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3. TRAIL forciert Invasion von duktalen Pankreasadenokarzinomzellen in vitro und in vivo

Author

Trauzold, A., Schniewind, B., Siegmund, D., Emme, D., Klose, S., Röder, C., Wajant, H., Kalthoff, H., Bruch, H. P., editor, Büchler, M. W., editor, Buhr, H. J., editor, Hohenberger, W., editor, Klar, E., editor, Kremer, B., editor, Post, S., editor, Schilling, M., editor, Schumpelick, V., editor, Siewert, J. R., editor, Thiede, A., editor, Becker, H., editor, Bittner, R., editor, Függer, R., editor, Köckerling, F., editor, Saeger, H. D., editor, Zornig, C., editor, Hölscher, A., editor, Izbicki, J. R., editor, Junginger, T., editor, Senninger, N., editor, Allgayer, H., editor, Broll, R., editor, Bruns, C. J., editor, Fries, H., editor, Kalthoff, H., editor, Schackert, H. K., editor, Ertel, W., editor, Faist, E., editor, Holzheimer, R. G., editor, Holzmann, B., editor, Schade, U. F., editor, Vollmar, B., editor, Brückner, U. B., editor, Heidecke, C. D., editor, Menger, M. D., editor, Neugebauer, E., editor, Spiegel, H. U., editor, Biemer, E., editor, Germann, G., editor, Haas, N., editor, Machens, H. G., editor, Stark, G. B., editor, Steinau, H. U., editor, Haverich, A., editor, Heberer, M., editor, Rogiers, X., editor, Jauch, K. W., editor, Roth, H., editor, von Schweinitz, D., editor, Waag, K. L., editor, Altendorf-Hofmann, A., editor, Celik, I., editor, Lehnert, T., editor, Lorenz, W., editor, Ohmann, C., editor, Bechstein, W. O., editor, Broelsch, C., editor, Hopt, U., editor, Klempnauer, J., editor, Neuhaus, P., editor, Fändrich, F., editor, Markus, B., editor, Minor, T., editor, Wonigeit, K., editor, Dralle, H., editor, Goretzki, P. E., editor, Rothmund, M., editor, Bühren, V., editor, Josten, C., editor, Muhr, G., editor, Nast-Kolb, D., editor, Stürmer, K. M., editor, Trentz, O., editor, Brunkwall, J., editor, Sandmann, W., editor, Schmitz-Rixen, T., editor, Storck, M., editor, Branscheid, D., editor, Dienemann, H., editor, Hirner, A., editor, Passlick, B., editor, Toomes, H., editor, Beyersdorf, F., editor, Hetzer, R., editor, Schäfers, H. J., editor, Zerkowski, H. R., editor, Becker, H. D., editor, Saeger, H. -D., editor, Jauch, K. -W., editor, and Bauer, H., editor

Published
2006
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13. PS1001 HACE1, A NOVEL TUMOR SUPPRESSOR GENE WHICH REGULATE THE RESPONSE OF VENETOCLAX, GANT61 AND NECROPTOSIS ACTIVATORS BY CONTROLLING C-FLIP, GLI2 AND BCL2 GENES IN ACUTE MYELOID LEUKEMIA

Author

Garitano, A., primary, Teufel, E., additional, Kreckel, J., additional, Nadine, R., additional, Stühmer, T., additional, Via, M. Da, additional, Barrio, S., additional, Nerreter, S., additional, Haertle, L., additional, Vogt, C., additional, Düll, J., additional, Rasche, L., additional, Wajant, H., additional, Rosenwald, A., additional, Einsele, H., additional, and Kortüm, M., additional

Published
2019
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14. The anti-myeloma activity of bone morphogenetic protein 2 predominantly relies on the induction of growth arrest and is apoptosis-independent

Author

Lagler, C., El-Mesery, M., Kübler, A.C., Müller-Richter, U.D.A., Stühmer, T., Nickel, Joachim, Müller, T.D., Wajant, H., Seher, A., and Publica

Subjects
Cell Physiology, B Cells, animal structures, Immune Cells, Immunology, Cell Enumeration Techniques, Bone Morphogenetic Protein 2, Gene Expression, lcsh:Medicine, Apoptosis, Research and Analysis Methods, Plasma Cell Disorders, Necrotic Cell Death, Hematologic Cancers and Related Disorders, Mice, White Blood Cells, Animal Cells, Cell Line, Tumor, Medicine and Health Sciences, Genetics, Animals, Humans, Myelomas and Lymphoproliferative Diseases, Cell Cycle and Cell Division, ddc:610, Antibody-Producing Cells, lcsh:Science, Cell Proliferation, Blood Cells, Cell Death, lcsh:R, Biology and Life Sciences, Cancers and Neoplasms, Cell Cycle Checkpoints, Cell Biology, Hematology, Cell Metabolism, Myelomas, HEK293 Cells, Oncology, Cell Processes, embryonic structures, lcsh:Q, Cellular Types, Multiple Myeloma, Cell Division, Research Article
Abstract

Multiple myeloma (MM), a malignancy of the bone marrow, is characterized by a pathological increase in antibody-producing plasma cells and an increase in immunoglobulins (plasmacytosis). In recent years, bone morphogenetic proteins (BMPs) have been reported to be activators of apoptotic cell death in neoplastic B cells in MM. Here, we use bone morphogenetic protein 2 (BMP2) to show that the "apoptotic" effect of BMPs on human neoplastic B cells is dominated by anti-proliferative activities and cell cycle arrest and is apoptosis-independent. The anti-proliferative effect of BMP2 was analysed in the human cell lines KMS12-BM and L363 using WST-1 and a Coulter counter and was confirmed using CytoTox assays with established inhibitors of programmed cell death (zVAD-fmk and necrostatin-1). Furthermore, apoptotic activity was compared in both cell lines employing western blot analysis for caspase 3 and 8 in cells treated with BMP2 and FasL. Additionally, expression profiles o f marker genes of different cell death pathways were analysed in both cell lines after stimulation with BMP2 for 48h using an RT-PCR-based array. In our experiments we observed that there was rather no reduction in absolute cell number, but cells stopped proliferating following treatment with BMP2 instead. The time frame (48â72 h) after BMP2 treatment at which a reduction in cell number is detectable is too long to indicate a directly BMP2-triggered apoptosis. Moreover, in comparison to robust apoptosis induced by the approved apoptotic factor FasL, BMP2 only marginally induced cell death. Consistently, neither the known inhibitor of apoptotic cell death zVAD-fmk nor the necroptosis inhibitor necrostatin-1 was able to rescue myeloma cell growth in the presence of BMP2.

Published
2017

16. Inhibitor of apoptosis protein-1 regulates tumor necrosis factor-mediated destruction of intestinal epithelial cells

Author

Grabinger, T, Bode, K J, Demgenski, J, Seitz, C, Delgado, M E, Kostadinova, F, Reinhold, C, Etemadi, N, Wilhelm, S, Schweinlin, M, Hänggi, Kay, Knop, J, Hauck, C, Walles, H, Silke, J, Wajant, H, Nachbur, U, Wong, W Wei-Lynn, Brunner, T, Grabinger, T, Bode, K J, Demgenski, J, Seitz, C, Delgado, M E, Kostadinova, F, Reinhold, C, Etemadi, N, Wilhelm, S, Schweinlin, M, Hänggi, Kay, Knop, J, Hauck, C, Walles, H, Silke, J, Wajant, H, Nachbur, U, Wong, W Wei-Lynn, and Brunner, T

Abstract

Background and aims: Tumor necrosis factor (TNF) is a cytokine that promotes inflammation and contributes to pathogenesis of inflammatory bowel diseases. Unlike other cells and tissues, intestinal epithelial cells undergo rapid cell death upon exposure to TNF, by unclear mechanisms. We investigated the roles of inhibitor of apoptosis proteins (IAPs) in the regulation of TNF-induced cell death in the intestinal epithelium of mice and intestinal organoids. Methods: RNA from cell lines and tissues and analyzed by quantitative PCR, protein levels were analyzed by immunoblot assays. BIRC2 (also called cIAP1) was expressed upon induction from lentiviral vectors in young adult mouse colon (YAMC) cells. YAMC cells, the mouse colon carcinoma cell line MC38, the mouse macrophage cell line RAW 264.7, or mouse and human organoids were incubated with Smac-mimetic compound LCL161 or recombinant TNF-like weak inducer of apoptosis (TNFSF12) along with TNF, and cell death was quantified. C57BL/6 mice with disruption of Xiap, Birc2 (encodes cIAP1), Birc3 (encodes cIAP2), Tnfrsf1a, or Tnfrsf1b (Tnfrsf1a and b encode TNF receptors) were injected with TNF or saline (control); liver and intestinal tissues were collected and analyzed for apoptosis induction by cleaved caspase 3 immunohistochemistry. We also measured levels of TNF and alanine aminotransferase in serum from mice. Results: YAMC cells, and mouse and human intestinal organoids, died rapidly in response to TNF. YAMC and intestinal crypts expressed lower levels of XIAP, cIAP1, cIAP2, and cFLIP than liver tissue. Smac-mimetics reduced levels of cIAP1 and XIAP in MC38 and YAMC cells, and Smac-mimetics and TWEAK increased TNF-induced cell death in YAMC cells and organoids—most likely by sequestering and degrading cIAP1. Injection of TNF greatly increased levels of cell death in intestinal tissue of cIAP1-null mice, compared to wild- type C57BL/6 mice, cIAP2-null mice, or XIAP-null mice. Excessive TNF-induced cell death in the intes

Published
2017

25. Crystallization and preliminary x-ray diffraction analysis of hydroxynitrile lyase from cassava (Manihot esculenta)

Author

Lauble, Peter, Decanniere, Klaas, Wajant, H, Forster, S, Effenberger, F, and Structural Biology Brussels

Subjects
manihot esculenta, hydroxynitrile lyase
Abstract

Hydroxynitrile lyase from M. esculenta (cassava) was crystallized in two different crystal forms by the hanging-drop vapour-diffusion method. Crystals of form I were obtained from a mixture of polyethylene glycol 8000 and 2-methyl-2,4-pentanediol, and belong to the tetragonal space group P41212 or its enantiomorph P43212, with unit-cell parameters a = b = 105.9, c = 188.9 A and with two molecules in the asymmetric unit. These crystals diffract to 2.9 A with conventional X-ray sources and beyond 2.1 A resolution with synchrotron radiation. The crystals are relatively sensitive to radiation damage and conditions for flash-cooling the crystals have been established. A complete native data set has been collected up to 2.2 A resolution. Crystal form II has been obtained at pH 5.6 using lithium sulfate as a precipitant. The crystals apparently belong to the orthorhombic space group P21212, with unit-cell parameters a = 117.52, b = 127.09 and c = 78.08 A, have two molecules in the asymmetric unit and diffract to beyond 2.0 A resolution. A complete native data set has been collected to 2.2 A resolution.

Published
1999

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