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  • 1.
    Almgren, Malin
    et al.
    Karolinska Institutet.
    Nyengaard, Jens R
    Aarhus University.
    Persson, Bengt
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics .
    Lavebratt, Catharina
    Karolinska Institutet.
    Carbamazepine protects against neuronal hyperplasia and abnormal gene expression in the megencephaly mouse2008In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 32, p. 364-376Article in journal (Refereed)
  • 2.
    Crittenden, Jill R.
    et al.
    MIT, MA 02139 USA; MIT, MA 02139 USA; MIT, MA 02139 USA.
    Zhai, Shenyu
    Northwestern Univ, IL 60611 USA.
    Sauvage, Magdalena
    MIT, MA 02139 USA; MIT, MA 02139 USA; Leibniz Inst Neurobiol, Germany.
    Kitsukawa, Takashi
    Osaka Univ, Japan.
    Burguiere, Eric
    MIT, MA 02139 USA; MIT, MA 02139 USA; Hopl Pitie Salpetriere, France.
    Thomsen, Morgane
    Psychiat Ctr Copenhagen & Univ, Denmark; Harvard Med Sch, MA 02478 USA.
    Zhang, Hui
    Columbia Univ, NY 10032 USA; Thomas Jefferson Univ, PA 19107 USA.
    Costa, Cinzia
    Univ Perugia, Italy.
    Martella, Giuseppina
    IRCCS Fdn Santa Lucia, Italy.
    Ghiglieri, Veronica
    San Raffaele Univ, Italy.
    Picconi, Barbara
    IRCCS San Raffaele Pisana, Italy.
    Pescatore, Karen A.
    Temple Univ, PA 19140 USA; Temple Univ, PA 19140 USA.
    Unterwald, Ellen M.
    Department of Pharmacology and Center for Substance Abuse Research, Temple University School of Medicine, Philadelphia, PA 19140, USA.
    Jackson, Walker
    Linköping University, Department of Biomedical and Clinical Sciences, Division of Neurobiology. Linköping University, Faculty of Medicine and Health Sciences.
    Housman, David E.
    MIT, MA 02139 USA.
    Caine, S. Barak
    Harvard Med Sch, MA 02478 USA.
    Sulzer, David
    Columbia Univ, NY 10032 USA.
    Calabresi, Paolo
    Fdn Policlin Univ Agostino Gemelli IRCC, Italy; Univ Cattolica Sacro Cuore, Italy.
    Smith, Anne C.
    Univ Arizona, AZ 85724 USA.
    Surmeier, D. James
    Northwestern Univ, IL 60611 USA.
    Graybiel, Ann M.
    MIT, MA 02139 USA; MIT, MA 02139 USA.
    CalDAG-GEFI mediates striatal cholinergic modulation of dendritic excitability, synaptic plasticity and psychomotor behaviors2021In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 158, article id 105473Article in journal (Refereed)
    Abstract [en]

    CalDAG-GEFI (CDGI) is a protein highly enriched in the striatum, particularly in the principal spiny projection neurons (SPNs). CDGI is strongly down-regulated in two hyperkinetic conditions related to striatal dysfunction: Huntingtons disease and levodopa-induced dyskinesia in Parkinsons disease. We demonstrate that genetic deletion of CDGI in mice disrupts dendritic, but not somatic, M1 muscarinic receptors (M1Rs) signaling in indirect pathway SPNs. Loss of CDGI reduced temporal integration of excitatory postsynaptic potentials at dendritic glutamatergic synapses and impaired the induction of activity-dependent long-term potentiation. CDGI deletion selectively increased psychostimulant-induced repetitive behaviors, disrupted sequence learning, and eliminated M1R blockade of cocaine self-administration. These findings place CDGI as a major, but previously unrecognized, mediator of cholinergic signaling in the striatum. The effects of CDGI deletion on the selfadministration of drugs of abuse and its marked alterations in hyperkinetic extrapyramidal disorders highlight CDGIs therapeutic potential.

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  • 3.
    Domert, Jakob
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Rao, Sahana Bhima
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Agholme, Lotta
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Brorsson, Ann-Christin
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Marcusson, Jan
    Linköping University, Department of Clinical and Experimental Medicine, Division of Neuroscience. Linköping University, Faculty of Health Sciences.
    Hallbeck, Martin
    Linköping University, Department of Clinical and Experimental Medicine, Division of Inflammation Medicine. Linköping University, Faculty of Health Sciences. Östergötlands Läns Landsting, Center for Diagnostics, Department of Clinical Pathology and Clinical Genetics.
    Nath, Sangeeta
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Spreading of Amyloid-β Peptides via Neuritic Cell-to-cell Transfer Is Dependent on Insufficient Cellular Clearance2014In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 65, p. 82-92Article in journal (Refereed)
    Abstract [en]

    The spreading of pathology through neuronal pathways is likely to be the cause of the progressive cognitive loss observed in Alzheimer's disease (AD) and other neurodegenerative diseases. We have recently shown the propagation of AD pathology via cell-to-cell transfer of oligomeric amyloid beta (Aβ) residues 1-42 (oAβ1-42) using our donor-acceptor 3-D co-culture model. We now show that different Aβ-isoforms (fluorescently labeled 1-42, 3(pE)-40, 1-40 and 11-42 oligomers) can transfer from one cell to another. Thus, transfer is not restricted to a specific Aβ-isoform. Although different Aβ isoforms can transfer, differences in the capacity to clear and/or degrade these aggregated isoforms result in vast differences in the net amounts ending up in the receiving cells and the net remaining Aβ can cause seeding and pathology in the receiving cells. This insufficient clearance and/or degradation by cells creates sizable intracellular accumulations of the aggregation-prone Aβ1-42 isoform, which further promotes cell-to-cell transfer; thus, oAβ1-42 is a potentially toxic isoform. Furthermore, cell-to-cell transfer is shown to be an early event that is seemingly independent of later appearances of cellular toxicity. This phenomenon could explain how seeds for the AD pathology could pass on to new brain areas and gradually induce AD pathology, even before the first cell starts to deteriorate, and how cell-to-cell transfer can act together with the factors that influence cellular clearance and/or degradation in the development of AD.

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  • 4.
    Helmfors, Linda
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, Faculty of Science & Engineering.
    Boman, Andrea
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Medicine and Health Sciences.
    Civitelli, Livia
    Linköping University, Department of Clinical and Experimental Medicine, Division of Neuro and Inflammation Science. Linköping University, Faculty of Medicine and Health Sciences.
    Nath, Sangeeta
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Medicine and Health Sciences.
    Sandin, Linnea
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Medicine and Health Sciences.
    Janefjord, Camilla
    Linköping University, Department of Clinical and Experimental Medicine, Division of Neuro and Inflammation Science. Linköping University, Faculty of Medicine and Health Sciences.
    McCann, Heather
    Neuroscience Research Australia and University of New South Wales, Australia.
    Zetterberg, Henrik
    Clinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden / UCL Institute of Neurology, Queen Square, London, United Kingdom.
    Blennow, Kaj
    Clinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden.
    Halliday, Glenda
    UCL Institute of Neurology, Queen Square, London, United Kingdom.
    Brorsson, Ann-Christin
    Linköping University, Department of Physics, Chemistry and Biology, Molecular Biotechnology. Linköping University, Faculty of Science & Engineering.
    Kågedal, Katarina
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Medicine and Health Sciences.
    Protective properties of lysozyme on β-amyloid pathology: implications for Alzheimer disease2015In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 83, p. 122-133Article in journal (Refereed)
    Abstract [en]

    The hallmarks of Alzheimer disease are amyloid-β plaques and neurofibrillary tangles accompanied by signs of neuroinflammation. Lysozyme is a major player in the innate immune system and has recently been shown to prevent the aggregation of amyloid-β1-40 in vitro. In this study we found that patients with Alzheimer disease have increased lysozyme levels in the cerebrospinal fluid and lysozyme co-localized with amyloid-β in plaques. In Drosophila neuronal co-expression of lysozyme and amyloid-β1-42 reduced the formation of soluble and insoluble amyloid-β species, prolonged survival and improved the activity of amyloid-β1-42 transgenic flies. This suggests that lysozyme levels rise in Alzheimer disease as a compensatory response to amyloid-β increases and aggregation. In support of this, in vitro aggregation assays revealed that lysozyme associates with amyloid-β1-42 and alters its aggregation pathway to counteract the formation of toxic amyloid-β species. Overall, these studies establish a protective role for lysozyme against amyloid-β associated toxicities and identify increased lysozyme in patients with Alzheimer disease. Therefore, lysozyme has potential as a new biomarker as well as a therapeutic target for Alzheimer disease.

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  • 5.
    Hu, Z.
    et al.
    Karolinska Institute, Stockholm, Sweden.
    Ulfendahl, M.
    Karolinska Institute, Stockholm, Sweden.
    Olivius, Petri
    Karolinska Institute/Karolinska University Hospital, Stockholm, Sweden .
    NGF stimulates extensive neurite outgrowth from implanted dorsal root ganglion neurons following transplantation into the adult rat inner ear2005In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 18, no 1, p. 184-192Article in journal (Refereed)
    Abstract [en]

    Neuronal tissue transplantation is a potential way to replace degenerated spiral ganglion neurons (SGNs) since these cells cannot regenerate in adult mammals. To investigate whether nerve growth factor (NGF) can stimulate neurite outgrowth from implanted neurons, mouse embryonic dorsal root ganglion (DRG) cells expressing enhanced green fluorescent protein (EGFP) were transplanted into the scala tympani of adult rats with a supplement of NGF or artificial perilymph. DRG neurons were observed in the cochlea for up to 6 weeks postoperatively. A significant difference was identified in the number of DRG neurons between the NGF and non-NGF groups. In the NGF group, extensive neurite projections from DRGs were found penetrating the osseous modiolus towards the spiral ganglion. These results suggest the possibility that embryonic neuronal implants may become integrated within the adult auditory nervous system. In combination with a cochlear prosthesis, a neuronal implantation strategy may provide a possibility for further treatment of profoundly deaf patients.

  • 6.
    Sandberg, Alexander
    et al.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
    Ling, Helen
    UCL, England.
    Gearing, Marla
    Emory Univ, GA USA.
    Dombroski, Beth
    Univ Penn, PA USA.
    Cantwell, Laura
    Univ Penn, PA USA.
    RBibo, Lea
    University College London, London, UK .
    Levey, Allan
    Emory Univ, GA USA.
    Schellenberg, Gerard D.
    Univ Penn, PA USA.
    Hardy, John
    UCL, England; UCL, England; Hong Kong Univ Sci & Technol, Peoples R China.
    Wood, Nicholas
    UCL, England.
    Fernius, Josefin
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, Faculty of Science & Engineering.
    Nyström, Sofie
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
    Svensson, Samuel
    CBD Solut, Sweden.
    Thor, Stefan
    Univ Queensland, Australia.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
    Revesz, Tamas
    UCL, England.
    Mok, Kin Y.
    UCL, England; UCL, England; Hong Kong Univ Sci & Technol, Peoples R China.
    Fibrillation and molecular characteristics are coherent with clinical and pathological features of 4-repeat tauopathy caused by MAPT variant G273R2020In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 146, article id 105079Article in journal (Refereed)
    Abstract [en]

    Microtubule Associated Protein Tau (MAPT) forms proteopathic aggregates in several diseases. The G273R tau mutation, located in the first repeat region, was found by exome sequencing in a patient who presented with dementia and parkinsonism. We herein return to pathological examination which demonstrated tau immunoreactivity in neurons and glia consistent of mixed progressive supranuclear palsy (PSP) and corticobasal degeneration (CBD) features. To rationalize the pathological findings, we used molecular biophysics to characterize the mutation in more detail in vitro and in Drosophila. The G273R mutation increases the aggregation propensity of 4-repeat (4R) tau and alters the tau binding affinity towards microtubules (MTs) and F-actin. Tau aggregates in PSP and CBD are predominantly 4R tau. Our data suggest that the G273R mutation induces a shift in pool of 4R tau by lower F-actin affinity, alters the conformation of MT bound 4R tau, while increasing chaperoning of 3R tau by binding stronger to F-actin. The mutation augmented fibrillation of 4R tau initiation in vitro and in glial cells in Drosophila and showed preferential seeding of 4R tau in vitro suggestively causing a late onset 4R tauopathy reminiscent of PSP and CBD.

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  • 7. Wang, X Y
    et al.
    Zhu, C L
    Wang, X H
    Hagberg, H
    Korhonen, L
    Linköping University. Uppsala universitet.
    Sandberg, M
    Lindholm, D
    Blomgren, K
    X-linked inhibitor of apoptosis (XIAP) protein protects against caspase activation and tissue loss after neonatal hypoxia-ischemia2004In: Neurobiology of Disease, ISSN 0969-9961, E-ISSN 1095-953X, Vol. 16, no 1, p. 179-189Article in journal (Refereed)
    Abstract [en]

    Nine-day-old transgenic XIAP overexpressing (TG-XIAP) and wildtype mice were subjected to left carotid artery ligation and 10% O-2 for 60 min, leading to widespread infarctions in the ipsilateral hemisphere during reperfusion. The activation of caspase-3 and -9 seen in wild-type animals was virtually abolished in TG-XIAP mice. Tissue loss was significantly reduced from 54.4 +/- 4.1 mm(3) (Mean +/- SEM) in wild-type mice to 33.1 +/- 2.1 mm(3) in the TG-XIAP mice. Injured neurons displayed stronger XIAP staining during reperfusion, particularly in the nuclei. XIAP was colocalized with XAF-1, Smac, and HtrA2 in injured neurons after hypoxia-ischemia (HI). XIAP was cleaved after HI, and Smac immunoprecipitation co-precipitated a 25-kDa C-terminal fragment of XIAP, indicating that Smac preferentially bound to cleaved XIAP. These findings provide the first evidence that increased XIAP levels protect the neonatal brain against HI. (C) 2004 Elsevier Inc. All rights reserved.

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