples, isolated from <i>daf-2(e1370)</i> or <i>daf-16(mgDf47)</i> mutant animals, were used as positive and negative controls, respectively. Additionally, an internal control of <i>act-1</i> was used for qRT-PCR and relative mRNA expression levels of <i>sod-3</i> or <i>mtl-1</i> were normalized to that of <i>act-1</i>. (C) Increased SOD-3::GFP expression was observed when multiple <i>asm</i> genes were inactivated in the <i>asm-3(ok1744);rrf-3(pk1426);sod-3p::gfp</i> mutant background compared to the vector control (L4440) RNAi. As negative controls, RNAi of <i>daf-16</i> or <i>daf-18</i> was used. As a positive control, the <i>daf-2</i> RNAi was used. Animals, treated with the indicated RNAi molecules, were examined on adult day 3. All fluorescence microscopy images were photographed using identical exposure times.</p

    Effects of <i>asm-3</i> on dauer formation regulation in various mutants defective in the<i>daf-2</i> signaling.

    No full text
    <p>(A) Loss of <i>asm-3</i> enhanced dauer formation of <i>daf-2(e1370)</i> mutants at the semi-permissive temperature 22.5°C. (B) <i>asm-3</i> mutation greatly enhanced dauer arrest phenotype of <i>age-1(mg305)</i> mutants at 22.5°C. (C) <i>asm-3</i> mutation did not affect dauer arrest induced by the <i>pdk-1(sa709)</i> mutation at 27°C. The mutant animals carrying <i>sa709</i> allele formed dauer at 27°C but not at 25°C. (D) <i>asm-3</i> mutation partially suppressed the dauer arrest phenotype of <i>akt-1(mg306)</i> mutants at 27°C. No dauers at 25°C were observed for the <i>akt-1(mg306)</i> mutant animals with or without the presence of the <i>asm-3(ok1744)</i> allele. (E) <i>asm-3</i> mutation had no effect on dauer arrest phenotype of <i>daf-7(e1372)</i> mutants at either 22.5°C or 25°C. The <i>asm-3(ok1744)</i> allele by itself did not induce dauer formation at either 22.5°C or 25°C. Error bars indicate standard deviation from triplicates. Details including total worm numbers used in the assay are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0045890#pone.0045890.s007" target="_blank">Table S1</a>.</p

    Nickel ions and hypoxia increased phosphorylation levels of c-Myc at T58 in A549 cells but not through GSK3β.

    No full text
    <p>(A) A549 cells were pretreated with 4 µM proteasome inhibitor MG-132 for 2 hr and then exposed to NiSO<sub>4</sub> (1 mM) or cultured in 1% O<sub>2</sub> (Hy) for another 24 hr. Immunoblotting of P-T58-Myc, total c-Myc, or α-tubulin was then performed as described in the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0008531#s2" target="_blank">Materials and Methods</a>. The densitometric data, presented between the blots, is expressed as density-ratio of P-T58-Myc band to corresponding total c-Myc band. (B–C) A549 cells were transfected with non-coding control siRNA or siRNA targeting human <i>GSK3β</i> for 48 hr, and then were treated with NiSO<sub>4</sub> (1.0 mM) or cultured under hypoxic conditions (1% O<sub>2</sub>) in the absence (B) or presence of 4 µM MG-132 (C) for another 24 hr. After treatment, cells were lysed and 50 µg of whole cell lysate was analyzed by Western blotting with the indicated antibodies. Similar data were obtained in at least two other independent experiments; one representative blot is shown here.</p

    Improvement of Water-, Sulfur Dioxide-, and Dust-Resistance in Selective Catalytic Reduction of NO<sub><i>x</i></sub> with NH<sub>3</sub> Using a Wire-Mesh Honeycomb Catalyst

    No full text
    A novel V<sub>2</sub>O<sub>5</sub>/WO<sub>3</sub>/TiO<sub>2</sub>/Al<sub>2</sub>O<sub>3</sub>/wire-mesh honeycomb (WMH) catalyst was prepared for selective catalytic reduction (SCR) of NO<sub><i>x</i></sub> with NH<sub>3</sub>. The resistances to H<sub>2</sub>O, SO<sub>2</sub>, and dust were investigated for the WMH catalyst, which were compared with those for ceramic honeycomb (CH) catalysts. The results showed that the WMH catalyst kept above 95% NO<sub><i>x</i></sub> conversion in the broad temperature window (250–425 °C) and provided nearly 92% NO<sub><i>x</i></sub> conversion during H<sub>2</sub>O and SO<sub>2</sub> durability test, which might be attributed to the unique three-dimensional structure. Furthermore, the WMH catalyst could provide nearly 90% NO<sub><i>x</i></sub> conversion during 40 h dust exposure experiment owing to the little dust deposition of 2.9 g/m<sup>2</sup>, whereas the amount of dust deposited on the CH catalyst with the same cell density reached 6.7 g/m<sup>2</sup>, which resulted in a decrease of the NO<sub><i>x</i></sub> conversion from 72% to 58%
    corecore