Search results for: W. Hennig

Authors: V. Thomas, O. Delaune, W. Hennig, S. Hoover

Abstract:

Measurement of radioactive isotopes of atmospheric xenon is used to detect, locate and identify any confined nuclear tests as part of the Comprehensive Nuclear Test-Ban Treaty (CTBT). In this context, the Alternative Energies and French Atomic Energy Commission (CEA) has developed a fixed device to continuously measure the concentration of these fission products, the SPALAX process. During its atmospheric transport, the radioactive xenon will undergo a significant dilution between the source point and the measurement station. Regarding the distance between fixed stations located all over the globe, the typical volume activities measured are near 1 mBq m⁻³. To avoid the constraints induced by atmospheric dilution, the development of a mobile detection system is in progress; this system will allow on-site measurements in order to confirm or infringe a suspicious measurement detected by a fixed station. Furthermore, this system will use beta/gamma coincidence measurement technique in order to drastically reduce environmental background (which masks such activities). The detector prototype consists of a gas cell surrounded by two large silicon wafers, coupled with two square NaI(Tl) detectors. The gas cell has a sample volume of 30 cm³ and the silicon wafers are 500 µm thick with an active surface area of 3600 mm². In order to minimize leakage current, each wafer has been segmented into four independent silicon pixels. This cell is sandwiched between two low background NaI(Tl) detectors (70x70x40 mm³ crystal). The expected Minimal Detectable Concentration (MDC) for each radio-xenon is in the order of 1-10 mBq m⁻³. Three 4-channels digital acquisition modules (Pixie-NET) are used to process all the signals. Time synchronization is ensured by a dedicated PTP-network, using the IEEE 1588 Precision Time Protocol. We would like to present this system from its simulation to the laboratory tests.

Keywords: beta/gamma coincidence technique, low level measurement, radioxenon, silicon pixels

Procedia PDF Downloads 106

Authors: Yuanyuan Zhang, Yujuan Zheng, Giuseppina Barutello, Sumako Kameishi, Kungchun Chiu, Katharina Hennig, Martial Balland, Federica Cavallo, Lars Holmgren

Abstract:

Angiogenesis describes that new blood vessels migrate from pre-existing ones to form 3D lumenized structure and remodeling. During directional migration toward the gradient of pro-angiogenic factors, the endothelial cells, especially the tip cells need filopodia to sense the environment and exert the pulling force. Of particular interest are the integrin proteins, which play an essential role in focal adhesion in the connection between migrating cells and extracellular matrix (ECM). Understanding how these biomechanical complexes orchestrate intrinsic and extrinsic forces is important for our understanding of the underlying mechanisms driving angiogenesis. We have previously identified Angiomotin (Amot), a member of Amot scaffold protein family, as a promoter for endothelial cell migration in vitro and zebrafish models. Hence, we established inducible endothelial-specific Amot knock-out mice to study normal retinal angiogenesis as well as tumor angiogenesis. We found that the migration ratio of the blood vessel network to the edge was significantly decreased in Amotec- retinas at postnatal day 6 (P6). While almost all the Amot defect tip cells lost migration advantages at P7. In consistence with the dramatic morphology defect of tip cells, there was a non-autonomous defect in astrocytes, as well as the disorganized fibronectin expression pattern correspondingly in migration front. Furthermore, the growth of transplanted LLC tumor was inhibited in Amot knockout mice due to fewer vasculature involved. By using MMTV-PyMT transgenic mouse model, there was a significantly longer period before tumors arised when Amot was specifically knocked out in blood vessels. In vitro evidence showed that Amot binded to beta-actin, Integrin beta 1 (ITGB1), Fibronectin, FAK, Vinculin, major focal adhesion molecules, and ITGB1 and stress fibers were distinctly induced by Amot transfection. Via traction force microscopy, the total energy (force indicater) was found significantly decreased in Amot knockdown cells. Taken together, we propose that Amot is a novel partner of the ITGB1/Fibronectin protein complex at focal adhesion and required for exerting force transition between endothelial cell and extracellular matrix.

Keywords: angiogenesis, angiomotin, endothelial cell migration, focal adhesion, integrin beta 1

Procedia PDF Downloads 204