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1. Myotonic dystrophy CTG expansion affects synaptic vesicle proteins, neurotransmission and mouse behaviour. : Synaptic dysfunction in myotonic dystrophy

Author

Takashi Kimura, Bulmaro Cisneros, Esther Steidl, F. Trovero, Elodie Marciniak, Arnold Munnich, Yasuhiro Suzuki, Luc Buée, Geneviève Gourdon, Bruno Buisson, Oscar Hernández-Hernández, Hélène Obriot, Friedrich Metzger, Stefanie Saenger, Maurice S. Swanson, Tohru Matsuura, Konstantinos Charizanis, Jean-Charles Bizot, Mário Gomes-Pereira, Guillaume Bassez, Sabrina Luilier, Caroline Chevarin, Géraldine Sicot, Sandrine Humez, Michel Hamon, Kuang-Yung Lee, Nicolas Sergeant, Aline Huguet, Céline Guiraud-Dogan, Annie Nicole, Lucile Revillod, Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement (Inserm U781), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Département de pathologie [Mondor], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Henri Mondor-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Parc Technologique de la Source, Key-Obs, Neuroservice, Laboratoire privé, CNS Discovery Research, F. Hoffmann-La Roche [Basel], Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837 (JPArc), Université Lille Nord de France (COMUE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Institut de psychiatrie et neurosciences (U894 / UMS 1266), Department of Molecular Genetics and Microbiology and the Center for NeuroGenetics, University of Florida [Gainesville] (UF), Department of Neurology, Chang Gung Memorial Hospital [Taipei] (CGMH), National Hospital Organization-Asahikawa Medical Center, Okayama University, Departamento de Génética y Biologia Molecular, Centro de Investigacion y de Estufios Avanzados del I.P.N., Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Université de Lille, Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement ( Inserm U781 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Assistance publique - Hôpitaux de Paris (AP-HP)-Hôpital Henri Mondor-Université Paris-Est Créteil Val-de-Marne - Paris 12 ( UPEC UP12 ), Centre de recherche Jean-Pierre Aubert-Neurosciences et Cancer, Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Lille, Droit et Santé, Centre de Psychiatrie et Neurosciences ( CPN - U894 ), University of Florida [Gainesville], Chang Gung Memorial Hospital, Okayama University [Okayama], Institut Mondor de Recherche Biomédicale ( IMRB ), and Institut National de la Santé et de la Recherche Médicale ( INSERM ) -IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 ( UPEC UP12 )

Subjects
Genetically modified mouse, Adult, Male, Synapsin I, Central nervous system, Blotting, Western, Mice, Transgenic, Biology, Real-Time Polymerase Chain Reaction, Myotonic dystrophy, Synaptic Transmission, Synapse, 03 medical and health sciences, Mice, 0302 clinical medicine, synapse, medicine, Animals, Humans, Electrophoresis, Gel, Two-Dimensional, In Situ Hybridization, Fluorescence, mouse, 030304 developmental biology, Aged, 0303 health sciences, [SDV.GEN]Life Sciences [q-bio]/Genetics, myotonic dystrophy, Behavior, Animal, Reverse Transcriptase Polymerase Chain Reaction, Original Articles, Middle Aged, medicine.disease, Myotonia, central nervous system, 3. Good health, Electrophysiology, medicine.anatomical_structure, Synaptic plasticity, Neurology (clinical), Synaptic Vesicles, [ SDV.GEN ] Life Sciences [q-bio]/Genetics, Trinucleotide repeat expansion, Trinucleotide Repeat Expansion, Neuroscience, 030217 neurology & neurosurgery
Abstract

International audience; Myotonic dystrophy type 1 is a complex multisystemic inherited disorder, which displays multiple debilitating neurological manifestations. Despite recent progress in the understanding of the molecular pathogenesis of myotonic dystrophy type 1 in skeletal muscle and heart, the pathways affected in the central nervous system are largely unknown. To address this question, we studied the only transgenic mouse line expressing CTG trinucleotide repeats in the central nervous system. These mice recreate molecular features of RNA toxicity, such as RNA foci accumulation and missplicing. They exhibit relevant behavioural and cognitive phenotypes, deficits in short-term synaptic plasticity, as well as changes in neurochemical levels. In the search for disease intermediates affected by disease mutation, a global proteomics approach revealed RAB3A upregulation and synapsin I hyperphosphorylation in the central nervous system of transgenic mice, transfected cells and post-mortem brains of patients with myotonic dystrophy type 1. These protein defects were associated with electrophysiological and behavioural deficits in mice and altered spontaneous neurosecretion in cell culture. Taking advantage of a relevant transgenic mouse of a complex human disease, we found a novel connection between physiological phenotypes and synaptic protein dysregulation, indicative of synaptic dysfunction in myotonic dystrophy type 1 brain pathology.

Published
2013
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2. Misregulation of miR-1 processing is associated with heart defects in myotonic dystrophy

Author

John W. Day, Frédérique Rau, Masanori P. Takahashi, Fernande Freyermuth, Harutoshi Fujimura, Annie Nicole, Doulaye Dembélé, Charlotte Fugier, Geneviève Gourdon, Karim Wahbi, Didier Auboeuf, Denis Duboc, Jean-Philippe Villemin, Natacha Dreumont, Denis Furling, Marie-Christine Fischer, Nicolas Charlet-Berguerand, Bernard Jost, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogénèse et progression tumorale, Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM), Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement (Inserm U781), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Université Paris Descartes - Paris 5 (UPD5), Institut de Myologie, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Association française contre les myopathies (AFM-Téléthon)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Toneyama National Hospital, University Graduate School of Medicine [Osaka, Japan], Université Pierre et Marie Curie - Paris 6 (UPMC), and Centre National de la Recherche Scientifique (CNRS)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Association française contre les myopathies (AFM-Téléthon)-Sorbonne Université (SU)

Subjects
Ribonuclease III, [SDV]Life Sciences [q-bio], Connexin, RNA-binding protein, Biology, Myotonic dystrophy, Binding, Competitive, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Downregulation and upregulation, Structural Biology, medicine, MBNL1, Humans, Myotonic Dystrophy, RNA Processing, Post-Transcriptional, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Genetics, 0303 health sciences, Models, Genetic, RNA, RNA-Binding Proteins, medicine.disease, Cell biology, Up-Regulation, DNA-Binding Proteins, MicroRNAs, chemistry, biology.protein, Nucleic Acid Conformation, Trinucleotide repeat expansion, Trinucleotide Repeat Expansion, 030217 neurology & neurosurgery, Dicer
Abstract

Myotonic dystrophy is an RNA gain-of-function disease caused by expanded CUG or CCUG repeats, which sequester the RNA binding protein MBNL1. Here we describe a newly discovered function for MBNL1 as a regulator of pre-miR-1 biogenesis and find that miR-1 processing is altered in heart samples from people with myotonic dystrophy. MBNL1 binds to a UGC motif located within the loop of pre-miR-1 and competes for the binding of LIN28, which promotes pre-miR-1 uridylation by ZCCHC11 (TUT4) and blocks Dicer processing. As a consequence of miR-1 loss, expression of GJA1 (connexin 43) and CACNA1C (Cav1.2), which are targets of miR-1, is increased in both DM1- and DM2-affected hearts. CACNA1C and GJA1 encode the main calcium- and gap-junction channels in heart, respectively, and we propose that their misregulation may contribute to the cardiac dysfunctions observed in affected persons.

Published
2011
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3. Changes in activities of superoxide dismutase, nitric oxide synthase, gluthatione-dependent enzymes and the incidence of apoptosis in sheep corpus luteum duing the estrous cycle

Author

Marie Michaud, Kaïs H Al-Gubory, Guy Germain, Philippe Bolifraud, Annie Nicole, François Blachier, Camille Mayeur, Irene Ceballos-Picot, Biologie du développement et reproduction (BDR), Centre National de la Recherche Scientifique (CNRS)-École nationale vétérinaire d'Alfort (ENVA)-Institut National de la Recherche Agronomique (INRA), Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de nutrition et sécurité alimentaire, and Institut National de la Recherche Agronomique (INRA)

Subjects
[SDV]Life Sciences [q-bio], Glutathione reductase, Biochemistry, chemistry.chemical_compound, 0302 clinical medicine, HYDROGEN PEROXIDE, Progesterone, reproductive and urinary physiology, ComputingMilieux_MISCELLANEOUS, Glutathione Transferase, chemistry.chemical_classification, 0303 health sciences, 030219 obstetrics & reproductive medicine, biology, Glutathione peroxidase, Glutathione, APOPTOSIS, Nitric oxide synthase, Glutathione Reductase, medicine.anatomical_structure, Female, Corpus luteum, hormones, hormone substitutes, and hormone antagonists, endocrine system, medicine.medical_specialty, Biophysics, Estrous Cycle, Luteal phase, Superoxide dismutase, 03 medical and health sciences, Internal medicine, CORPUS LUTEUM, In Situ Nick-End Labeling, medicine, Animals, [INFO]Computer Science [cs], Molecular Biology, 030304 developmental biology, Estrous cycle, Glutathione Peroxidase, Sheep, Superoxide Dismutase, urogenital system, SUPEROXIDE RADICAL, DNA FRAGMENTATION, Endocrinology, chemistry, ANTI- AND PRO-OXIDANT ENZYME, biology.protein, Nitric Oxide Synthase
Abstract

Anti-oxidative enzymes play a role in protecting cells from oxidative stress-induced cell death. The present study was conducted to evaluate whether the anti-oxidant and pro-oxidant enzymatic capacities of the sheep corpus luteum (CL) are correlated with steroidogenic and structural status of the gland during the estrous cycle. Steroidogenic activity, apoptosis and superoxide dismutase (SOD1 and SOD2), nitric oxide synthase (NOS), glutathione peroxidase (GPX), glutathione reductase (GSR) and glutathione S-transferase (GST) activities were determined in the CL at specific developmental stages of the luteal phase. The intensity of apoptotic DNA fragmentation, characteristic of physiological cell death, was much greater in CL at late luteal phase than at early and mid-luteal phase, concomitantly with the diminution in the plasma progesterone concentrations from mid-to late luteal phase. SOD1 and GPX activities increased from early to mid-luteal phase, and increased further at late luteal phase. SOD2 and GST activities were not different between early and mid-luteal phase, but increased at late luteal phase. GSR activity was not different between any luteal phase examined. NOS activity decreased from early to mid- and late luteal phase. These results show that the activities of SOD1, SOD2, NOS, GPX, GSR and GST in the sheep CL are subject to major changes during the estrous cycle, and that the anti-oxidant and pro-oxidant enzymatic capacities of luteal cells are not correlated with cell steroidogenic status and integrity during the late luteal phase.

Published
2005
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4. Reduction of Ischemic Damage in NGF-Transgenic Mice: Correlation with Enhancement of Antioxidant Enzyme Activities

Author

Christelle Guégan, Annie Nicole, Brigitte Onteniente, Brigitte Sola, Elisabeth Chevalier, Irène Ceballos-Picot, Neurodégénérescence : modèles et stratégies thérapeutiques, Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Neuroplasticité et thérapeutique, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Immunité de l'infection et transplantations, and Normandie Université (NU)-Normandie Université (NU)

Subjects
Male, [SDV]Life Sciences [q-bio], medicine.disease_cause, Antioxidants, cerebral ischemia, Brain Ischemia, Mice, 0302 clinical medicine, Glutathione Transferase, bcl-2-Associated X Protein, Cerebral Cortex, chemistry.chemical_classification, 0303 health sciences, biology, Glutathione peroxidase, apoptosis, Cerebral Infarction, superoxide dismutase, bcl-2 Homologous Antagonist-Killer Protein, Proto-Oncogene Proteins c-bcl-2, Neurology, Biochemistry, Mice, Inbred DBA, bcl-Associated Death Protein, Bcl-2 Homologous Antagonist-Killer Protein, medicine.medical_specialty, Programmed cell death, Blotting, Western, bcl-X Protein, Mice, Transgenic, transgenic mice, nerve growth factor, lcsh:RC321-571, Superoxide dismutase, 03 medical and health sciences, Bcl-2-associated X protein, Bcl-2 family, Proto-Oncogene Proteins, Internal medicine, medicine, Animals, Nerve Growth Factors, cardiovascular diseases, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, 030304 developmental biology, Glutathione Peroxidase, Membrane Proteins, glutathione metabolism, Mice, Inbred C57BL, Endocrinology, Nerve growth factor, chemistry, nervous system, Apoptosis, biology.protein, Carrier Proteins, 030217 neurology & neurosurgery, Oxidative stress
Abstract

International audience; If permanent focal ischemia is induced by middle cerebral artery occlusion (MCAO), neurons within the infarcted territory die by necrosis and apoptosis (or programmed cell death). We have previously shown, using a mouse strain transgenic (tg) for the nerve growth factor (NGF) gene, that tg mice have consistently smaller infarcted areas than wild-type (wt) animals, correlated with upregulated NGF synthesis and impaired apoptotic cell death. We studied, in wt and tg mice subjected to MCAO, the activities of several antioxidant enzymes and the synthesis of the proteins of the Bcl-2 family. Our results show that the antiapoptotic Bcl-2 protein and glutathione peroxidase are recruited after MCAO. NGF-tg mice also had an intrinsic resistance to oxidative stress because their basal copper zinc superoxide dismutase (SOD) and glutathione transferase activities were high. Additionally, manganese SOD activity increased in NGF-tg mice after MCAO, correlating strongly with the resistance of these mice to apoptosis.

Published
1999
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