48 research outputs found

    Neutron imaging with fission and thermal neutrons at NECTAR at MLZ

    Get PDF
    The instrument NECTAR is located at beam port SR10 of the neutron source FRM II at the Heinz Maier-Leibnitz Zentrum (MLZ). With a pair of moveable uranium plates placed in front of the entrance window of the beam tube, a fission neutron spectrum with a mean energy of 1.9 MeV can be used for neutron imaging applications. Via remote control these plates can be removed and a thermal neutron spectrum (mean energy at 28 meV) gets available for experiments. While the fission neutron spectrum is regularly used, some upgrades of the instrument are necessary to make the thermal neutron spectrum routinely available for user experiments. This includes additional equipment like a new sample stage and a second detector system foreseen to extend the capabilities of NECTAR. The current state of the instrumentation and necessary changes for the future thermal beam option and its usage for standard user experiments will be presented. First measurements were carried out with a temporary flight tube installed and a compact detector (510 mm × 180 mm x 180 mm) for thermal neutrons with a spatial resolution in the range of 100 μm. The feasibility of the thermal beam option could already be verified at an L/D ratio of 240 and a thermal neutron flux of 7.92·106 cm−2 s−1. The thermal neutron beam option adds a pure thermal neutron spectrum – Maxwell spectrum originating from the moderator without alteration by a secondary source or converter – to the energy ranges available for neutron imaging at MLZ instruments. It also offers a unique possibility to combine two quite different neutron energy ranges at a single instrument including their respective advantages. The thermal neutron beam option is funded by BMBF in the frame of research project 05K16VK3

    Characterization of relativistic electron bunch duration and travelling wave structure phase velocity based on momentum spectra measurements on the ARES linac at DESY

    Full text link
    The ARES linac at DESY aims to generate and characterize ultrashort electron bunches (fs to sub-fs duration) with high momentum and arrival time stability for the purpose of applications related to accelerator R&D, e.g. development of advanced and compact diagnostics and accelerating structures, test of new accelerator components, medical applications studies, machine learning, etc. During its commissioning phase, the bunch duration characterization of the electron bunches generated at ARES has been performed with an RF-phasing technique relying on momentum spectra measurements, using only common accelerator elements (RF accelerating structures and magnetic spectrometers). The sensitivity of the method allowed highlighting different response times for Mo and Cs2Te cathodes. The measured electron bunch duration in a wide range of machine parameters shows excellent agreement overall with the simulation predictions, thus demonstrating a very good understanding of the ARES operation on the bunch duration aspect. The importance of a precise in-situ experimental determination of the phase velocity of the first travelling wave accelerating structure after the electron source, for which we propose a simple new beam-based method precise down to sub-permille variation respective to the speed of light in vacuum, is emphasized for this purpose. A minimum bunch duration of 20 fs rms, resolution-limited by the space charge forces, is reported. This is, to the best of our knowledge, around 4 times shorter than what has been previously experimentally demonstrated based on RF-phasing techniques with a single RF structure. The present study constitutes a strong basis for future time characterization down to the sub-fs level at ARES, using dedicated X-band transverse deflecting structures.Comment: 17 pages, 11 figures. To be submitted to Physical Review Accelerators and Beam

    Calcium sulfate precipitation pathways in natural and engineering environments

    Get PDF
    International audienceThe solution-mediated formation of calcium sulfate minerals, i.e. gypsum, anhydrite and bassanite, is a common process in both natural and engineered settings. It plays a key role in the global sulfur cycle and serves as an indicator of past environmental conditions on Earth and Mars. Products relying on the crystallization of these minerals have been employed since antiquity, and today they are an essential part of a wide array of industrial applications. Accordingly, the fundamental aspects of calcium sulfate mineralization have been the focus of intensive research during the past century. However, a recent flurry of studies addressing alternative, i.e. non-classical, nucleation and growth mechanisms has spurred a revisit of the precipitation pathway of the most common phase, gypsum. The newly obtained data sketch a far more complex picture of the mineralization process than previously assumed. This has important consequences for the interpretation of calcium sulfate deposits, both from a geochemical and industrial point of view. In order to shed light on this issue, we discuss in this review both recent and long-standing observations of abiotic formation routes of calcium sulfate minerals as a function of the physicochemical solution properties. By integrating both the classical and non-classical perspectives on crystallization we put forward a unified model for calcium sulfate crystallization. Using this model, we (re)-evaluate the phase stability and transformations taking place in the CaSO 4-H 2 O system. Next, we look into the formation of calcium sulfate minerals occurring in close association with the biosphere. Employing the abiotic case scenario as a benchmarking tool, the possible influence and/or control exerted by biological activity (and its byproducts) on the precipitation pathway is critically reviewed. Finally, we point out the central issues that need to be resolved if we wish to fully understand and control the formation of calcium sulfate solids in natural and engineered environments

    LABELLING DEVICE

    No full text

    Development of a compact combined plasma sensor for plasma surface engineering processes

    No full text
    A combined sensor for the investigation of plasma based surface engineering processes has been developed, which basically consists of a quartz crystal microbalance that is simultaneously used as a heat flux sensor and a planar Langmuir probe in one active element. The sensor can thus measure deposition flux, heat flux, and charged particle flux laterally resolved at the same time and position. The setup and working principle of the sensor are shown, and the suitability for process investigations is demonstrated exemplarily for a dc magnetron sputtering discharge for Ti thin film depositio

    Protein tyrosine phosphatase N2 regulates TNFα-induced signalling and cytokine secretion in human intestinal epithelial cells

    Full text link
    Objective The Crohn's disease (CD) susceptibility gene, protein tyrosine phosphatase N2 (PTPN2), regulates interferon γ (IFNγ)-induced signalling and epithelial barrier function in T(84) intestinal epithelial cells (IECs). The aim of this study was to investigate whether PTPN2 is also regulated by tumour necrosis factor α (TNFα) and if PTPN2 controls TNFα-induced signalling and effects in IECs. Methods T(84) IECs were used for all cell studies. Protein levels were assessed by western blotting, mRNA levels by reverse transcription-PCR (RT-PCR) and cytokine levels by ELISA. PTPN2 knock-down was induced by small interfering RNA (siRNA). Imaging was performed by immunohistochemistry or immunofluorescence. Results TNFα treatment elevated PTPN2 mRNA as well as nuclear and cytoplasmic protein levels and caused cytoplasmic accumulation of PTPN2. Biopsy specimens from patients with active CD showed strong immunohistochemical PTPN2 staining in the epithelium, whereas samples from patients with CD in remission featured PTPN2 levels similar to controls without inflammatory bowel disease (IBD). Though samples from patients with active ulcerative colitis (UC) revealed more PTPN2 protein than non-IBD patients and patients with UC in remission, their PTPN2 expression was lower than in active CD. Samples from patients with CD in remission and responding to anti-TNF treatment also showed PTPN2 levels that were similar to those in control patients. Pharmacological inhibition of nuclear factor-κB (NF-κB) by BMS-345541 prevented the TNFα-induced rise in PTPN2 protein, independent of apoptotic events. PTPN2 knock-down revealed that the phosphatase regulates TNFα-induced extracellular signal-regulated kinase 1/2 (ERK1/2) and p38 phosphorylation, without affecting c-Jun N-terminal kinase (JNK), inhibitor of κB (IκB) or NF-κB phosphorylation. Loss of PTPN2 potentiated TNFα-induced secretion of interleukin 6 (IL-6) and IL-8. In TNFα- and IFNγ-co-treated cells, loss of PTPN2 enhanced protein expression of inducible nitric oxide synthase (iNOS). Conclusions TNFα induces PTPN2 expression in IECs. Loss of PTPN2 promotes TNFα-induced mitogen-activated protein kinase signalling and the induction of inflammatory mediators. These data indicate that PTPN2 activity could play a crucial role in the establishment of chronic inflammatory conditions in the intestine, such as CD

    Sphingomyelin induces cathepsin D-mediated apoptosis in intestinal epithelial cells and increases inflammation in DSS colitis.

    Full text link
    t BACKGROUND: The sphingolipid sphingomyelin is a constituent in food derived from animals. Digestive breakdown of sphingomyelin results in ceramide, recently suggested to be involved in activation of cathepsin D as a novel mediator of apoptosis. Damage of the epithelial barrier was detected in patients with inflammatory bowel disease (IBD) due to increased rates of intestinal epithelial cell (IEC) apoptosis. METHODS: Acute colitis was induced in C57-BL/6 mice with 2.0% dextran sulfate sodium (DSS) over 7 days. Spontaneous colitis was developed in B6-IL10tm1Cgn (interleukin 10-negative (IL-10(-/-))) mice. Mice received 4 or 8 mg sphingomyelin/day by oral gavage. IECs were isolated ex vivo. Apoptosis was determined by propidium iodide (PI) and terminal deoxynucleotidyl transferase dUTP nick end labelling (TUNEL) staining. Execution of apoptosis was confirmed by analysis of active cathepsin D, caspase-3 and caspase-9 with western blot and immunohistochemistry (IHC). RESULTS: Following DSS-mediated colitis, fluorescence-activated cell sorting (FACS) analysis indicated increased apoptosis of IECs under dietary sphingomyelin. The mean sub-G(1) portion increased from 8.7±2.5% under a normal diet to 14.0±3.1% under dietary sphingomyelin. Cathepsin activity was significantly increased in isolated IECs after gavage of 4 mg of sphingomyelin per day. Western blot and IHC revealed execution of the apoptotic cascade via activated caspase-3 and caspase-9. Dietary sphingomyelin in the IL-10(-/-) model confirmed aggravation of mucosal inflammation. CONCLUSION: Apoptosis of IEC induced by dietary sphingomyelin is mediated via ceramide and cathepsin D activation. This shortens the physiological life cycle of IECs and impairs crucial functions of the intestinal mucosa: barrier, defence and nutrient absorption. The findings provide evidence that dietary sphingomyelin may increase intestinal inflammation

    Actin and an unconventional myosin motor, TgMyoF, control the organization and dynamics of the endomembrane network in Toxoplasma gondii.

    No full text
    Toxoplasma gondii is an obligate intracellular parasite that relies on three distinct secretory organelles, the micronemes, rhoptries, and dense granules, for parasite survival and disease pathogenesis. Secretory proteins destined for these organelles are synthesized in the endoplasmic reticulum (ER) and sequentially trafficked through a highly polarized endomembrane network that consists of the Golgi and multiple post-Golgi compartments. Currently, little is known about how the parasite cytoskeleton controls the positioning of the organelles in this pathway, or how vesicular cargo is trafficked between organelles. Here we show that F-actin and an unconventional myosin motor, TgMyoF, control the dynamics and organization of the organelles in the secretory pathway, specifically ER tubule movement, apical positioning of the Golgi and post-Golgi compartments, apical positioning of the rhoptries, and finally, the directed transport of Rab6-positive and Rop1-positive vesicles. Thus, this study identifies TgMyoF and actin as the key cytoskeletal components that organize the endomembrane system in T. gondii
    corecore