15 research outputs found

    Nyugdíj és gyermekvállalás 2.0 Nyugdíjreform elképzelések Konferencia kötet

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    A kötet a 2019. június 13-án, a Corvinus Egyetemen tartott hasonló című konferenciaelőadásait, illetve az azok alapján készült tanulmányokat tartalmazza. A címben található „2.0" arra utal, hogy 2012-ben, hasonló címmel, ugyancsak a Corvinus Egyetemen már tartottunk egy konferenciát, így az érdeklődő olvasó összehasonlíthatja, hogy a téma kutatása mennyit fejlődött 6 éve alatt. Az itt található nyugdíjreform elképzelések között sok a hasonlóság, de jelentősek a különbségek is, így azok alapos tanulmányozása és összehasonlítása javasolt, hiszen a szerzők sok helyen - expliciten vagy impliciten - egymással is vitatkoznak. Fontosnak tartottuk bemutatni a témával kapcsolatos szkeptikus hangokat is, bár a szerkesztők maguk úgy vélik, hogy a gyermeknevelést és a nyugdíjrendszert össze kell kapcsolni - ahogy az itt szereplő szerzők döntő hányada javasolja

    Investigation of protein and epitope characteristics of oats and its implications for celiac disease

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    The use of pure oats (oats cultivated with special care to avoid gluten contamination from wheat, rye, and barley) in the gluten-free diet (GFD) represents important nutritional benefits for the celiac consumer. However, emerging evidence suggests that some oat cultivars may contain wheat gliadin analog polypeptides. Consequently, it is necessary to screen oats in terms of protein and epitope composition to be able to select safe varieties for gluten-free applications. The overall aim of our study is to investigate the variability of oat protein composition directly related to health-related and techno-functional properties. Elements of an oat sample population representing 162 cultivated varieties from 20 countries and the protein composition of resulting samples have been characterized. Size distribution of the total protein extracts has been analyzed by size exclusion-high performance liquid chromatography (SE-HPLC) while the 70% ethanol-extracted proteins were analyzed by RP-HPLC. Protein extracts separated into three main groups of fractions on the SE-HPLC column: polymeric proteins, avenins (both containing three subgroups based on their size), and soluble proteins, representing respectively 68.79–86.60, 8.86–27.72, and 2.89–11.85% of the total protein content. The ratio of polymeric to monomeric proteins varied between 1.37 and 3.73. Seventy-six reversed phase-HPLC-separated peaks have been differentiated from the ethanol extractable proteins of the entire population. Their distribution among the cultivars varied significantly, 6–23 peaks per cultivar. The number of appearances of peaks also showed large variation: one peak has been found in 107 samples, while 15 peaks have been identified, which appeared in less than five cultivars. An estimation method for ranking the avenin-epitope content of the samples has been developed by using MS spectrometric data of collected RP-HPLC peaks and bioinformatics methods. Using ELISA methodology with the R5 antibody, a high number of the investigated samples were found to be contaminated with wheat, barley, or rye

    Altered functional protein networks in the prefrontal cortex and amygdala of victims of suicide.

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    Probing molecular brain mechanisms related to increased suicide risk is an important issue in biological psychiatry research. Gene expression studies on post mortem brains indicate extensive changes prior to a successful suicide attempt; however, proteomic studies are scarce. Thus, we performed a DIGE proteomic analysis of post mortem tissue samples from the prefrontal cortex and amygdala of suicide victims to identify protein changes and biomarker candidates of suicide. Among our matched spots we found 46 and 16 significant differences in the prefrontal cortex and amygdala, respectively; by using the industry standard t test and 1.3 fold change as cut off for significance. Because of the risk of false discoveries (FDR) in these data, we also made FDR adjustment by calculating the q-values for all the t tests performed and by using 0.06 and 0.4 as alpha thresholds we reduced the number of significant spots to 27 and 9 respectively. From these we identified 59 proteins in the cortex and 11 proteins in the amygdala. These proteins are related to biological functions and structures such as metabolism, the redox system, the cytoskeleton, synaptic function, and proteolysis. Thirteen of these proteins (CBR1, DPYSL2, EFHD2, FKBP4, GFAP, GLUL, HSPA8, NEFL, NEFM, PGAM1, PRDX6, SELENBP1 and VIM,) have already been suggested to be biomarkers of psychiatric disorders at protein or genome level. We also pointed out 9 proteins that changed in both the amygdala and the cortex, and from these, GFAP, INA, NEFL, NEFM and TUBA1 are interacting cytoskeletal proteins that have a functional connection to glutamate, GABA, and serotonin receptors. Moreover, ACTB, CTSD and GFAP displayed opposite changes in the two examined brain structures that might be a suitable characteristic for brain imaging studies. The opposite changes of ACTB, CTSD and GFAP in the two brain structures were validated by western blot analysis

    Altered Functional Protein Networks in the Prefrontal Cortex and Amygdala of Victims of Suicide

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    <div><p>Probing molecular brain mechanisms related to increased suicide risk is an important issue in biological psychiatry research. Gene expression studies on <em>post mortem</em> brains indicate extensive changes prior to a successful suicide attempt; however, proteomic studies are scarce. Thus, we performed a DIGE proteomic analysis of <em>post mortem</em> tissue samples from the prefrontal cortex and amygdala of suicide victims to identify protein changes and biomarker candidates of suicide. Among our matched spots we found 46 and 16 significant differences in the prefrontal cortex and amygdala, respectively; by using the industry standard <em>t</em> test and 1.3 fold change as cut off for significance. Because of the risk of false discoveries (FDR) in these data, we also made FDR adjustment by calculating the <em>q</em>-values for all the <em>t</em> tests performed and by using 0.06 and 0.4 as alpha thresholds we reduced the number of significant spots to 27 and 9 respectively. From these we identified 59 proteins in the cortex and 11 proteins in the amygdala. These proteins are related to biological functions and structures such as metabolism, the redox system, the cytoskeleton, synaptic function, and proteolysis. Thirteen of these proteins (CBR1, DPYSL2, EFHD2, FKBP4, GFAP, GLUL, HSPA8, NEFL, NEFM, PGAM1, PRDX6, SELENBP1 and VIM,) have already been suggested to be biomarkers of psychiatric disorders at protein or genome level. We also pointed out 9 proteins that changed in both the amygdala and the cortex, and from these, GFAP, INA, NEFL, NEFM and TUBA1 are interacting cytoskeletal proteins that have a functional connection to glutamate, GABA, and serotonin receptors. Moreover, ACTB, CTSD and GFAP displayed opposite changes in the two examined brain structures that might be a suitable characteristic for brain imaging studies. The opposite changes of ACTB, CTSD and GFAP in the two brain structures were validated by western blot analysis.</p> </div

    Functionally clustered changes in proteins of the amygdala.

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    *<p>proteins involved in schizophrenia; +: proteins involved in depression; S: proteins involved in suicide.</p>*<p>proteins involved in schizophrenia; +: proteins involved in depression; S: proteins involved in suicide. Bold-italic gene names highlighting those proteins that were found in those differently expressed protein spots that proved significant with both statistical tests. ↑ or ↓: the direction of the spot intensity change of a given spot compared to control.</p

    Representative gel image.

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    <p>The first dimension was carried out in pH 3–10 NL IPG strip and the second dimension was 24×20 cm 10% SDS PAGE. Part A shows the overlaid image, part B shows the standardized log abundance of a representative spot (2406, prefrontal cortex) on the different gels, part C shows 3D views of the individual spots (C1–C6: control brains; S1–S6: suicide brains).</p
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