TY - JOUR A1 - Fedders, Ronja A1 - Muenzner, Matthias A1 - Weber, Pamela A1 - Sommerfeld, Manuela A1 - Knauer, Miriam A1 - Kedziora, Sarah A1 - Kast, Naomi A1 - Heidenreich, Steffi A1 - Raila, Jens A1 - Weger, Stefan A1 - Henze, Andrea A1 - Schupp, Michael T1 - Liver-secreted RBP4 does not impair glucose homeostasis in mice JF - The journal of biological chemistry N2 - Retinol-binding protein 4 (RBP4) is the major transport protein for retinol in blood. Recent evidence from genetic mouse models shows that circulating RBP4 derives exclusively from hepatocytes. Because RBP4 is elevated in obesity and associates with the development of glucose intolerance and insulin resistance, we tested whether a liver-specific overexpression of RBP4 in mice impairs glucose homeostasis. We used adeno-associated viruses (AAV) that contain a highly liver-specific promoter to drive expression of murine RBP4 in livers of adult mice. The resulting increase in serum RBP4 levels in these mice was comparable with elevated levels that were reported in obesity. Surprisingly, we found that increasing circulating RBP4 had no effect on glucose homeostasis. Also during a high-fat diet challenge, elevated levels of RBP4 in the circulation failed to aggravate the worsening of systemic parameters of glucose and energy homeostasis. These findings show that liver-secreted RBP4 does not impair glucose homeostasis. We conclude that a modest increase of its circulating levels in mice, as observed in the obese, insulin-resistant state, is unlikely to be a causative factor for impaired glucose homeostasis. KW - liver KW - retinoid-binding protein KW - glucose metabolism KW - insulin resistance KW - mouse KW - TTR Y1 - 2018 U6 - https://doi.org/10.1074/jbc.RA118.004294 SN - 1083-351X VL - 293 IS - 39 SP - 15269 EP - 15276 PB - American Society for Biochemistry and Molecular Biology CY - Bethesda ER - TY - JOUR A1 - Weingart, C. A1 - Raila, Jens A1 - Lübke-Becker, A. A1 - Kershaw, O. A1 - Brunnberg, M. A1 - Kohn, B. T1 - Calcitriol induced hypercalcemia in a hunting dog with a disseminated Paecilomyces variotii infection T1 - Calcitriol-bedingte Hyperkalzämie bei einem Jagdhund mit disseminierter Paecilomyces variotii-Infektion JF - Schweizer Archiv für Tierheilkunde N2 - A 5-year old hunting dog was presented with reduced appetite, weight loss and polyuria/polydipsia. Hematology and clinical chemistry revealed anemia, leukocytosis, increased liver enzymes, hypoalbuminemia and hypercalcemia. The cytological, pathohistological and microbiological examination identified a disseminated infection with the saprophytic mould fungus Paecilomyces variotii in the biopsies of the spleen and a lymph node. Determination of vitamin D metabolites confirmed a calcitriol induced hypercalcemia. N2 - Ein 5-jähriger Jagdhund wurde wegen verminderter Futteraufnahme, Gewichtsverlust und Polyurie/Polydipsie vorgestellt. In der hämatologischen und klinisch-chemischen Blutuntersuchung wurde neben einer Anämie und Leukozytose eine Erhöhung der Leberenzyme, Hypoalbuminämie und Hyperkalzämie festgestellt. Durch zytologische, pathohistologische und mikrobiologische Untersuchungen von Biopsien aus Milz und Lymphknoten konnte eine systemische Schimmelpilzinfektion mit Paecilomyces variotii nachgewiesen werden. Die Bestimmung der Vitamin-D-Metabolite bestätigte das Vorliegen einer Hyperkalzämie infolge einer Erhöhung der Calcitriolkonzentration. KW - mould fungus KW - calcium KW - polyuria/polydipsia KW - dog KW - Schimmelpilzinfektion KW - Kalzium KW - Polyurie/ Polydipsie KW - Hund Y1 - 2018 U6 - https://doi.org/10.17236/sat00161 SN - 0036-7281 SN - 1664-2848 IS - 5 SP - 313 EP - 319 PB - Gesellschaft Schweizer Tierärztinnen und Tierärzte CY - Bern ET - 160 ER - TY - JOUR A1 - Henze, Andrea A1 - Raila, Jens A1 - Scholze, Alexandra A1 - Zidek, Walter A1 - Tepel, Martin A1 - Schweigert, Florian J. T1 - Does N-Acetylcysteine modulate post-translational modifications of transthyretin in hemodialysis patients? JF - Antioxidants & redox signaling N2 - It is assumed that effects of the thiol antioxidant N-acetylcysteine (NAC) are mediated by interaction with protein-associated cysteine residues, however, information on protein level in vivo are missing. Therefore, we analyzed NAC-induced modifications of the protein transthyretin (TTR) in plasma of hemodialysis patients in a randomized, placebo-controlled study. TTR was selected due to its low molecular weight and the free cysteine residue in the polypeptide chain, which is known to be extensively modified by formation of mixed disulfides. The intravenous application of NAC during a hemodialysis session resulted in a substantial increase of native TTR from median 15% (range 8.8%-30%) to median 40% (37-50) and reduction of S-cysteinylated TTR [51% (44-60) vs. 6.6% (2.4-10)]. Additionally the pronounced formation of a TTR-NAC adduct was detected. However, all these modifications seemed to be reversible. Additionally, in vitro incubation of plasma with NAC confirmed the in vivo results and indicated that changes in post-translational modification pattern of TTR were a function of NAC concentration. Based on these observations and the essential metabolic and biochemical role of protein-associated cysteine residues we hypothesize that the interaction of NAC with proteins may explain altered protein functions due to modification of cysteine residues. Antioxid. Redox Signal. 19, 1166-1172. Y1 - 2013 U6 - https://doi.org/10.1089/ars.2012.5125 SN - 1523-0864 VL - 19 IS - 11 SP - 1166 EP - 1172 PB - Liebert CY - New Rochelle ER - TY - CHAP A1 - Schweigert, Florian J. A1 - Raila, Jens A1 - Mothes, Ralf A1 - Frey, S. T1 - Point of care measurements of Vitamin A in blood and breast milk for low resource settings T2 - Annals of nutrition & metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS) KW - Blood KW - Milk KW - Point of Care Assay and Vitamin A Y1 - 2011 SN - 0250-6807 VL - 58 IS - 2 SP - 382 EP - 382 PB - Karger CY - Basel ER -