Högskolan i Skövde

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  • 1.
    Carlström, Karl E.
    et al.
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Ewing, Ewoud
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Granqvist, Mathias
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Gyllenberg, Alexandra
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Aeinehband, Shahin
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Enoksson, Sara Lind
    Department of Clinical Immunology Karolinska University Hospital, Stockholm, Sweden.
    Checa, Antonio
    Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
    Badam, Tejaswi
    University of Skövde, School of Bioscience. University of Skövde, The Systems Biology Research Centre. Department of Physics, Chemistry & Biology (IFM), Bioinformatics, Linköping University, Sweden.
    Huang, Jesse
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Gomez-Cabrero, David
    Translational Bioinformatics Unit, Navarrabiomed, Complejo Hospitalario de Navarra (CHN), Universidad Publica de Nevarra (UPNA), IdiSNA, Pamplona, Spain.
    Gustafsson, Mika
    Department of Physics, Chemistry and Biology, Linköping University, Sweden.
    Al Nimer, Faiez
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Wheelock, Craig E.
    Division of Physiological Chemistry II, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
    Kockum, Ingrid
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Olsson, Tomas
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Jagodic, Maja
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Piehl, Fredrik
    Department of Clinical Neurosciences, Section of Neurology, Karolinska Institutet, Stockholm, Sweden.
    Therapeutic efficacy of dimethyl fumarate in relapsing-remitting multiple sclerosis associates with ROS pathway in monocytes2019In: Nature Communications, E-ISSN 2041-1723, Vol. 10, no 1, p. 1-13, article id 3081Article in journal (Refereed)
    Abstract [en]

    Dimethyl fumarate (DMF) is a first-line-treatment for relapsing-remitting multiple sclerosis (RRMS). The redox master regulator Nrf2, essential for redox balance, is a target of DMF, but its precise therapeutic mechanisms of action remain elusive. Here we show impact of DMF on circulating monocytes and T cells in a prospective longitudinal RRMS patient cohort. DMF increases the level of oxidized isoprostanes in peripheral blood. Other observed changes, including methylome and transcriptome profiles, occur in monocytes prior to T cells. Importantly, monocyte counts and monocytic ROS increase following DMF and distinguish patients with beneficial treatment-response from non-responders. A single nucleotide polymorphism in the ROS-generating NOX3 gene is associated with beneficial DMF treatment-response. Our data implicate monocyte-derived oxidative processes in autoimmune diseases and their treatment, and identify NOX3 genetic variant, monocyte counts and redox state as parameters potentially useful to inform clinical decisions on DMF therapy of RRMS.

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  • 2.
    Davegårdh, Cajsa
    et al.
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    Säll, Johanna
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    Benrick, Anna
    University of Skövde, School of Health Sciences. University of Skövde, Digital Health Research (DHEAR). Department of Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy, University of Gothenburg, Sweden.
    Broholm, Christa
    Diabetes and Bone-metabolic Research Unit, Department of Endocrinology, Rigshospitalet, Copenhagen, Denmark.
    Volkov, Petr
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    Perfilyev, Alexander
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    Henriksen, Tora Ida
    The Centre of Inflammation and Metabolism and the Centre for Physical Activity Research, Rigshospitalet, University of Copenhagen, Denmark.
    Wu, Yanling
    Department of Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy, University of Gothenburg, Sweden.
    Hjort, Line
    Diabetes and Bone-metabolic Research Unit, Department of Endocrinology, Rigshospitalet, Copenhagen, Denmark ; Department of Obstetrics, Rigshospitalet, Copenhagen, Denmark.
    Brøns, Charlotte
    Diabetes and Bone-metabolic Research Unit, Department of Endocrinology, Rigshospitalet, Copenhagen, Denmark.
    Hansson, Ola
    Genomics, Diabetes and Endocrinology Unit, Department of Clinical Sciences, Lund University, Malmö, Sweden ; Finnish Institute of Molecular Medicine, University of Helsinki, Finland.
    Pedersen, Maria
    The Centre of Inflammation and Metabolism and the Centre for Physical Activity Research, Rigshospitalet, University of Copenhagen, Denmark.
    Würthner, Jens U.
    ADC Therapeutics, Biopole, Epalinges, Switzerland.
    Pfeffer, Klaus
    Institute of Medical Microbiology and Hospital Hygiene, Heinrich Heine University Düsseldorf, Germany.
    Nilsson, Emma
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    Vaag, Allan
    Steno Diabetes Center Copenhagen, Gentofte, Denmark.
    Stener-Victorin, Elisabet
    Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Pircs, Karolina
    Laboratory of Molecular Neurogenetics, Department of Experimental Medical Science, Wallenberg Neuroscience Center and Lund Stem Cell Center, Lund University, Sweden.
    Scheele, Camilla
    The Centre of Inflammation and Metabolism and the Centre for Physical Activity Research, Rigshospitalet, University of Copenhagen, Denmark ; Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
    Ling, Charlotte
    Epigenetics and Diabetes Unit, Department of Clinical Sciences, Lund University Diabetes Centre, Lund University, Scania University Hospital, Malmö, Sweden.
    VPS39-deficiency observed in type 2 diabetes impairs muscle stem cell differentiation via altered autophagy and epigenetics2021In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 2431Article in journal (Refereed)
    Abstract [en]

    Insulin resistance and lower muscle quality (strength divided by mass) are hallmarks of type 2 diabetes (T2D). Here, we explore whether alterations in muscle stem cells (myoblasts) from individuals with T2D contribute to these phenotypes. We identify VPS39 as an important regulator of myoblast differentiation and muscle glucose uptake, and VPS39 is downregulated in myoblasts and myotubes from individuals with T2D. We discover a pathway connecting VPS39-deficiency in human myoblasts to impaired autophagy, abnormal epigenetic reprogramming, dysregulation of myogenic regulators, and perturbed differentiation. VPS39 knockdown in human myoblasts has profound effects on autophagic flux, insulin signaling, epigenetic enzymes, DNA methylation and expression of myogenic regulators, and gene sets related to the cell cycle, muscle structure and apoptosis. These data mimic what is observed in myoblasts from individuals with T2D. Furthermore, the muscle of Vps39+/− mice display reduced glucose uptake and altered expression of genes regulating autophagy, epigenetic programming, and myogenesis. Overall, VPS39-deficiency contributes to impaired muscle differentiation and reduced glucose uptake. VPS39 thereby offers a therapeutic target for T2D. 

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  • 3.
    Di Marco, I.
    et al.
    Uppsala University, Sweden.
    Thunström, P.
    Uppsala University, Sweden / Institute for Solid State Physics, Vienna University of Technology, Austria.
    Katsnelson, M. I.
    Radboud University Nijmegen, The Netherlands.
    Sadowski, J.
    Polish Academy of Sciences, Poland / Lund University, Sweden.
    Karlsson, Krister
    University of Skövde, School of Life Sciences. University of Skövde, The Virtual Systems Research Centre.
    Lebegue, S.
    Institut Jean Barriol, Université de Lorraine, France.
    Kanski, J.
    Chalmers University of Technology, Sweden.
    Eriksson, O.
    Uppsala University, Sweden.
    Electron correlations in MnxGa1-xAs as seen by resonant electron spectroscopy and dynamical mean field theory2013In: Nature Communications, E-ISSN 2041-1723, Vol. 4, article id 2645Article in journal (Refereed)
    Abstract [en]

    After two decades since the discovery of ferromagnetism in manganese-doped gallium arsenide, its origin is still debated, and many doubts are related to the electronic structure. Here we report an experimental and theoretical study of the valence electron spectrum of manganese-doped gallium arsenide. The experimental data are obtained through the differences between off- and on-resonance photo emission data. The theoretical spectrum is calculated by means of a combination of density-functional theory in the local density approximation and dynamical mean field theory, using exact diagonalization as impurity solver. Theory is found to accurately reproduce measured data and illustrates the importance of correlation effects. Our results demonstrate that the manganese states extend over a broad range of energy, including the top of the valence band, and that no impurity band splits-off from the valence band edge, whereas the induced holes seem located primarily around the manganese impurity.

  • 4.
    Jonsson, Tomas
    et al.
    University of Skövde, School of Bioscience. University of Skövde, The Systems Biology Research Centre. Department of Ecology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
    Setzer, Malin
    University of Skövde, School of Bioscience. University of Skövde, The Systems Biology Research Centre.
    A freshwater predator hit twice by effects of warming across trophic levels2015In: Nature Communications, E-ISSN 2041-1723, Vol. 6, article id 5992Article in journal (Refereed)
  • 5.
    Åkesson, Julia
    et al.
    University of Skövde, School of Bioscience. University of Skövde, Systems Biology Research Environment. Bioinformatics, Department of Physics, Chemistry and Biology, Linköping University, Sweden.
    Hojjati, Sara
    Division of Inflammation and Infection, Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Hellberg, Sandra
    Bioinformatics, Department of Physics, Chemistry and Biology, Linköping University, Sweden ; Division of Inflammation and Infection, Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Raffetseder, Johanna
    Division of Inflammation and Infection, Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Khademi, Mohsen
    Neuroimmunology Unit, Department of Clinical Neuroscience, Center for Molecular Medicine, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden.
    Rynkowski, Robert
    Department of Neurology, and Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Kockum, Ingrid
    Neuroimmunology Unit, Department of Clinical Neuroscience, Center for Molecular Medicine, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden.
    Altafini, Claudio
    Division of Automatic Control, Department of Electrical Engineering, Linköping University, Sweden.
    Lubovac-Pilav, Zelmina
    University of Skövde, School of Bioscience. University of Skövde, Systems Biology Research Environment.
    Mellergård, Johan
    Department of Neurology, and Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Jenmalm, Maria C.
    Division of Inflammation and Infection, Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Piehl, Fredrik
    Neuroimmunology Unit, Department of Clinical Neuroscience, Center for Molecular Medicine, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden.
    Olsson, Tomas
    Neuroimmunology Unit, Department of Clinical Neuroscience, Center for Molecular Medicine, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden.
    Ernerudh, Jan
    Department of Clinical Immunology and Transfusion Medicine, and Department of Biomedical and Clinical Sciences, Linköping University, Sweden.
    Gustafsson, Mika
    Bioinformatics, Department of Physics, Chemistry and Biology, Linköping University, Sweden.
    Proteomics reveal biomarkers for diagnosis, disease activity and long-term disability outcomes in multiple sclerosis2023In: Nature Communications, E-ISSN 2041-1723, Vol. 14, no 1, article id 6903Article in journal (Refereed)
    Abstract [en]

    Sensitive and reliable protein biomarkers are needed to predict disease trajectory and personalize treatment strategies for multiple sclerosis (MS). Here, we use the highly sensitive proximity-extension assay combined with next-generation sequencing (Olink Explore) to quantify 1463 proteins in cerebrospinal fluid (CSF) and plasma from 143 people with early-stage MS and 43 healthy controls. With longitudinally followed discovery and replication cohorts, we identify CSF proteins that consistently predicted both short- and long-term disease progression. Lower levels of neurofilament light chain (NfL) in CSF is superior in predicting the absence of disease activity two years after sampling (replication AUC = 0.77) compared to all other tested proteins. Importantly, we also identify a combination of 11 CSF proteins (CXCL13, LTA, FCN2, ICAM3, LY9, SLAMF7, TYMP, CHI3L1, FYB1, TNFRSF1B and NfL) that predict the severity of disability worsening according to the normalized age-related MS severity score (replication AUC = 0.90). The identification of these proteins may help elucidate pathogenetic processes and might aid decisions on treatment strategies for persons with MS.

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