12 research outputs found

    Association between Eating Habits and Sodium Intake among Chinese University Students

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    (1) Background: Insufficient evidence exists regarding the dietary habits that may contribute to high sodium intake among college students in China. This cross-sectional study aimed to investigate the dietary sodium intake of college students in Hunan and its association with their dietary habits. (2) Methods: In total, 585 university students from Hunan were recruited for this study. The sodium Food Frequency Questionnaire (sodium-FFQ) and dietary habits were assessed. (3) Results: Excluding cooking salt and high-sodium seasonings, the daily dietary sodium intake among college students in Changsha, Hunan Province, was 1183.74 (563.38, 2054.86) mg/day. A vast majority (89%) of college students reported eating outside of school at least once a week, and approximately one-third (34%) ordered takeaways at least once a week. After adjusting for confounding factors, the associations between the frequency of eating out and ordering takeaways with college students’ sodium intake remained significant. (4) Conclusions: The findings indicate that excessive dietary sodium intake among college students in Hunan is a growing concern. College students who frequently eat out and order takeaways tend to have a higher sodium intake. Future research should focus on identifying the main sources of dietary sodium and developing interventions that promote healthy dietary habits among college students

    Synergistic Effects of C/α-MoC and Ag for Efficient Oxygen Reduction Reaction

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    It remains challenging to prepare highly active and stable catalysts from earth-abundant elements for the oxygen reduction reaction (ORR). Herein we report a facile method to synthesize cost-effective heterogeneous C/α-MoC/Ag electrocatalysts. Rotating disc electrode (RDE) experiments revealed that the obtained C/α-MoC/Ag exhibited much superior catalytic performance for ORR than that of C/Ag, C/α-MoC, or even the conventional Pt/C. First-principles calculations indicated that the enhanced activity could be attributed to the efficient synergistic effects between Ag and α-MoC/C by which the energy barrier for O<sub>2</sub> dissociation has been substantially reduced. Furthermore, Li–air and Al–air cells were assembled to demonstrate the unprecedented electrochemical performance of C/α-MoC/Ag nanocomposites surpassing the Pt/C. Thus experimental results and theoretical calculations together showed that the heterogeneous C/α-MoC/Ag nanocomposites are a promising alternative to platinum for applications in industrial metal-air batteries

    HOXB7 is the substrate of PARP-1 and is poly(ADP ribosyl)ated by PARP-1.

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    <p>A. Different amounts of Flag tagged HOXB7 plasmids were transfected into SKBR3 cells, cells were harvested and permeabilized by 0.01% digitonin in PARP-1 activity reaction buffer. PARP-1 auto-modification was visualized by autoradiograph after the cell lysates were separated by SDS-PAGE (top panel). Immunoblot with anti-Flag, PARP-1 and β-actin antibodies were performed after autoradiography (bottom panels). B. GST and GST-HOXB7 fusion proteins were incubated with or without purified PARP-1 protein or <sup>32</sup>P NAD+. After 30 minutes incubation, free 32P NAD+ and unbound PARP-1 proteins were washed off with reaction buffer. Proteins on glutathione sepharose beads were then separated by SDS-PAGE and transferred to PVDF membrane and stained with Ponceau (left panel). The poly(ADP ribosyl)ated proteins were visualized by autoradiography (right panel). C. Vector control and Flag-tagged HOXB7 plasmids were transfected into SKBR3 cells. Cells were harvested and incubated with PARP-1 activity assay buffer including <sup>32</sup>P NAD+ or PARP-1 inhibitor (20 µM DPQ). Cell lysates were immunoprecipitated with anti-Flag antibody and separated by SDS-PAGE followed by autoradiography (top panel) and immunoblotting with anti-Flag antibodies (bottom panel).</p

    Defining regions of PARP-1 that interact with HOXB7.

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    <p>A. The molecular structure of PARP-1 and the deletion constructs used in the present study are shown in the panel. B, C. Full-length PARP-1 and different truncations of PARP-1 proteins as indicated were <i>in vitro</i> transcribed and translated (TNT) in presence of the <sup>35</sup>S-methionine and subjected to GST-HOXB7 or GST pull-down assay (left panels Fig. 2B and 2C). The right panels of <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040644#pone-0040644-g002" target="_blank">Figure 2B and 2C</a> show the input (20%) of the PARP-1 full-length and truncation proteins from TNT products. D. Plasmids coding Flag-tagged HOXB7 and Myc-tagged wild type PARP1 or first zinc-finger deleted PARP1 were cotransfected into MCF-7 cells. Cell lysates were immunoprecipitated with anti-Flag antibody. PARP-1 and HOXB7 protein were detected with anti-Myc or anti-Flag antibodies.</p

    PARP-1 interacts and modifies other HOX proteins.

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    <p>A. SKBR3 cells were transfected with empty vector, or Flag-tagged HOXA5, B6, B7, C6 and C8, respectively. Cell lysates were immunoprecipitated with anti-Flag antibody, and western blotted with anti-PARP-1 (top panel) and Flag antibodies (bottom panel), respectively. HOXC6 transfected SKBR3 cell lysate was used as loading control. B. Vector control and Flag-tagged HOX plasmids were transfected into SKBR3 cells as indicated. Cells were harvested and incubated with PARP activity reaction buffer containing 0.01% digitonin and <sup>32</sup>P NAD+. Cells were then lysed after incubation and immunoprecipitated with anti-Flag antibody. The precipitated complexes were then separated by SDS-PAGE, transferred to the nitrocellulose membrane that was used for autoradiography (top panel) and western blot (bottom panel) using anti-PARP-1 and anti-Flag antibodies. C. Multiple sequence alignment of the C-terminal peptides of HOXA5, HOXA7, HOXB6, HOXB7, HOXC6 and HOXC8 show extent of homology. D. The ONP assay was performed with the SKBR3 cells transfected with Flag HOXA7 with or without PARP-1, and one set of the HOXA7 and PARP-1 co-transfected cells was treated with DPQ 6 hours post transfection. Cell lysates were used for ONP (top panel) and western blots (bottom panel). E. ONP assays were performed with SKBR3 cells transfected with Flag HOXA1, Flag HOXA5, Flag HOXC6 or Flag HOXB6 plasmids with or without PARP-1 plasmids, and one set of each of the HOX and PARP-1 co-transfected cells was treated with DPQ 6 hours post transfection. Cell lysates were used for ONP assays (top panel) and western blots (bottom panel). F. ONP assay was performed with the SKBR3 cells transfected with Flag-tagged HOXB6 or the Lys to Glu mutant, HOXB6K221E, with or without PARP-1. Cell lysates were used for ONP assays (top panel) and western blots (bottom panel).</p
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