Die Weltgeschichte ist das Weltgericht : Schillers Vers und die deutsche Geschichtsphilosophie des 19. Jahrhunderts

<p><b>A.</b><i>SerpinA3N</i> gene expression in the liver was significantly up-regulated in a HF diet at all times tested 3 days (<i>P</i><0.01), 1 week (<i>P</i><0.001) and 16 weeks (<i>P</i><0.01). <b>B.</b><i>Haptoglobin</i> gene expression was unchanged in HF fed mice liver after 3 days on diet but was increased after 1 week (<i>P</i><0.01) and 16 weeks (<i>P</i><0.01). <b>C.</b><i>SAA</i> gene expression was significantly higher on a HF diet after 3 days (<i>P</i><0.01) and 1 week (<i>P</i><0.001) but was not different after 16 weeks. <b>D.</b><i>ApoA-IV</i> gene expression was significantly down-regulated in the liver of HF fed mice after 3 days (<i>P</i><0.05) and 1 week (<i>P</i><0.01) on diet but was unchanged after 16 weeks on diet. <b>E.</b> In comparison <i>ApoA-IV</i> gene expression was significantly up-regulated in the ileum of HF fed mice after 3 days, 1 week and 16 weeks on diet (<i>P</i><0.05). <b>F.</b><i>SerpinA3N</i> gene expression in the liver was significantly down-regulated with time on a LF diet between 3 days and 16 weeks (<i>P</i><0.001). Units are fold expression changes between experimental groups relative to <i>B2M</i> and calculated from the ΔΔ<i>C</i>_t values (n = 6–8).</p

The effect of eicosapentaenoic and docosahexaenoic acid on protein synthesis and breakdown in murine C2C12 myotubes

Eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) have been found to stimulate protein synthesis with little information regarding their effects on protein breakdown. Furthermore whether there are distinct effects of EPA and DHA remains to be established. The aim of the current study was to determine the distinct effects of EPA and DHA on protein synthesis, protein breakdown and signalling pathways in C2C12 myotubes. Fully differentiated C2C12 cells were incubated for 24 h with 0.1% ethanol (control), 50 μM EPA or 50 μM DHA prior to experimentation. After serum (4 h) and amino acid (1 h) starvation cells were stimulated with 2 mM l-leucine and protein synthesis measured using 3H-labelled phenylalanine. Protein breakdown was measured using 3H-labelled phenylalanine and signalling pathways (Akt, mTOR, p70S6k, 4EBP1, rps6 and FOXO3a) via Western blots. Data revealed that after incubation with EPA protein synthesis was 25% greater (P &#60; 0.05) compared to control cells, with no effect of DHA. Protein breakdown was 22% (P &#60; 0.05) lower, compared to control cells, after incubation with EPA, with no effect of DHA. Analysis of signalling pathways revealed that both EPA and DHA incubation increased (P &#60; 0.05) p70s6k phosphorylation, EPA increased (P &#60; 0.05) FOXO3a phosphorylation, with no alteration in other signalling proteins. The current study has demonstrated distinct effects of EPA and DHA on protein metabolism with EPA showing a greater ability to result in skeletal muscle protein accretion

The effect of exercise induced cytokines on insulin stimulated glucose transport in C2C12 cells

Copyright © 2011 Elsevier Ltd. All rights reserved.Peer reviewedPostprin

Fish oil positively regulates anabolic signalling alongside an increase in whole-body gluconeogenesis in ageing skeletal muscle

Purpose: Fish oil, containing mainly long-chain n-3 polyunsaturated fatty acids (LCn-3PUFA), has been found to acutely stimulate protein synthesis and insulin-mediated glucose metabolism. However, the underlying mechanism and more prolonged effect of fish oil during ageing remain to be determined.&lt;p&gt;&lt;/p&gt; Methods: Fish oil (EPAX6000; 49.6 % eicosapentaenoic acid, 50.4 % docosahexaenoic acid) or control oil (60 % olive, 40 % soy) supplementation was delivered, via chocolate-derived sweets, to rats for 8 weeks. Throughout the study, food intake and body weight were recorded and body composition was investigated using EchoMRI. During the last 40 min of a 6 h infusion, with labelled dextrose ([U-13C]glucose) and amino acids ([1-13C]phenylalanine), blood samples were collected to assess glucose and phenylalanine kinetics. Soleus and longissimus dorsi muscles were extracted for protein and mRNA analyses.&lt;p&gt;&lt;/p&gt; Results: Fish oil had no effect on food intake or body composition. An increased whole-body glucose turnover, mainly accounted for via an increase in endogenous glucose production, was observed with fish oil feeding. No effects on whole-body phenylalanine turnover were observed. In longissimus dorsi, fish oil augmented the phosphorylation of phosphoinositide 3-kinase (PI3K)[Tyr458] (P = 0.04) and 70 kDa ribosomal protein S6 kinase (p70s6k)[Thr389] (P = 0.04). There were no differences in protein kinase B (Akt)[Ser473], mammalian target of rapamycin (mTOR)[Ser2448], protein phosphatase 2A (PP2A) 56 kDa regulatory B subunit γ (PP2A-B56-γ), forkhead box containing proteins O-subclass 3a (FOX03a)[Ser253] or inflammatory markers (Interleukin-6, Interleukin-1 β, tumour necrosis factor-α, and cyclooxygenase-2).&lt;p&gt;&lt;/p&gt; Conclusions: Our data suggest that the fish oil may stimulate endogenous glucose production and increase anabolic signalling in ageing rats

Representative 2D Coomassie stained gel of mouse plasma after 3 days on the HF diet. Bio-Rad, 11 cm, immobilized pH gradient (IPG) strips (pH 3–10) were used for the separation of plasma proteins in the first dimension.

<p>After the first dimension the IPG strip was applied to the top of a precast Criterion XT Bis-Tris 3–12% IPG+ 1 well gel cassette and 5 µl of All Blue Precision Protein Standards (Bio-Rad) were loaded in the reference well. The gels were fixed and stained with Coomassie Blue. Numbered spots indicate those with significantly different average normalised volumes (<i>P</i><0.05) (n = 5) in HF compared to LF mice. Proteins were identified by LC/MS/MS. Spots inside dotted lines have been identified as the same protein. See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0106159#pone-0106159-t001" target="_blank">Table 1</a> for protein identification.</p

Protein identification by LC/MS/MS of spots in 2DE gels of 3 day mice which were significantly different in averaged normalised volume in HF compared to LF fed mice (n = 5).

<p>Proteins identified as acute phase are marked*.</p><p>Protein identification by LC/MS/MS of spots in 2DE gels of 3 day mice which were significantly different in averaged normalised volume in HF compared to LF fed mice (n = 5).</p