TY - GEN A1 - Hauffe, Robert A1 - Rath, Michaela A1 - Schell, Mareike A1 - Ritter, Katrin A1 - Kappert, Kai A1 - Deubel, Stefanie A1 - Ott, Christiane A1 - Jähnert, Markus A1 - Jonas, Wenke A1 - Schürmann, Annette A1 - Kleinridders, André T1 - HSP60 reduction protects against diet-induced obesity by modulating energy metabolism in adipose tissue T2 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Objective Insulin regulates mitochondrial function, thereby propagating an efficient metabolism. Conversely, diabetes and insulin resistance are linked to mitochondrial dysfunction with a decreased expression of the mitochondrial chaperone HSP60. The aim of this investigation was to determine the effect of a reduced HSP60 expression on the development of obesity and insulin resistance. Methods Control and heterozygous whole-body HSP60 knockout (Hsp60+/−) mice were fed a high-fat diet (HFD, 60% calories from fat) for 16 weeks and subjected to extensive metabolic phenotyping. To understand the effect of HSP60 on white adipose tissue, microarray analysis of gonadal WAT was performed, ex vivo experiments were performed, and a lentiviral knockdown of HSP60 in 3T3-L1 cells was conducted to gain detailed insights into the effect of reduced HSP60 levels on adipocyte homeostasis. Results Male Hsp60+/− mice exhibited lower body weight with lower fat mass. These mice exhibited improved insulin sensitivity compared to control, as assessed by Matsuda Index and HOMA-IR. Accordingly, insulin levels were significantly reduced in Hsp60+/− mice in a glucose tolerance test. However, Hsp60+/− mice exhibited an altered adipose tissue metabolism with elevated insulin-independent glucose uptake, adipocyte hyperplasia in the presence of mitochondrial dysfunction, altered autophagy, and local insulin resistance. Conclusions We discovered that the reduction of HSP60 in mice predominantly affects adipose tissue homeostasis, leading to beneficial alterations in body weight, body composition, and adipocyte morphology, albeit exhibiting local insulin resistance. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1235 KW - Mitochondria KW - Stress response KW - Obesity KW - Glucose homeostasis KW - Insulin resistance KW - Adipose tissue Y1 - 2022 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-548002 SN - 1866-8372 SP - 1 EP - 14 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - JOUR A1 - Aichert, Ingrid A1 - Staiger, Anja A1 - Schulte-Mäter, Anne A1 - Becker-Redding, Ulrike A1 - Stahn, Corinna A1 - Peschke, Claudia A1 - Heide, Judith A1 - Ott, Susan A1 - Herrmann, Heike A1 - Völsch, Juliane A1 - Mayer, Jörg A1 - Rohnke, Lucie A1 - Frank, Ulrike A1 - Stadie, Nicole A1 - Jentsch, Nadine A1 - Blech, Anke A1 - Kurtenbach, Stephanie A1 - Thieke, Johanna A1 - Schröder, Astrid A1 - Stahn, Corinna A1 - Hörnig, Robin A1 - Burchert, Frank A1 - De Bleser, Ria A1 - Heister, Julian A1 - Bartels, Luise A1 - Würzner, Kay-Michael A1 - Böhme, Romy A1 - Burmester, Juliane A1 - Krajewski, Melanie A1 - Nager, Wido A1 - Jungehülsing, Gerhard Jan A1 - Wartenburger, Isabell A1 - Jöbges, Michael A1 - Schwilling, Eleonore A1 - Lidzba, Karen A1 - Winkler, Susanne A1 - Konietzko, Andreas A1 - Krägeloh-Mann, Ingeborg A1 - Rilling, Eva A1 - Wilken, Rainer A1 - Wismann, Kathrin A1 - Glandorf, Birte A1 - Hoffmann, Hannah A1 - Hinnenkamp, Christiane A1 - Rohlmann, Insa A1 - Ludewigt, Jacqueline A1 - Bittner, Christian A1 - Orlov, Tatjana A1 - Claus, Katrin A1 - Ehemann, Christine A1 - Winnecken, Andreas A1 - Hummel, Katja A1 - Breitenstein, Sarah ED - Wahl, Michael ED - Stahn, Corinna ED - Hanne, Sandra ED - Fritzsche, Tom T1 - Spektrum Patholinguistik = Schwerpunktthema: Von der Programmierung zur Artikulation : Sprechapraxie bei Kindern und Erwachsenen N2 - Das 3. Herbsttreffen Patholinguistik fand am 21. November 2009 an der Universität Potsdam statt. Der vorliegende Tagungsband enthält die drei Hauptvorträge zum Schwerpunktthema „Von der Programmierung zu Artikulation: Sprechapraxie bei Kindern und Erwachsenen“. Darüber hinaus enthält der Band die Beiträge aus dem Spektrum Patholinguistik, sowie die Abstracts der Posterpräsentationen. N2 - The 3rd Herbsttreffen Patholinguistik was held on November 21st, 2009 at the University of Potsdam. These proceedings contain the three main lectures of the central topic „From programming to articulation: Apraxia of speech of children and adults “. Additionally this volume contains the contributions of Spektrum Patholinguistik, as well as the abstracts of the poster presentations. T3 - Spektrum Patholinguistik - 3 KW - Patholinguistik KW - Sprechapraxie KW - Sprachtherapie KW - patholinguistics KW - apraxia of speech KW - speech and language therapy Y1 - 2010 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-45470 SN - 978-3-86956-079-3 SN - 1869-3822 SN - 1866-9433 IS - 3 PB - Universitätsverlag Potsdam CY - Potsdam ER - TY - GEN A1 - Raupbach, Jana A1 - Ott, Christiane A1 - König, Jeannette A1 - Grune, Tilman T1 - Proteasomal degradation of glycated proteins depends on substrate unfolding BT - preferred degradation of moderately modified myoglobin T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - The Maillard reaction generates protein modifications which can accumulate during hyperglycemia or aging and may have inflammatory consequences. The proteasome is one of the major intracellular systems involved in the proteolytic degradation of modified proteins but its role in the degradation of glycated proteins is scarcely studied. In this study, chemical and structural changes of glycated myoglobin were analyzed and its degradation by 20S proteasome was studied. Myoglobin was incubated with physiological (5-10 mM), moderate (50-100 mM) and severe levels (300 mM) of glucose or methylglyoxal (MGO, 50 mM). Glycation increased myoglobin's fluorescence and surface hydrophobicity. Severe glycation generated crosslinked proteins as shown by gel electrophoresis. The concentration of advanced glycation endproducts (AGEs) N-epsilon-carboxymethyl lysine (CML), N-epsilon-carboxyethyl lysine (CEL), methylglyoxal-derived hydroimidazolone-1 (MG-H1), pentosidine and pyrraline was analyzed after enzymatic hydrolysis followed by UPLC-MS/MS. Higher concentrations of glucose increased all analyzed AGEs and incubation with MGO led to a pronounced increase of CEL and MG-H1. The binding of the heme group to apo-myoglobin was decreased with increasing glycation indicating the loss of tertiary protein structure. Proteasomal degradation of modified myoglobin compared to native myoglobin depends on the degree of glycation: physiological conditions decreased proteasomal degradation whereas moderate glycation increased degradation. Severe glycation again decreased proteolytic cleavage which might be due to crosslinking of protein monomers. The activity of the proteasomal subunit beta 5 is influenced by the presence of glycated myoglobin. In conclusion, the role of the proteasome in the degradation of glycated proteins is highly dependent on the level of glycation and consequent protein unfolding. KW - glycation KW - myoglobin KW - heme KW - advanced glycation endproducts KW - 20S proteasome Y1 - 2022 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-527570 SN - 1866-8372 SP - 516 EP - 524 ER -