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3. Aktualisierte S3-Leitlinie Colitis ulcerosa (Version 6.2).

Author

Kucharzik, T., Dignass, A., Atreya, R., Bokemeyer, B., Esters, P., Herrlinger, K., Kannengiesser, K., Kienle, P., Langhorst, J., Lügering, A., Schreiber, S., Stallmach, A., Stein, J., Sturm, A., Teich, N., Siegmund, B., Andus, T., Autschbach, F., Bachmann, O., and Baretton, G.

Published
2024
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4. Update des Addendums zu den S3-Leitlinien Morbus Crohn und Colitis ulcerosa: Betreuung von Patienten mit chronisch-entzündlichen Darmerkrankungen in Bezug auf COVID-19 (Version 2.0).

Author

Schmidt, Carsten, Stallmach, Andreas, Sturm, Andreas, Bachmann, Oliver, Helwig, Ulf, Koletzko, Sibylle, Lynen, Petra, Schnoy, Elisabeth, Dignass, Axel, Kucharzik, Torsten, Blumenstein, Irina, Aden, K., Andus, T., Anlauf, M., Atreya, R., Autschbach, F., Baretton, G. B., Baumgart, D. C., Bettenworth, D., and Bläker, M.

Published
2024
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9. Functional characterisation of decoy receptor 3 in Crohn's disease

Author

Funke, B., Autschbach, F., Kim, S., Lasitschka, F., Strauch, U., Rogler, G., Gdynia, G., Li, L., Gretz, N., Macher-Goeppinger, S., Sido, B., Schirmacher, P., Meuer, S.C., and Roth, W.

Subjects
Crohn's disease -- Development and progression, Crohn's disease -- Research, Tumor necrosis factor -- Physiological aspects, Tumor necrosis factor -- Research, Health
Published
2009

13. Erhöhung der Substanz P Expression in nicht entzündeten Darmabschnitten bei M. Crohn

Author

Shi, X., Michalski, C., Francesco Di Mola, F., Di Sebastiano, P., Giese, T., Autschbach, F., Friess, 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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14. Updated S3-Guideline Colitis ulcerosa. German Society for Digestive and Metabolic Diseases (DGVS) : AWMF Registry 021/009

Author

Kucharzik, Torsten, Dignass, Axel U., Atreya, Raja, Bokemeyer, Bernd, Esters, Philip, Herrlinger, Klaus, Kannengießer, Klaus, Kienle, Peter, Langhorst, Jost, Lügering, Andreas, Schreiber, Stefan, Stallmach, Andreas, Stein, Jürgen, Sturm, Andreas, Teich, Niels, Siegmund, Britta, Andus, T., Autschbach, F., Bachmann, O., Baretton, G., Baumgart, D.C., Bettenworth, D., Bläker, M., Buderus, S., Büning, J., Ehehalt, R., Fellermann, K., Fichtner-Feigl, S., Götz, M., Gross, C., Hartmann, F., Hartmann, P., In Der Smitten, S., Häuser, W., Helwig, U., Kaltz, B., Kanbach, I., Keller, K.M., Klaus, J., Koletzko, S., Kroesen, A., Kruis, W., Kühbacher, T., Leifeld, L., Maaser, C., Matthes, H., Moog, G., Ockenga, J., Pace, A., Reinshagen, M., Rijcken, E., Rogler, G., Stange, E., Veltkamp, C., and Zemke, J.

Subjects
Medizin, Gastroenterology
Abstract

ZusammenfassungDie neue S3-Leitlinie Colitis stellt aktuelle und evidenzbasierte Empfehlungen zur Behandlung der Colitis ulcerosa zur Verfügung. Sie ersetzt damit die Vorläuferversion von 2011. Neben den neuesten Erkenntnissen zu Diagnostik und Therapie werden insbesondere infektiologische Probleme, chirurgische und Ernährungsmaßnahmen aufgegriffen. Unter der Federführung der DGVS wurde die Leitlinie gemeinsam mit 10 weiteren Fachgesellschaften und Patientenvertretern erarbeitet mit dem Ziel, eine optimale interdisziplinäre Versorgung der Patienten zu gewährleisten.

Published
2018
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26. Blockade of interleukin 6 trans signaling suppresses T-cell resistance against apoptosis in chronic intestinal inflammation: Evidence in Crohn disease and experimental colitis in vivo

Author

Atreya, R., Mudter, J., Finotto, S., Mullberg, J., Jostock, T., Wirtz, S., Schutz, M., Bartsch, B., Holtmann, M., Becker, C., Strand, D., Czaja, J., Schlaak, J. F., Lehr, H.A., Autschbach, F., Schurmann, G., Nishimoto, N., Yoshizaki, K., Ito, H., Kishimoto, T., Galle, P.R., Rose-John, S., and Neurath, M.F.

Abstract

The pro-inflammatory cytokine interleukin (IL)-6 (refs. 1-5) can bind to cells lacking the IL-6 receptor (IL-6R) when it forms a complex with the soluble IL-6R (sIL-6R) (trans signaling). Here, we have assessed the contribution of this system to the increased resistance of mucosal T cells against apoptosis in Crohn disease (CD), a chronic inflammatory disease of the gastrointestinal tract. A neutralizing antibody against IL-6R suppressed established experimental colitis in various animal models of CD mediated by type 1 T-helper cells, by inducing apoptosis of lamina propria T cells. Similarly, specific neutralization of sIL-6R in vivo by a newly designed gp130-Fc fusion protein caused suppression of colitis activity and induction of apoptosis, indicating that sIL-6R prevents mucosal T-cell apoptosis. In patients with CD, mucosal T cells showed strong evidence for IL-6 trans signaling, with activation of signal transducer and activator of transcription 3, bcl-2 and bcl-xl. Blockade of IL-6 trans signaling caused T-cell apoptosis, indicating that the IL-6-sIL-6R system mediates the resistance of T cells to apoptosis in CD. These data indicate that a pathway of T-cell activation driven by IL-6-sIL-6R contributes to the perpetuation of chronic intestinal inflammation. Specific targeting of this pathway may be a promising new approach for the treatment of CD., Author(s): R. Atreya [1, 6]; J. Mudter [1, 6]; S. Finotto [1]; J. Mullberg [1]; T. Jostock [1]; S. Wirtz [1]; M. Schutz [1]; B. Bartsch [1]; M. Holtmann [1]; [...]

Published
2000
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48. Blockade of interleukin 6 trans signaling suppresses T-cell resistance against apoptosis in chronic intestinal inflammation : Evidence in Crohn disease and experimental colitis in vivo (vol 6, pg 583, 2000)

Author

Atreya, R., Mudter, J., Finotto, S., Mullberg, J., Jostock, T., Wirtz, S., Schutz, M., Bartsch, B., Holtmann, Marianne, Becker, C., Strand, D., Czaja, J., Schlaak, Jörg Friedrich, Lehr, H. A., Autschbach, F., Schurmann, G., Nishimoto, N., Yoshizaki, K., Ito, H., Kishimoto, T., Galle, P. R., Rose-John, S., and Neurath, M. F.

Subjects
Medizin
Published
2010

49. Functional characterisation of decoy receptor 3 in Crohn's disease

Author

Funke, B, Autschbach, F, Kim, S, Lasitschka, F, Strauch, U, Rogler, G, Gdynia, G, Li, L, Gretz, N, Macher-Goeppinger, S, Sido, B, Schirmacher, P, Meuer, S C, Roth, W, University of Zurich, and Roth, W

Subjects
10219 Clinic for Gastroenterology and Hepatology, 610 Medicine & health, 2715 Gastroenterology
Published
2009
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50. DMBT1 functions as pattern-recognition molecule for poly-sulfated and poly-phosphorylated ligands

Author

End, C., Bikker, F.J., Renner, M., Bergmann, G., Lyer, S., Blaich, S., Hudler, M., Helmke, B., Gassler, N., Autschbach, F., Ligtenberg, A.J.M., Benner, A., Holmskov, U., Schirmacher, P., Nieuw Amerongen, A.V., Rosenstiel, P., Sina, C., Franke, A., Hafner, M., Kioschis, P., Schreiber, S., Poustka, A., Mollenhauer, J., and Orale Biochemie (OUD, ACTA)

Subjects
Salmonella typhimurium, Unclassified drug, Mouse, Cell aggregation, Cytotoxicity, Enzyme linked immunosorbent assay, Protein function, Heparan sulfate, Cell surface receptor, Antimicrobial activity, Carrageenan, Ligands, Inflammatory bowel disease, Epithelium cell, Drug antagonism, Bacterium, Mucosal immunity, Sulfation, Intestinal Mucosa, Protein motif, Innate immunity, Dextran Sulfate, Crohn disease, Scavenger receptor cysteine-rich, Colitis, Intestine, DNA-Binding Proteins, Intestines, Health, Host pathogen interaction, Deleted in malignant brain tumors 1, Protein determination, Human, Antiinflammatory activity, Immunology, Lipopolysaccharide, Ligand, Phosphate, Receptors, Cell Surface, Microbiology, Cell Line, Phosphates, Protein phosphorylation, Intestine epithelium cell, Pattern recognition, Dose response, Escherichia coli, Experimental mouse, Genetics, Protein binding, Humans, Animal model, Animal experiment, Salmonella minnesota, Binding competition, Bacteria, Tumor Suppressor Proteins, Calcium-Binding Proteins, In vitro study, Epithelial Cells, Nonhuman, Lipoteichoic acid, Metabolism, Human cell, DMBT1 protein, human, Streptococcus gordonii, Protein expression, Glycoprotein, Controlled study
Abstract

Deleted in malignant brain tumors 1 (DMBT1) is a secreted glycoprotein displaying a broad bacterial-binding spectrum. Recent functional and genetic studies linked DMBT1 to the suppression of LPS-induced TLR4-mediated NF-kappaB activation and to the pathogenesis of Crohn's disease. Here, we aimed at unraveling the molecular basis of its function in mucosal protection and of its broad pathogen-binding specificity. We report that DMBT1 directly interacts with dextran sulfate sodium (DSS) and carrageenan, a structurally similar sulfated polysaccharide, which is used as a texturizer and thickener in human dietary products. However, binding of DMBT1 does not reduce the cytotoxic effects of these agents to intestinal epithelial cells in vitro. DSS and carrageenan compete for DMBT1-mediated bacterial aggregation via interaction with its bacterial-recognition motif. Competition and ELISA studies identify poly-sulfated and poly-phosphorylated structures as ligands for this recognition motif, such as heparansulfate, LPS, and lipoteichoic acid. Dose-response studies in Dmbt1(-/-) and Dmbt1(+/+) mice utilizing the DSS-induced colitis model demonstrate a differential response only to low but not to high DSS doses. We propose that DMBT1 functions as pattern-recognition molecule for poly-sulfated and poly-phosphorylated ligands providing a molecular basis for its broad bacterial-binding specificity and its inhibitory effects on LPS-induced TLR4-mediated NF-kappaB activation. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Published
2009
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