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2. P16 differenziert high-risk GIST und ist ein Prädiktor für ungünstiges Outcome

Author

Kramer, K., Schmieder, M., Wolf, S., Danner, B., Stoehr, S., Knippschild, U., Barth, T., Hasel, C., Henne-Bruns, D., Buhr, H. J., editor, Hölscher, A., editor, Izbicki, J. R., editor, Jauch, K. W., editor, Post, S., editor, Allgayer, H., editor, Bartsch, D. K., editor, Fries, H., editor, Ghadimi, B. M., editor, Habermann, J. K., editor, Kalthoff, H., editor, Schackert, H. K., editor, Bruns, C. J., editor, Duda, D. N., editor, Fändrich, F., editor, Heberer, M., editor, Nüssler, A. K., editor, Stark, G. B., editor, Brückner, U. B., editor, Ertel, W., editor, Faist, E., editor, Heidecke, C. D., editor, Kalff, J. C., editor, Menger, M. D., editor, Schade, U. F., editor, Vollmar, B., editor, Bechstein, W. O., editor, Klar, E., editor, Klempnauer, J., editor, Minor, T., editor, Neuhaus, P., editor, Schmidt, J., editor, Langer, S., editor, Laschke, M. W., editor, Machens, H. G., editor, Steinau, H. U., editor, Südkamp, N., editor, Vogt, P., editor, Berger, D., editor, Klinge, U., editor, Schachtrupp, A., editor, Schilling, M. K., editor, Schumpelick, V., editor, Altendorf-Hofmann, A., editor, Bollschweiler, E., editor, Bruch, H. -P., editor, Lehnert, T., editor, Lorenz, W., editor, Neugebauer, E., editor, Ohmann, C., editor, Seiler, C. M., editor, Becker, H., editor, Betzler, M., editor, Bittner, R., editor, Broelsch, C., editor, Büchler, M. W., editor, Bumm, R., editor, Dralle, H., editor, Friess, H., editor, Frilling, A., editor, Germer, C. T., editor, Hopt, U., editor, Jonas, S., editor, Jost, J., editor, Markus, B., editor, Raab, H. R., editor, Reith, H. B., editor, Schlag, P. M., editor, Teichmann, W., editor, Uhl, W., editor, Wenisch, H., editor, and Zornig, C., editor

Published
2009
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7. Charakterisierung der Bedeutung von CK1δ für die Tumorgenese und-progression des Mammakarzinoms unter Nutzung eines SV40 T-Ag/mtCK1δ bitransgenen Mausmodells

Author

Hirner, H., Grothey, A., Deppert, W., Henne-Bruns, D., Knippschild, U., Buhr, H. J., editor, Hölscher, A., editor, Izbicki, J. R., editor, Jauch, K. W., editor, Post, S., editor, Allgayer, H., editor, Bartsch, D. K., editor, Fries, H., editor, Ghadimi, B. M., editor, Habermann, J. K., editor, Kalthoff, H., editor, Schackert, H. K., editor, Bruns, C. J., editor, Duda, D. N., editor, Fändrich, F., editor, Heberer, M., editor, Nüssler, A. K., editor, Stark, G. B., editor, Brückner, U. B., editor, Ertel, W., editor, Faist, E., editor, Heidecke, C. D., editor, Kalff, J. C., editor, Menger, M. D., editor, Schade, U. F., editor, Vollmar, B., editor, Bechstein, W. O., editor, Klar, E., editor, Klempnauer, J., editor, Minor, T., editor, Neuhaus, P., editor, Schmidt, J., editor, Langer, S., editor, Laschke, M. W., editor, Machens, H. G., editor, Steinau, H. U., editor, Südkamp, N., editor, Vogt, P., editor, Berger, D., editor, Klinge, U., editor, Schachtrupp, A., editor, Schilling, M. K., editor, Schumpelick, V., editor, Altendorf-Hofmann, A., editor, Bollschweiler, E., editor, Bruch, H. -P., editor, Lehnert, T., editor, Lorenz, W., editor, Neugebauer, E., editor, Ohmann, C., editor, Seiler, C. M., editor, Becker, H., editor, Betzler, M., editor, Bittner, R., editor, Broelsch, C., editor, Büchler, M. W., editor, Bumm, R., editor, Dralle, H., editor, Friess, H., editor, Frilling, A., editor, Germer, C. T., editor, Hopt, U., editor, Jonas, S., editor, Jost, J., editor, Markus, B., editor, Raab, H. R., editor, Reith, H. B., editor, Schlag, P. M., editor, Teichmann, W., editor, Uhl, W., editor, Wenisch, H., editor, and Zornig, C., editor

Published
2009
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8. Anti-apoptotic and growth-stimulatory functions of CK1 delta and epsilon in ductal adenocarcinoma of the pancreas are inhibited by IC261 in vitro and in vivo

Author

Brockschmidt, C., Hirner, H., Huber, N., Eismann, T., Hillenbrand, A., Giamas, G., Radunsky, B., Ammerpohl, O., Bohm, B., Henne-Bruns, D., Kalthoff, H., Leithauser, F., Trauzold, A., and Knippschild, U.

Subjects
Protein kinases -- Physiological aspects, Protein kinases -- Research, Apoptosis -- Prevention, Adenocarcinoma -- Prevention, Adenocarcinoma -- Care and treatment, Pancreatic tumors -- Development and progression, Pancreatic tumors -- Care and treatment, Pancreatic tumors -- Research, Health
Published
2008

10. Sensibilisierung resistenter Pankreastumorzelllinien gegenüber einer CD95 vermittelten Apoptose durch Casein Kinase 1 (CK1) spezifische Inhibitoren

Author

Brockschmidt, C., Eismann, T., Kalthoff, H., Henne-Bruns, D., Trauzold, A., Bohm, B., Huber, N., Giamas, G., Knippschild, U., 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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11. Regulation der Casein Kinase 1 delta (CK1δ) Aktivität durch Protein Kinase A (PKA): ein Ansatzpunkt für neue Therapiekonzepte in der Tumorbehandlung?

Author

Knippschild, U., Shoshiashvili, L., Henne-Bruns, D., Giamas, G., 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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20. Structure, regulation, and (patho-)physiological functions of the stress-induced protein kinase CK1 delta (CSNK1D)

Author

Xu, P., Ianes, C., Gärtner, F., Liu, C., Burster, T., Bakulev, V., Rachidi, N., Knippschild, U., and Bischof, J.

Subjects
GENETIC VARIATION, ENZYME STRUCTURE, GENETIC VARIABILITY, STRESS, ISOENZYME, NEOPLASM, CYTOSKELETON, ANTAGONISTS AND INHIBITORS, DISEASE COURSE, HIPPO SIGNALING, CHEMISTRY, GENE SEQUENCE, PHOSPHORYLATION, PRIORITY JOURNAL, GENETIC TRANSCRIPTION, WNT SIGNALING, SEQUENCE ALIGNMENT, CARCINOGENESIS, SIGNAL TRANSDUCTION, HUMAN, HUMANS, MEIOSIS, CANCER, AMINO ACID SEQUENCE, PROTEIN INTERACTION, METABOLIC DISORDER, GENETIC CODE, ENZYME SUBSTRATE, MITOSIS, CASEIN KINASE IDELTA, HEDGEHOG SIGNALING, TUMOR GROWTH, NEOPLASM PROTEINS, NEOPLASMS, SITE-SPECIFIC PHOSPHORYLATION, GENETICS, SMALL MOLECULE INHIBITOR, CIRCADIAN RHYTHM, PATHOPHYSIOLOGY, ISOENZYMES, MOLECULAR RECOGNITION, CSNK1D, METABOLISM, DNA DAMAGE, DRUG DELIVERY SYSTEMS, POLYADENYLATION, CASEIN KINASE 1, NONHUMAN, REVIEW, CELL CYCLE, CSNK1D GENE, STRUCTURE-ACTIVITY RELATIONSHIP, WNT SIGNALING PATHWAY, P53, PROTEIN TARGETING, ANIMALS, ANIMAL, ENZYME REGULATION, PATHOLOGY, RNA FOLDING, HEDGEHOG PATHWAY, TUMOR PROTEIN, PROCEDURES, DRUG DEPENDENCE, DRUG DELIVERY SYSTEM, STRUCTURE ACTIVITY RELATION, STRESS-INDUCED KINASE, CELL STRESS, CELLULAR DISTRIBUTION, ENZYMOLOGY
Abstract

Members of the highly conserved pleiotropic CK1 family of serine/threonine-specific kinases are tightly regulated in the cell and play crucial regulatory roles in multiple cellular processes from protozoa to human. Since their dysregulation as well as mutations within their coding regions contribute to the development of various different pathologies, including cancer and neurodegenerative diseases, they have become interesting new drug targets within the last decade. However, to develop optimized CK1 isoform-specific therapeutics in personalized therapy concepts, a detailed knowledge of the regulation and functions of the different CK1 isoforms, their various splice variants and orthologs is mandatory. In this review we will focus on the stress-induced CK1 isoform delta (CK1δ), thereby addressing its regulation, physiological functions, the consequences of its deregulation for the development and progression of diseases, and its potential as therapeutic drug target. © 2019 Elsevier B.V.

Published
2019

23. Immune Cells and Immunosenescence

Author

Bischof, J., primary, Gärtner, F., additional, Zeiser, K., additional, Kunz, R., additional, Schreiner, C., additional, Hoffer, E., additional, Burster, T., additional, Knippschild, U., additional, and Zimecki, Michał, additional

Published
2019
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30. Prävalenz der nicht-alkoholischen Steatohepatose (NASH) in vier gewichtsabhängigen Patientengruppen; Risikofaktoren und Zusammenhang mit Dünndarmlänge

Author

Hillenbrand, A, Henne-Bruns, D, and Knippschild, U

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Die Nicht-alkoholische Steatohepatitis (NASH) ist eine adipositas assoziiere Ursache einer Hepatitis und kann zu einer Leberzirrhose führen. Mit Zunahme der Adipositas wird die NASH die häufigste Ursache einer Leberzirrhose sein. Wir ermittelten die Prävalenz einer NASH in[zum vollständigen Text gelangen Sie über die oben angegebene URL], 133. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2016
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31. New potential peptide therapeutics perturbing CK1δ/α-tubulin interaction

Author

Krüger, M. Kalbacher, H. Kastritis, P.L. Bischof, J. Barth, H. Henne-Bruns, D. Vorgias, C. Sarno, S. Pinna, L.A. Knippschild, U.

Abstract

Members of the CK1 family are highly conserved serine/threonine specific kinases being expressed in all eukaryotes. They are involved in many cellular processes and therefore tightly regulated. A central mechanism to modulate CK1 activity is via interaction with cellular proteins. CK1δ interacts with α-/β-tubulin and is involved in the regulation of microtubule dynamics. Therefore, it is important to identify the structural elements responsible for the interaction between these proteins. Using a peptide library covering the human CK1δ amino acid sequence in SPR and ELISA analyses, we identified peptide 39 (P39), encompassing aa361-aa375 of CK1δ, as a prominent binding partner of α-tubulin. P39 decreases α-tubulin phosphorylation by CK1δ and reduces the thermodynamic stability of α-tubulin in fluorescence thermal shift assays. Furthermore, P39 induces an inhibition of mitotic progression and a disruption of cells entering mitosis in CV-1 cells. Taken together our data provide valuable information regarding the interaction of CK1δ and α-tubulin and a novel approach for the development of pharmacological tools to inhibit proliferation of cancer cells. © 2016 Elsevier Ireland Ltd.

Published
2016

32. The CK1 family: Contribution to cellular stress response and its role in carcinogenesis

Author

Knippschild, U., Krüger, M., Richter, J., Xu, P., Balbina, García-Reyes, Peifer, C., Halekotte, J., Bakulev, V., and Bischof, J.

Subjects
CASEIN KINASE IBETA, INFLAMMATORY PAIN, PROTEIN EXPRESSION, MICROTUBULE ASSOCIATED PROTEIN, TUBULIN, PROTEIN SERINE THREONINE KINASE, CELL DIFFERENTIATION, CASEIN KINASE IEPSILON, UNCLASSIFIED DRUG, CELL CYCLE REGULATION, DISEASE, NUCLEOTIDE SEQUENCE, BETA CATENIN, ENZYME SPECIFICITY, SCAFFOLD PROTEIN, OXIDATIVE STRESS, ACTIVITY REGULATED CYTOSKELETON ASSOCIATED PROTEIN, SIGNAL TRANSDUCTION, SONIC HEDGEHOG PROTEIN, CARCINOGENESIS, INHIBITOR, HUMAN, M PHASE CELL CYCLE CHECKPOINT, APOPTOSIS, OVARY CANCER, VIRUS PROTEIN, CELLULAR STRESS, HIPPO SIGNALING PATHWAY, CELL PROTEIN, CASEIN KINASE IDELTA, ALCOHOLISM, TUMOR GROWTH, CASEIN KINASE IALPHA, GENE EXPRESSION, PHOSPHATASE, PROTEIN KINASE, FIBRONECTIN, CELLULAR STRESS RESPONSE, PROTEIN MDM2, BREAST CARCINOMA, CELL DIVISION, DNA DAMAGE, INFLAMMATION, CASEIN KINASE 1, IMMUNE RESPONSE, GENE MUTATION, TUMORIGENESIS, CENTROSOME, REVIEW, CASEIN KINASE IGAMMA 1, TUMOR ANTIGEN, CASEIN KINASE IGAMMA 2, CASEIN KINASE IGAMMA 3, GENETIC ANALYSIS, WNT SIGNALING PATHWAY, CIRCADIAN RHYTHM SIGNALING PROTEIN, P53, MOUTH ULCER, PROTEIN P53, ADENOCARCINOMA, PROTEIN STRUCTURE, CASEIN KINASE I
Abstract

Members of the highly conserved and ubiquitously expressed pleiotropic CK1 family play major regulatory roles in many cellular processes including DNA-processing and repair, proliferation, cytoskeleton dynamics, vesicular trafficking, apoptosis, and cell differentiation. As a consequence of cellular stress conditions, interaction of CK1 with the mitotic spindle is manifold increased pointing to regulatory functions at the mitotic checkpoint. Furthermore, CK1 is able to alter the activity of key proteins in signal transduction and signal integration molecules. In line with this notion, CK1 is tightly connected to the regulation and degradation of ß-catenin, p53, and MDM2. Considering the importance of CK1 for accurate cell division and regulation of tumor suppressor functions, it is not surprising that mutations and alterations in the expression and/or activity of CK1 isoforms are often detected in various tumor entities including cancer of the kidney, choriocarcinomas, breast carcinomas, oral cancer, adenocarcinomas of the pancreas, and ovarian cancer. Therefore, scientific effort has enormously increased (i) to understand the regulation of CK1 and its involvement in tumorigenesis- and tumor progression-related signal transduction pathways and (ii) to develop CK1-specific inhibitors for the use in personalized therapy concepts. In this review, we summarize the current knowledge regarding CK1 regulation, function, and interaction with cellular proteins playing central roles in cellular stress-responses and carcinogenesis. © 2014 Knippschild.

Published
2014

34. Impaired CK1 delta activity attenuates SV40-induced cellular transformation in vitro and mouse mammary carcinogenesis in vivo

Author

Hirner, H., Guenes, C., Bischof, J., Wolff, S., Grothey, A., Kueh, M., Oswald, F., Wegwitz, F., Bösl, M., Trauzold, A., Henne-Bruns, D., Peifer, C., Leithaeuser, F., Deppert, W., and Knippschild, U.

Subjects
Male, Models, Molecular, lcsh:Medicine, Mice, Transgenic, Simian virus 40, Biochemistry, Cell Line, Mice, Mammary Glands, Animal, Cell Line, Tumor, Molecular Cell Biology, Animals, Phosphorylation, Antigens, Viral, Tumor, Promoter Regions, Genetic, lcsh:Science, Biology, Mice, Inbred BALB C, lcsh:R, Proteins, Mammary Neoplasms, Experimental, Cell Transformation, Viral, Milk Proteins, Survival Analysis, Cellular Structures, Signaling Cascades, Enzymes, Protein Structure, Tertiary, Phenotype, Gene Expression Regulation, Casein Kinase Idelta, Mutation, Cytochemistry, Disease Progression, Female, lcsh:Q, Research Article, Signal Transduction
Abstract

Simian virus 40 (SV40) is a powerful tool to study cellular transformation in vitro, as well as tumor development and progression in vivo. Various cellular kinases, among them members of the CK1 family, play an important role in modulating the transforming activity of SV40, including the transforming activity of T-Ag, the major transforming protein of SV40, itself. Here we characterized the effects of mutant CK1 delta variants with impaired kinase activity on SV40-induced cell transformation in vitro, and on SV40-induced mammary carcinogenesis in vivo in a transgenic/bi-transgenic mouse model. CK1 delta mutants exhibited a reduced kinase activity compared to wtCK1 delta in in vitro kinase assays. Molecular modeling studies suggested that mutation N172D, located within the substrate binding region, is mainly responsible for impaired mutCK1 delta activity. When stably over-expressed in maximal transformed SV-52 cells, CK1 delta mutants induced reversion to a minimal transformed phenotype by dominant-negative interference with endogenous wtCK1 delta. To characterize the effects of CK1 delta on SV40-induced mammary carcinogenesis, we generated transgenic mice expressing mutant CK1 delta under the control of the whey acidic protein (WAP) gene promoter, and crossed them with SV40 transgenic WAP-T-antigen (WAP-T) mice. Both WAP-T mice as well as WAP-mutCK1 delta/WAP-T bi-transgenic mice developed breast cancer. However, tumor incidence was lower and life span was significantly longer in WAP-mutCK1 delta/WAP-T bi-transgenic animals. The reduced CK1 delta activity did not affect early lesion formation during tumorigenesis, suggesting that impaired CK1 delta activity reduces the probability for outgrowth of in situ carcinomas to invasive carcinomas. The different tumorigenic potential of SV40 in WAP-T and WAP-mutCK1 delta/WAP-T tumors was also reflected by a significantly different expression of various genes known to be involved in tumor progression, specifically of those involved in wnt-signaling and DNA repair. Our data show that inactivating mutations in CK1 delta impair SV40-induced cellular transformation in vitro and mouse mammary carcinogenesis in vivo.

Published
2012

35. Risikoklassifikation bei Gastrointestinalen Stromatumoren

Author

Schmieder, M, Knippschild, U, Henne-Bruns, D, and Kramer, K

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Bei zunehmender Bedeutung adjuvanter Therapieansätze mit Tyrosinkinaseinhibitoren (TKI) bei Gastrointestinalen Stromatumoren wächst das Interesse für bestmögliche Risiko-Indikatoren. Ziel der vorliegenden Studie war die Re-Evaluation von sechs aktuell diskutierten GIST-Risikoklassifikations-Systemen[for full text, please go to the a.m. URL], 129. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2012
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36. Mutationsmuster in Gastrointestinalen Stromatumoren

Author

Schmieder, M, Schwarz, S, Schönleben, A, Melzner, I, Knippschild, U, Henne-Bruns, D, and Kramer, K

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Die meisten GIST zeigen eine gain-of-function-Mutation in c-Kit, ein auf dem Chromosom 4 lokalisiertes Proto-Oncogen oder in PDGFRa/b, ein homologer Typ III Tyrosinkinase-Rezeptor. Nur ein kleiner Teil von Wild-Typ-GIST zeigt weder in c-Kit noch in PDGFRa/b eine Mutation. Ziel [for full text, please go to the a.m. URL], 129. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2012
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37. Cyclin H ist ein Indikator für 'very high-risk' GIST

Author

Kramer, K, Dorn, J, Spatz, J, Barth, T, Danner, B, Schmieder, M, Knippschild, U, and Henne-Bruns, D

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Die Risikoabschätzung von Gastrointestinalen Stromatumoren stützt sich auf Tumorgröße, Mitoserate sowie inkonstant auch auf die Tumorlokalisation (Fletcher 2002, Miettinnen 2006, Hornick 2007 und Joensuu 2008). Dadurch gelingt die Erkennung von „non-high-risk“[for full text, please go to the a.m. URL], 127. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2010
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38. Mögliche Zusammenhänge zwischen adipositas-assoziierten metabolischen Veränderungen und der Entwicklung colorektaler Carcinome

Author

Wolf, A.M., Templin, M., Knippschild, U., Henne-Bruns, D., and Beisiegel, U.

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Die Adipositas ist Ursache einer Reihe schwerwiegender Co-morbiditäten und wird zunehmend auch für die Entwicklung colorektaler Carcinome verantwortlich gemacht. Ausgehend von der Hypothese, dass inflammatorische Vorgänge sowohl die Adipositas als auch die Entstehung colorektaler[for full text, please go to the a.m. URL], 126. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2009
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39. Charakterisierung der Bedeutung von CK1δ für die Tumorgenese und –progression des Mammakarzinoms unter Nutzung eines SV40 T-Ag/mtCK1δ bitransgenen Mausmodells

Author

Hirner, H, Grothey, A, Süssner, N, Deppert, W, Henne-Bruns, D, and Knippschild, U

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Das Mammakarzinom ist der häufigste maligne Tumor der Frau. Das duktale Karzinom stellt dabei die mit Abstand häufigste Entität dar. Die Vorstufe des duktalen Mammakarzinoms wird als ductales Carcinoma in situ (DCIS) bezeichnet. Die entscheidenden malignen Veränderungen,[for full text, please go to the a.m. URL], 126. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2009
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40. P16 differenziert high-risk GIST und ist ein Prädiktor für ungünstiges Outcome

Author

Kramer, K, Schmieder, M, Wolf, S, Danner, B, Stoehr, S, Knippschild, U, Barth, T, Hasel, C, and Henne-Bruns, D

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Einleitung: Die GIST-Risikoklassifikationssysteme, welche Tumorgröße, Mitoserate sowie inkonstant auch die Tumorlokalisation mit einbeziehen (Fletcher 2002, Miettinnen 2006 und Hornick 2007) eignen sich gut zur Unterscheidung von "high-risk" und „non-high-risk“ GIST.[for full text, please go to the a.m. URL], 126. Kongress der Deutschen Gesellschaft für Chirurgie

Published
2009
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43. Phosphorylation of CK1δ: Identification of Ser370 as the major phosphorylation site targeted by PKA in vitro and in vivo

Author

Giamas, G. Hirner, H. Shoshiashvili, L. Grothey, A. Gessert, S. Kühl, M. Henne-Bruns, D. Vorgias, C.E. Knippschild, U.

Abstract

The involvement of CK1 (casein kinase 1) δ in the regulation of multiple cellular processes implies a tight regulation of its activity on many different levels. At the protein level, reversible phosphorylation plays an important role in modulating the activity of CK1δ. In the present study, we show that PKA (cAMP-dependent protein kinase), Akt (protein kinase B), CLK2 (CDC-like kinase 2) and PKC (protein kinase C) α all phosphorylate CK1δ. PKA was identified as the major cellular CK1δCK (CK1δ C-terminal-targeted protein kinase) for the phosphorylation of CK1δ in vitro and in vivo. This was implied by the following evidence: PKA was detectable in the CK1δCK peak fraction of fractionated MiaPaCa-2 cell extracts, PKA shared nearly identical kinetic properties with those of CK1δCK, and both PKA and CK1δCK phosphorylated CK1δ at Ser370 in vitro. Furthermore, phosphorylation of CK15 by PKA decreased substrate phosphorylation of CK1δ in vitro. Mutation of Ser 370 to alanine increased the phosphorylation affinity of CK1δ for β-casein and the GST (gluthatione S-transferase)-p53 1-64 fusion protein in vitro and enhanced the formation of an ectopic dorsal axis during Xenopus laevis development. Anchoring of PKA and CK1δ to centrosomes was mediated by AKAP (A-kinase-anchoring protein) 450. Interestingly, pre-incubation of MiaPaCa-2 cells with the synthetic peptide St-Ht31, which prevents binding between AKAP450 and the regulatory subunit RII of PKA, resulted in a 6-fold increase in the activity of CK1δ. In summary, we conclude that PKA phosphorylates CK1β, predominantly at Ser370 in vitro and in vivo, and that site-specific phosphorylation of CK1δ by PKA plays an important role in modulating CK1δ-dependent processes. © The Authors.

Published
2007

44. Protein kinases as targets for cancer treatment

Author

Giamas, G. Stebbing, J. Vorgias, C.E. Knippschild, U.

Abstract

In various types of malignancies, conventional forms of therapy (surgery, radiation and chemotherapy) are often ineffective, as well as harmful. In the last few years, a convergence of scientific advances has enabled the identification of molecular targets and signaling pathways specific to cancer cells, resulting in therapies with enhanced selectivity and efficacy and reduced toxicity. Compound validation has relied on target validation first, although some of the most successful drugs often have effects outside of their postulated mechanism. Protein kinases represent such molecular targets; considerable research effort has been devoted to the development of targeted drugs that inhibit the action of pathogenic kinases, and clinical studies performed so far have validated the positive effects of kinase inhibitors for cancer treatment. In this review, the specificity, mechanism of action and antitumor activity of several new small-molecule inhibitors of tyrosine and serine/threonine kinases are discussed. © 2007 Future Medicine Ltd.

Published
2007

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