TY - GEN A1 - Schäfer, Paul T1 - Bundesregierung mit Tunnelblick T1 - German government with tunnel vision N2 - Dass die Große Koalition die Kontinuität deutscher Außenpolitik fortsetzt, ist für den Autor, verteidigunspolitischer Sprecher von DIE LINKE, ein Zeichen der Stagnation, sogar des Versagens. Er wirft der Bundesregierung Einfallslosigkeit, mangelndes Engagement und kalte Interessenpolitik vor. Doch neben der umfassenden Kritik werden auch neue Lösungsansätze vorgestellt, die sich auf Erwartungen an die neue US-Administration stützen. KW - Deutsche Außenpolitik KW - NATO KW - DIE LINKE KW - German Foreign Policy KW - NATO KW - DIE LINKE Y1 - 2009 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-32716 SN - 0944-8101 ER - TY - BOOK A1 - Lothar, Bisky A1 - Brie, Andre A1 - Gysi, Gregor A1 - Kickut, Gabriele A1 - Krabatsch, Ernst A1 - liebich, Stefan A1 - Schäfer, Paul A1 - Troost, Axel A1 - Woop, Gerry ED - Liebich, Stefan ED - Woop, Gerry T1 - Linke Aussenpolitik : Reformperspektiven Y1 - 2013 SN - 978-3-941880-65-8 PB - WeltTrends CY - Potsdam ER - TY - GEN A1 - Schäfer, Marjänn Helena A1 - Kakularam, Kumar Reddy A1 - Reisch, Florian A1 - Rothe, Michael A1 - Stehling, Sabine A1 - Heydeck, Dagmar A1 - Püschel, Gerhard Paul A1 - Kuhn, Hartmut T1 - Male Knock-in Mice Expressing an Arachidonic Acid Lipoxygenase 15B (Alox15B) with Humanized Reaction Specificity Are Prematurely Growth Arrested When Aging T2 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Mammalian arachidonic acid lipoxygenases (ALOXs) have been implicated in cell differentiation and in the pathogenesis of inflammation. The mouse genome involves seven functional Alox genes and the encoded enzymes share a high degree of amino acid conservation with their human orthologs. There are, however, functional differences between mouse and human ALOX orthologs. Human ALOX15B oxygenates arachidonic acid exclusively to its 15-hydroperoxy derivative (15S-HpETE), whereas 8S-HpETE is dominantly formed by mouse Alox15b. The structural basis for this functional difference has been explored and in vitro mutagenesis humanized the reaction specificity of the mouse enzyme. To explore whether this mutagenesis strategy may also humanize the reaction specificity of mouse Alox15b in vivo, we created Alox15b knock-in mice expressing the arachidonic acid 15-lipoxygenating Tyr603Asp+His604Val double mutant instead of the 8-lipoxygenating wildtype enzyme. These mice are fertile, display slightly modified plasma oxylipidomes and develop normally up to an age of 24 weeks. At later developmental stages, male Alox15b-KI mice gain significantly less body weight than outbred wildtype controls, but this effect was not observed for female individuals. To explore the possible reasons for the observed gender-specific growth arrest, we determined the basic hematological parameters and found that aged male Alox15b-KI mice exhibited significantly attenuated red blood cell parameters (erythrocyte counts, hematocrit, hemoglobin). Here again, these differences were not observed in female individuals. These data suggest that humanization of the reaction specificity of mouse Alox15b impairs the functionality of the hematopoietic system in males, which is paralleled by a premature growth arrest. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1295 KW - eicosanoids KW - lipid peroxidation KW - oxidative stress KW - polyenoic fatty acids KW - erythropoiesis Y1 - 2023 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-576491 SN - 1866-8372 IS - 1295 ER - TY - JOUR A1 - Schäfer, Marjänn Helena A1 - Kakularam, Kumar Reddy A1 - Reisch, Florian A1 - Rothe, Michael A1 - Stehling, Sabine A1 - Heydeck, Dagmar A1 - Püschel, Gerhard Paul A1 - Kuhn, Hartmut T1 - Male Knock-in Mice Expressing an Arachidonic Acid Lipoxygenase 15B (Alox15B) with Humanized Reaction Specificity Are Prematurely Growth Arrested When Aging JF - Biomedicines N2 - Mammalian arachidonic acid lipoxygenases (ALOXs) have been implicated in cell differentiation and in the pathogenesis of inflammation. The mouse genome involves seven functional Alox genes and the encoded enzymes share a high degree of amino acid conservation with their human orthologs. There are, however, functional differences between mouse and human ALOX orthologs. Human ALOX15B oxygenates arachidonic acid exclusively to its 15-hydroperoxy derivative (15S-HpETE), whereas 8S-HpETE is dominantly formed by mouse Alox15b. The structural basis for this functional difference has been explored and in vitro mutagenesis humanized the reaction specificity of the mouse enzyme. To explore whether this mutagenesis strategy may also humanize the reaction specificity of mouse Alox15b in vivo, we created Alox15b knock-in mice expressing the arachidonic acid 15-lipoxygenating Tyr603Asp+His604Val double mutant instead of the 8-lipoxygenating wildtype enzyme. These mice are fertile, display slightly modified plasma oxylipidomes and develop normally up to an age of 24 weeks. At later developmental stages, male Alox15b-KI mice gain significantly less body weight than outbred wildtype controls, but this effect was not observed for female individuals. To explore the possible reasons for the observed gender-specific growth arrest, we determined the basic hematological parameters and found that aged male Alox15b-KI mice exhibited significantly attenuated red blood cell parameters (erythrocyte counts, hematocrit, hemoglobin). Here again, these differences were not observed in female individuals. These data suggest that humanization of the reaction specificity of mouse Alox15b impairs the functionality of the hematopoietic system in males, which is paralleled by a premature growth arrest. KW - eicosanoids KW - lipid peroxidation KW - oxidative stress KW - polyenoic fatty acids KW - erythropoiesis Y1 - 2022 U6 - https://doi.org/10.3390/biomedicines10061379 SN - 2227-9059 VL - 10 SP - 1 EP - 22 PB - MDPI CY - Basel, Schweiz ET - 6 ER - TY - JOUR A1 - Hocher, Berthold A1 - Oberthür, Dominik A1 - Slowinski, Torsten A1 - Querfeld, Uwe A1 - Schäfer, Franz A1 - Doyon, Anke A1 - Tepel, Martin A1 - Roth, Heinz J. A1 - Grön, Hans J. A1 - Reichetzeder, Christoph A1 - Betzel, Christian A1 - Armbruster, Franz Paul T1 - Modeling of Oxidized PTH (oxPTH) and Non-oxidized PTH (n-oxPTH) Receptor Binding and Relationship of Oxidized to Non-Oxidized PTH in Children with Chronic Renal Failure, Adult Patients on Hemodialysis and Kidney Transplant Recipients JF - Kidney & blood pressure research : official organ of the Gesellschaft für Nephrologie N2 - Background: The biological properties of oxidized and non-oxidized PTH are substantially different. Oxidized PTH (oxPTH) loses its PTH receptor-stimulating properties, whereas non-oxidized PTH (n-oxPTH) is a full agonist of the receptor. This was described in more than 20 well published studies in the 1970(s) and 80(s). However, PTH oxidation has been ignored during the development of PTH assays for clinical use so far. Even the nowadays used third generation assay systems do not consider oxidation of PTH. We recently developed an assay to differentiate between oxPTH and n-oxPTH. In the current study we established normal values for this assay system. Furthermore, we compare the ratio of oxPTH to n-oxPTH in different population with chronic renal failure: 620 children with renal failure stage 2-4 of the 4C study, 342 adult patients on dialysis, and 602 kidney transplant recipients. In addition, we performed modeling of the interaction of either oxPTH or n-oxPTH with the PTH receptor using biophysical structure approaches. Results: The children had the highest mean as well as maximum n-oxPTH concentrations as compared to adult patients (both patients on dialysis as well as kidney transplant recipients). The relationship between oxPTH and n-oxPTH of individual patients varied substantially in all three populations with renal impairment. The analysis of n-oxPTH in 89 healthy control subjects revealed that n-oxPTH concentrations in patient with renal failure were higher as compared to healthy adult controls (2.25-fold in children with renal failure, 1.53-fold in adult patients on dialysis, and 1.56-fold in kidney transplant recipients, respectively). Computer assisted biophysical structure modeling demonstrated, however, minor sterical- and/or electrostatic changes in oxPTH and n-oxPTH. This indicated that PTH oxidation may induce refolding of PTH and hence alters PTH-PTH receptor interaction via oxidation induced three-dimensional structure alteration of PTH. Conclusion: A huge proportion of circulating PTH measured by current state-of-the-art assay systems is oxidized and thus not biologically active. The relationship between oxPTH and n-oxPTH of individual patients varied substantially. Non-oxidized PTH concentrations are 1.5 - 2.25 fold higher in patients with renal failure as compared to health controls. Measurements of n-oxPTH may reflect the hormone status more precise. The iPTH measures describes most likely oxidative stress in patients with renal failure rather than the PTH hormone status. This, however, needs to be demonstrated in further clinical studies. KW - n-oxPTH KW - Chronic Renal Failure KW - Kidney Transplantation KW - Hemodialysis KW - Oxidation KW - PTH KW - Chronic Renal Failure in Children Y1 - 2013 U6 - https://doi.org/10.1159/000350149 SN - 1420-4096 SN - 1423-0143 VL - 37 IS - 4-5 SP - 240 EP - 251 PB - Karger CY - Basel ER - TY - BOOK A1 - Mientus, Lukas A1 - Klempin, Christiane A1 - Nowak, Anna A1 - Wyss, Corinne A1 - Aufschnaiter, Claudia von A1 - Faix, Ann-Christin A1 - te Poel, Kathrin A1 - Wahbe, Nadia A1 - Pieper, Martin A1 - Höller, Katharina A1 - Kallenbach, Lea A1 - Förster, Magdalena A1 - Redecker, Anke A1 - Dick, Mirjam A1 - Holle, Jörg A1 - Schneider, Edina A1 - Rehfeldt, Daniel A1 - Brauns, Sarah A1 - Abels, Simone A1 - Ferencik-Lehmkuhl, Daria A1 - Fränkel, Silvia A1 - Frohn, Julia A1 - Liebsch, Ann-Catherine A1 - Pech, Detlef A1 - Schreier, Pascal A1 - Jessen, Moiken A1 - Großmann, Uta A1 - Skintey, Lesya A1 - Voerkel, Paul A1 - Vaz Ferreira, Mergenfel A. A1 - Zimmermann, Jan-Simon A1 - Buddeberg, Magdalena A1 - Henke, Vanessa A1 - Hornberg, Sabine A1 - Völschow, Yvette A1 - Warrelmann, Julia-Nadine A1 - Malek, Jennifer A1 - Tinnefeld, Anja A1 - Schmidt, Peggy A1 - Bauer, Tobias A1 - Jänisch, Christopher A1 - Spitzer, Lisa A1 - Franken, Nadine A1 - Degeling, Maria A1 - Preisfeld, Angelika A1 - Meier, Jana A1 - Küth, Simon A1 - Scholl, Daniel A1 - Vogelsang, Christoph A1 - Watson, Christina A1 - Weißbach, Anna A1 - Kulgemeyer, Christoph A1 - Oetken, Mandy A1 - Gorski, Sebastian A1 - Kubsch, Marcus A1 - Sorge, Stefan A1 - Wulff, Peter A1 - Fellenz, Carolin D. A1 - Schnell, Susanne A1 - Larisch, Cathleen A1 - Kaiser, Franz A1 - Knott, Christina A1 - Reimer, Stefanie A1 - Stegmüller, Nathalie A1 - Boukrayâa Trabelsi, Kathrin A1 - Schißlbauer, Franziska A1 - Lemberger, Lukas A1 - Barth, Ulrike A1 - Wiehl, Angelika A1 - Rogge, Tim A1 - Böhnke, Anja A1 - Dietz, Dennis A1 - Großmann, Leroy A1 - Wienmeister, Annett A1 - Zoppke, Till A1 - Jiang, Lisa A1 - Grünbauer, Stephanie A1 - Ostersehlt, Dörte A1 - Peukert, Sophia A1 - Schäfer, Christoph A1 - Löbig, Anna A1 - Bröll, Leena A1 - Brandt, Birgit A1 - Breuer, Meike A1 - Dausend, Henriette A1 - Krelle, Michael A1 - Andersen, Gesine A1 - Falke, Sascha A1 - Kindermann-Güzel, Kristin A1 - Körner, Katrina A1 - Lottermoser, Lisa-Marie A1 - Pügner, Kati A1 - Sonnenburg, Nadine A1 - Akarsu, Selim A1 - Rechl, Friederike A1 - Gadinger, Laureen A1 - Heinze, Lena A1 - Wittmann, Eveline A1 - Franke, Manuela A1 - Lachmund, Anne-Marie A1 - Böttger, Julia A1 - Hannover, Bettina A1 - Behrendt, Renata A1 - Conty, Valentina A1 - Grundmann, Stephanie A1 - Ghassemi, Novid A1 - Opitz, Ben A1 - Brämer, Martin A1 - Gasparjan, David A1 - Sambanis, Michaela A1 - Köster, Hilde A1 - Lücke, Martin A1 - Nordmeier, Volkhard A1 - Schaal, Sonja A1 - Haberbosch, Maximilian A1 - Meissner, Maren A1 - Schaal, Steffen A1 - Brüchner, Melanie A1 - Riehle, Tamara A1 - Leopold, Bengta Marie A1 - Gerlach, Susanne A1 - Rau-Patschke, Sarah A1 - Skorsetz, Nina A1 - Weber, Nadine A1 - Damköhler, Jens A1 - Elsholz, Markus A1 - Trefzger, Thomas A1 - Lewek, Tobias A1 - Borowski, Andreas ED - Mientus, Lukas ED - Klempin, Christiane ED - Nowak, Anna T1 - Reflexion in der Lehrkräftebildung BT - Empirisch – Phasenübergreifend – Interdisziplinär T3 - Potsdamer Beiträge für Lehrkräftebildung und Bildungsforschung N2 - Reflexion ist eine Schlüsselkategorie für die professionelle Entwicklung von Lehrkräften, welche als Ausbildungsziel in den Bildungsstandards für die Lehrkräftebildung verankert ist. Eine Verstetigung universitär geprägter Forschung und Modellierung in der praxisnahen Anwendung im schulischen Kontext bietet Potentiale nachhaltiger Professionalisierung. Die Stärkung reflexionsbezogener Kompetenzen durch Empirie und Anwendung scheint eine phasenübergreifende Herausforderung der Lehrkräftebildung zu sein, die es zu bewältigen gilt. Ziele des Tagungsbandes Reflexion in der Lehrkräftebildung sind eine theoretische Schärfung des Konzeptes „Reflexive Professionalisierung“ und der Austausch über Fragen der Einbettung wirksamer reflexionsbezogener Lerngelegenheiten in die Lehrkräftebildung. Forschende und Lehrende der‚ drei Phasen (Studium, Referendariat sowie Fort- und Weiterbildung) der Lehrkräftebildung stellen Lehrkonzepte und Forschungsprojekte zum Thema Reflexion in der Lehrkräftebildung vor und diskutieren diese. Gemeinsam mit Teilnehmenden aller Phasen und von verschiedenen Standorten der Lehrkräftebildung werden zukünftige Herausforderungen identifiziert und Lösungsansätze herausgearbeitet. T3 - Potsdamer Beiträge zur Lehrkräftebildung und Bildungsforschung - 4 KW - Reflexion KW - Lehrkräftebildung KW - Reflexionskompetenz KW - Reflexivität KW - Feedback KW - Reflection KW - Teacher Education KW - Reflection Skills KW - Reflexivity KW - Feedback Y1 - 2023 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-591717 SN - 978-3-86956-566-8 SN - 2626-3556 SN - 2626-4722 IS - 4 PB - Universitätsverlag Potsdam CY - Potsdam ER -