20 research outputs found

    World Congress Integrative Medicine & Health 2017: Part one

    Get PDF

    Konflikten mellan att reducera miljö- och säkerhetsrisker under vintersäsongen på en flygplats – en studie på Oslos huvudflygplats Gardermoen

    No full text
    There are different rules and laws which companies and industries in a society must follow. Steps to comply with one law or rule may reduce the ability to comply with another. A sector where such a conflict could occur is in aviation, where the reduction of environmental and safety risks may be in conflict with each other. To meet the security requirements of an airport during the winter season when ice and snow can cause poor friction on runways, use of de-icing chemicals may be necessary. Using these de-icing chemicals means continued good conditions on the runway, despite the winter weather. This means that the airport's desire to reduce the security risk can be maintained. De-icing chemicals may be an environmental hazard to the surroundings of the runways, which is contrary to the desire to reduce environmental risk as far as possible. To reduce environmental and safety risks can thus cause a conflict for an airport in winter operation. This master thesis investigates the situation at Oslo airport Gardermoen (OSL). The purpose is to highlight the conflict between the reduction of environmental and safety risks at OSL by answering the question, "Is there currently a conflict between reducing environmental and safety risks at OSL?" To answer this question, five interviews and a calculation example are performed. The results of the interviews and calculation example both suggest that the conflict that has been highlighted here is strictly theoretical. It is according to the authors of this report not possible to identify a conflict between reducing the environmental and safety risks during the winter season at OSL

    RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability.

    Get PDF
    BACKGROUND: Red blood cells (RBC) possess a nitric oxide synthase (RBC-NOS) whose activation depends on the PI3-kinase/Akt kinase pathway. RBC-NOS-produced NO exhibits important biological functions like maintaining RBC deformability. Until now, the cellular target structure for NO, to exert its influence on RBC deformability, remains unknown. In the present study we analyzed the modification of RBC-NOS activity by pharmacological treatments, the resulting influence on RBC deformability and provide first evidence for possible target proteins of RBC-NOS-produced NO in the RBC cytoskeletal scaffold. METHODS/FINDINGS: Blood from fifteen male subjects was incubated with the NOS substrate L-arginine to directly stimulate enzyme activity. Direct inhibition of enzyme activity was induced by L-N5-(1-Iminoethyl)-ornithin (L-NIO). Indirect stimulation and inhibition of RBC-NOS were achieved by applying insulin and wortmannin, respectively, substances known to affect PI3-kinase/Akt kinase pathway. The NO donor sodium nitroprusside (SNP) and the NO scavenger 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (cPTIO) were additionally applied as NO positive and negative controls, respectively. Immunohistochemical staining was used to determine phosphorylation and thus activation of RBC-NOS. As a marker for NO synthesis nitrite was measured in plasma and RBCs using chemiluminescence detection. S-nitrosylation of erythrocyte proteins was determined by biotin switch assay and modified proteins were identified using LC-MS. RBC deformability was determined by ektacytometry. The data reveal that activated RBC-NOS leads to increased NO production, S-nitrosylation of RBC proteins and RBC deformability, whereas RBC-NOS inhibition resulted in contrary effects. CONCLUSION/SIGNIFICANCE: This study first-time provides strong evidence that RBC-NOS-produced NO modifies RBC deformability through direct S-nitrosylation of cytoskeleton proteins, most likely α- and β-spectrins. Our data, therefore, gain novel insights into biological functions of RBC-NOS by connecting impaired RBC deformability abilities to specific posttranslational modifications of RBC proteins. By identifying likely NO-target proteins in RBC, our results will stimulate new therapeutic approaches for patients with microvascular disorders

    Challenges and opportunities for Zimbabwean exports arising from environmental requirements in Europe

    No full text
    Umweltfragen spielen aus zwei Gruenden eine immer bedeutendere Rolle im internationalen Geschaeft: (1) In den Industrielaendern existiert eine staendig wachsende Anzahl von umweltfreundlichen bzw. -vertraeglichen Produktstandards, die sowohl von den heimischen Produzenten als auch von Importeuren zu beruecksichtigen sind; (2) Die Nachfrage der Verbraucher nach umweltvertraeglichen und gesunden Produkten steigt staendig. Die Studie untersucht diesen Trend und die daraus resultierenden Probleme am Beispiel Simbabwes und seinen Export von Textilien, Lederwaren, Holz und Nahrungsmitteln nach Europa. Die Ergebnisse der Studie zeigen, dass die Unternehmen dieser Branchen die Anforderungen und Vorstellungen der Europaeer noch weitgehend als koloniale Zumutungen erleben und sich ein Bewusstsein nur langsam entwickelt, dass hier ertragreiche Alternativen und Entwicklungsmoeglichkeiten liegen. (pre)German title: Herausforderungen und Gelegenheiten fuer den Export Zimbabwes durch Umweltanforderungen in EuropaAvailable from UuStB Koeln(38)-980106448 / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekSIGLEDEGerman

    Maximum deformability (EI max) after RBC incubation with RBC-NOS stimulants, inhibitors and NO controls and correlation of EI max with S-nitrosylation of α- and β-spectrin.

    No full text
    <p>(A) Bars show that EI max significantly increased after 60 min incubation with L-arginine (P<0.05), insulin (P<0.05) and SNP (P<0.05). Application of L-NIO (P<0.01), wortmannin (P<0.01) and cPTIO (P<0.01) significantly decreased EI max. (B) Correlation between EI max and S-nitrosylation of α-(black square) and β-(gray circle) spectrin. Data in (A) are presented as mean±S.E.M of n = 15.</p

    MS data evaluation using Proteome Discoverer 1.0.

    No full text
    <p>Excised and processed proteins were identified. The first four matches with their respective value concerning sequence coverage, number of peptides identified and score are presented.</p

    S-nitrosylation of RBC proteins after modification of RBC-NOS-dependent NO production.

    No full text
    <p>(A) Representative western blot bands after 60 min incubation of RBCs with RBC-NOS stimulants, inhibitors and NO controls are demonstrated. The image shows two distinctive bands with varying intensity depending on RBC-NOS modulation. LC-MS/MS analysis identified 240 kDa band as possible α- spectrin and 220 kDa band as possible β-spectrin. (B) Calculation of relative intensity in relation to the control sample revealed that S-nitrosylation of both, α- and β-spectrin, significantly increased upon L-arginine, insulin and SNP incubation and significantly decreased upon L-NIO, wortmannin and cPTIO incubation, respectively. Data in (B) are presented as mean±S.E.M., n = 6.</p

    Changes in nitrite concentration after modification of RBC-NOS activity, and plasma ADMA content after L-arginine application.

    No full text
    <p>Nitrite was measured as representative of NO synthesis after 60 min incubation of RBCs with RBC-NOS stimulants, inhibitors and NO controls. (A) RBC nitrite level significantly increased after L-arginine (<i>P</i><0.01), insulin (<i>P</i><0.01) and SNP (<i>P</i><0.01) application, while L-NIO (<i>P</i><0.001), wortmannin (<i>P</i><0.01) and cPTIO (<i>P</i><0.05) significantly decreased RBC nitrite content compared to control samples. (B) Plasma ADMA concentration was additionally measured after L-arginine incubation to present an explanation for the L-arginine paradox. Bars show that ADMA concentration in the plasma fraction significantly increased upon substrate addition (<i>P</i><0.001). (C) Plasma nitrite concentration was not altered by the applied substances, except SNP. Data in (A–C) are presented as mean±S.E.M., n = 15.</p
    corecore