21 results on '"Ardila-Osorio, Hector"'
Search Results
2. In vitro bioactivity of Bioroot™ RCS, via A4 mouse pulpal stem cells
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Dimitrova-Nakov, Sasha, Uzunoglu, Emel, Ardila-Osorio, Hector, Baudry, Anne, Richard, Gilles, Kellermann, Odile, and Goldberg, Michel
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- 2015
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3. Additional file 2 of Titanium dioxide and carbon black nanoparticles disrupt neuronal homeostasis via excessive activation of cellular prion protein signaling
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Ribeiro, Luiz W., Pietri, Mathéa, Ardila-Osorio, Hector, Baudry, Anne, Boudet-Devaud, François, Bizingre, Chloé, Arellano-Anaya, Zaira E., Haeberlé, Anne-Marie, Gadot, Nicolas, Boland, Sonja, Devineau, Stéphanie, Bailly, Yannick, Kellermann, Odile, Bencsik, Anna, and Schneider, Benoit
- Abstract
Additional file 2: Fig. S1. Hydrodynamic diameter (nm) of TiO2- and CB-NPs measured by DLS in DMEM/F12 at 37 °C. Diameter (nm) of aggregates of TiO2 and CB nanoparticles was measured by DLS following sonication of NPs, dilution in DMEM/F12, and centrifugation for 2 sec at 2000 g to remove large aggregates. At 10, 25 and 50 µg ml−1, TiO2-NPs displayed an average diameter of 130 nm (Polydispersity Index-PDI = 0.21), 206 nm (PDI = 0.53), and 375 nm (PDI = 0.22), respectively, and CB-NPs 171 nm (PDI = 0.13), 188 nm (PDI = 0.15), and 327 nm (PDI = 0.52), respectively. The experiments were performed in triplicates.
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- 2022
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4. Additional file 3 of Titanium dioxide and carbon black nanoparticles disrupt neuronal homeostasis via excessive activation of cellular prion protein signaling
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Ribeiro, Luiz W., Pietri, Mathéa, Ardila-Osorio, Hector, Baudry, Anne, Boudet-Devaud, François, Bizingre, Chloé, Arellano-Anaya, Zaira E., Haeberlé, Anne-Marie, Gadot, Nicolas, Boland, Sonja, Devineau, Stéphanie, Bailly, Yannick, Kellermann, Odile, Bencsik, Anna, and Schneider, Benoit
- Abstract
Additional file 3: Fig. S2. TiO2 and CB nanoparticles provoke TACE depletion and TNFR1 accumulation at the plasma membrane of serotonergic 1C115-HT neuronal cells in a PDK1-dependent manner. TNFR1 a and TACE b immunostaining at the cell surface of 1C115-HT neuronal cells exposed for 4 h to TiO2- or CB-NPs (1 µg cm−2) in the presence or not of the PDK1 inhibitor BX912 (1 µM) and related quantification histograms. Representative images of three experiments performed in triplicates are shown. Values are means ± SEM. * denotes p < 0.05 and **p < 0.01 versus unexposed cells.
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- 2022
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5. Additional file 1 of Titanium dioxide and carbon black nanoparticles disrupt neuronal homeostasis via excessive activation of cellular prion protein signaling
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Ribeiro, Luiz W., Pietri, Mathéa, Ardila-Osorio, Hector, Baudry, Anne, Boudet-Devaud, François, Bizingre, Chloé, Arellano-Anaya, Zaira E., Haeberlé, Anne-Marie, Gadot, Nicolas, Boland, Sonja, Devineau, Stéphanie, Bailly, Yannick, Kellermann, Odile, Bencsik, Anna, and Schneider, Benoit
- Abstract
Additional file 1: Table S1. Hydrodynamic diameter (nm) of TiO2- and CB-NPs in PBS at 22 °C measured by DLS. Diameter (nm) of aggregates of TiO2 and CB nanoparticles (5 up to 80 µg ml−1) measured by DLS after NP sonication, dilution in PBS, and centrifugation for 2 sec at 2000 g to remove large aggregates. The hydrodynamic diameter could not be measured for the 5 µg ml−1 NP concentration. The experiments were performed in triplicates.
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- 2022
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6. Additional file 5 of Titanium dioxide and carbon black nanoparticles disrupt neuronal homeostasis via excessive activation of cellular prion protein signaling
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Ribeiro, Luiz W., Pietri, Mathéa, Ardila-Osorio, Hector, Baudry, Anne, Boudet-Devaud, François, Bizingre, Chloé, Arellano-Anaya, Zaira E., Haeberlé, Anne-Marie, Gadot, Nicolas, Boland, Sonja, Devineau, Stéphanie, Bailly, Yannick, Kellermann, Odile, Bencsik, Anna, and Schneider, Benoit
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animal diseases ,mental disorders ,nervous system diseases - Abstract
Additional file 5: Fig. S4. Corruption of PrPC-coupled signaling pathways by TiO2- and CB-NPs in neuronal cells: toward a pro-Alzheimer effect of some TiO2 and CB nanoparticles. Cellular prion protein PrPC is a plasma membrane receptor recognized by TiO2- and CB-NPs in neuronal cells. The interaction between full-length PrPC and NPs mobilizes PrPC-coupled signaling pathways, leading to (i) the activation of NADPH oxidase and the production of ROS, and (ii) the activation of PDK1 that promotes the internalization of TACE α-secretase and thereby down-regulates TACE shedding activity at the root of plasma membrane TNFR1 accumulation and rise in Aβ40/42 production. Such NP interferences with the PrPC signaling network triggers molecular signs of Alzheimer’s disease: modification of cell redox equilibrium, neuronal priming to TNFα inflammatory stress, and accumulation of neurotoxic Aβ40/42 peptides (Image drawn using Servier medical art).
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- 2022
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7. Additional file 4 of Titanium dioxide and carbon black nanoparticles disrupt neuronal homeostasis via excessive activation of cellular prion protein signaling
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Ribeiro, Luiz W., Pietri, Mathéa, Ardila-Osorio, Hector, Baudry, Anne, Boudet-Devaud, François, Bizingre, Chloé, Arellano-Anaya, Zaira E., Haeberlé, Anne-Marie, Gadot, Nicolas, Boland, Sonja, Devineau, Stéphanie, Bailly, Yannick, Kellermann, Odile, Bencsik, Anna, and Schneider, Benoit
- Abstract
Additional file 4: Fig. S3. TiO2 and CB nanoparticles enhance Aβ40 production in 1C11 precursors and 1C115-HT neuronal cells. a ELISA-based quantification of Aβ40 peptides in 1C11 and 1C115-HT neuronal cells exposed to TiO2- or CB-NPs (1 µg cm−2) up to 24 h. b APP and BACE1 expression level as assessed by RT-qPCR and Western-blotting in 1C11 cells exposed to TiO2- or CB-NPs (1 µg cm−2) for 4 h. c ELISA-based quantification of Aβ40 peptides in 1C115-HT neuronal cells exposed to TiO2- or CB-NPs (1 µg cm−2) for 4 h in the presence or not of a siRNA toward PrPC (siPrP) or the PDK1 inhibitor, BX912 (1 µM). The experiments were performed three times in triplicates. Values are means ± SEM. * denotes p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 versus unexposed cells.
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- 2022
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8. Loss of prion protein control of glucose metabolism promotes neurodegeneration in model of prion diseases
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Arnould, Hélène, Baudouin, Vincent, Baudry, Anne, Ribeiro, Luiz W., Ardila-Osorio, Hector, Pietri, Mathéa, Caradeuc, Cédric, Soultawi, Cynthia, Williams, Declan, Alvarez, Marjorie, Crozet, Carole, Djouadi, Fatima, Laforge, Mireille, Bertho, Gildas, Kellermann, Odile, Launay, Jean-Marie, Schmitt-Ulms, Gerold, Schneider, Benoit, Toxicité environnementale, cibles thérapeutiques, signalisation cellulaire (T3S - UMR_S 1124), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), University of Toronto, Cellules Souches, Plasticité Cellulaire, Médecine Régénératrice et Immunothérapies (IRMB), Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Hôpital Lariboisière-Fernand-Widal [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), F. Hoffmann-La Roche [Basel], SCHNEIDER, Benoit, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), and Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord
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Male ,PrPSc Proteins ,animal diseases ,Biochemistry ,Hippocampus ,Prion Diseases ,Mice ,Medical Conditions ,Glucose Metabolism ,Animal Cells ,Zoonoses ,Medicine and Health Sciences ,Biology (General) ,[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Energy-Producing Organelles ,Neurons ,Organic Compounds ,Monosaccharides ,Fatty Acids ,Brain ,Ketones ,Lipids ,Mitochondria ,Chemistry ,Infectious Diseases ,Physical Sciences ,Carbohydrate Metabolism ,[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] ,Cellular Structures and Organelles ,Cellular Types ,Anatomy ,Research Article ,Pyruvate ,QH301-705.5 ,Carbohydrates ,Bioenergetics ,mental disorders ,Animals ,[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Organic Chemistry ,Chemical Compounds ,Biology and Life Sciences ,Cell Biology ,RC581-607 ,nervous system diseases ,Mice, Inbred C57BL ,Disease Models, Animal ,Oxidative Stress ,Metabolism ,Glucose ,Cellular Neuroscience ,Nerve Degeneration ,Immunologic diseases. Allergy ,Acids ,Protein Kinases ,Neuroscience - Abstract
Corruption of cellular prion protein (PrPC) function(s) at the plasma membrane of neurons is at the root of prion diseases, such as Creutzfeldt-Jakob disease and its variant in humans, and Bovine Spongiform Encephalopathies, better known as mad cow disease, in cattle. The roles exerted by PrPC, however, remain poorly elucidated. With the perspective to grasp the molecular pathways of neurodegeneration occurring in prion diseases, and to identify therapeutic targets, achieving a better understanding of PrPC roles is a priority. Based on global approaches that compare the proteome and metabolome of the PrPC expressing 1C11 neuronal stem cell line to those of PrPnull-1C11 cells stably repressed for PrPC expression, we here unravel that PrPC contributes to the regulation of the energetic metabolism by orienting cells towards mitochondrial oxidative degradation of glucose. Through its coupling to cAMP/protein kinase A signaling, PrPC tones down the expression of the pyruvate dehydrogenase kinase 4 (PDK4). Such an event favors the transfer of pyruvate into mitochondria and its conversion into acetyl-CoA by the pyruvate dehydrogenase complex and, thereby, limits fatty acids β-oxidation and subsequent onset of oxidative stress conditions. The corruption of PrPC metabolic role by pathogenic prions PrPSc causes in the mouse hippocampus an imbalance between glucose oxidative degradation and fatty acids β-oxidation in a PDK4-dependent manner. The inhibition of PDK4 extends the survival of prion-infected mice, supporting that PrPSc-induced deregulation of PDK4 activity and subsequent metabolic derangements contribute to prion diseases. Our study posits PDK4 as a potential therapeutic target to fight against prion diseases., Author summary Transmissible Spongiform Encephalopathies (TSEs), commonly named prion diseases, are caused by pathogenic prions PrPSc that trigger degeneration of neurons in the brain. Although PrPSc exerts its neurotoxicity by corrupting the function(s) of normal cellular prion protein (PrPC), our understanding of the mechanisms involved in prion diseases remains limited. There is still to date no medicine to fight against TSEs. The current study demonstrates that the deregulation of PrPC regulatory function towards glucose metabolism contributes to neurodegeneration in prion diseases. In the brain of prion-infected mice, PrPSc-induced overactivation of pyruvate dehydrogenase kinase 4 (PDK4) and downstream reduction in mitochondria pyruvate dehydrogenase (PDH) activity promote a metabolic shift from glucose oxidative degradation to pro-oxidant fatty acids β-oxidation contributing to prion pathogenesis. The pharmacological inhibition of PDK4 extends the lifespan of prion-infected mice by rescuing normal glucose metabolism. This study opens up new avenues to design PDK4-based therapeutic strategies to combat TSEs.
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- 2021
9. Biochemical analysis of Parkinsonʼs disease-causing variants of Parkin, an E3 ubiquitin–protein ligase with monoubiquitylation capacity
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Hampe, Cornelia, Ardila-Osorio, Hector, Fournier, Margot, Brice, Alexis, and Corti, Olga
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- 2006
10. Apoptosis and TRAF-1 cleavage in Epstein-Barr virus-positive nasopharyngeal carcinoma cells treated with doxorubicin combined with a farnesyl-transferase inhibitor
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Vicat, Jean-Michel, Ardila-Osorio, Hector, Khabir, Abdelmajid, Brezak, Marie-Christine, Viossat, Isabelle, Kasprzyk, Philip, Jlidi, Rachid, Opolon, Paule, Ooka, Tadamassa, Prevost, Grégoire, Huang, Dolly P., and Busson, Pierre
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- 2003
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11. Double-Edge Sword of Sustained ROCK Activation in Prion Diseases through Neuritogenesis Defects and Prion Accumulation
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Alleaume-Butaux , Aurélie, Nicot , Simon, Pietri , Mathéa, Baudry , Anne, Dakowski , Caroline, Tixador , Philippe, Ardila-Osorio , Hector, Haeberlé , Anne-Marie, Bailly , Yannick, Peyrin , Jean-Michel, Launay , Jean-Marie, Kellermann , Odile, Schneider , Benoit, Toxicité environnementale, cibles thérapeutiques, signalisation cellulaire (T3S - UMR_S 1124), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Neurosciences Cellulaires et Intégratives (INCI), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Pharma Research Department, F. Hoffmann-La Roche [Basel], Service de biochimie INSERM UMR-S942, Hôpital Lariboisière-APHP, HAL UPMC, Gestionnaire, Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Cytologie et cytopatholgie neuronales CNRS UPR 3212, Institut des Neurosciences Cellulaires et Intégratives (INCI) CNRS UPR-3212 67084 Strasbourg, Hoffmann-La Roche Ltd, Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Toxicologie, Pharmacologie et Signalisation Cellulaire ( U1124 ), Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing ( B2A ), and Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS )
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rho-Associated Kinases ,PrPSc Proteins ,Neurogenesis ,animal diseases ,Blotting, Western ,Fluorescent Antibody Technique ,Prion Diseases ,nervous system diseases ,Mice, Inbred C57BL ,Disease Models, Animal ,Mice ,nervous system ,[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] ,Lab-On-A-Chip Devices ,Neurites ,Animals ,Immunoprecipitation ,PrPC Proteins ,[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] ,[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] ,Research Article - Abstract
In prion diseases, synapse dysfunction, axon retraction and loss of neuronal polarity precede neuronal death. The mechanisms driving such polarization defects, however, remain unclear. Here, we examined the contribution of RhoA-associated coiled-coil containing kinases (ROCK), key players in neuritogenesis, to prion diseases. We found that overactivation of ROCK signaling occurred in neuronal stem cells infected by pathogenic prions (PrPSc) and impaired the sprouting of neurites. In reconstructed networks of mature neurons, PrPSc-induced ROCK overactivation provoked synapse disconnection and dendrite/axon degeneration. This overactivation of ROCK also disturbed overall neurotransmitter-associated functions. Importantly, we demonstrated that beyond its impact on neuronal polarity ROCK overactivity favored the production of PrPSc through a ROCK-dependent control of 3-phosphoinositide-dependent kinase 1 (PDK1) activity. In non-infectious conditions, ROCK and PDK1 associated within a complex and ROCK phosphorylated PDK1, conferring basal activity to PDK1. In prion-infected neurons, exacerbated ROCK activity increased the pool of PDK1 molecules physically interacting with and phosphorylated by ROCK. ROCK-induced PDK1 overstimulation then canceled the neuroprotective α-cleavage of normal cellular prion protein PrPC by TACE α-secretase, which physiologically precludes PrPSc production. In prion-infected cells, inhibition of ROCK rescued neurite sprouting, preserved neuronal architecture, restored neuronal functions and reduced the amount of PrPSc. In mice challenged with prions, inhibition of ROCK also lowered brain PrPSc accumulation, reduced motor impairment and extended survival. We conclude that ROCK overactivation exerts a double detrimental effect in prion diseases by altering neuronal polarity and triggering PrPSc accumulation. Eventually ROCK emerges as therapeutic target to combat prion diseases., Author Summary Transmissible Spongiform Encephalopathies (TSEs), commonly named prion diseases, are caused by deposition in the brain of pathogenic prions PrPSc that trigger massive neuronal death. Because of our poor understanding of the mechanisms sustaining prion-induced neurodegeneration, there is to date no effective medicine to combat TSEs. The current study demonstrates that ROCK kinases are overactivated in prion-infected cells and contribute to prion pathogenesis at two levels. First, PrPSc-induced ROCK overactivation affects neuronal polarity with synapse disconnection, axon/dendrite degradation, and disturbs neuronal functions. Second, ROCK overactivity amplifies the production of pathogenic prions. The pharmacological inhibition of ROCK protects diseased neurons from PrPSc toxicity by preserving neuronal architecture and functions and lowering PrPSc level. Inhibition of ROCK in prion-infected mice reduces brain PrPSc levels, improves motor activity and extends lifespan. This study opens up new avenues to design ROCK-based therapeutic strategies to fight TSEs.
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- 2015
12. The cellular prion protein controls Notch signalling and neuroectodermal stem cell architecture
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Martin-Lanneree, Severine, Hernandez-Rapp, Julia, Halliez, Sophie, Hirsch, Theo Z., Passet, Bruno, Ardila-Osorio, Hector, Launay, Jean-Marie, Beringue, Vincent, Vilotte, Jean-Luc, Sophie MOUILLET-RICHARD, Toxicité environnementale, cibles thérapeutiques, signalisation cellulaire (T3S - UMR_S 1124), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Biosigne ED419, Université Paris-Sud - Paris 11 (UP11), Unité de recherche Virologie et Immunologie Moléculaires (VIM), Institut National de la Recherche Agronomique (INRA), Génétique Animale et Biologie Intégrative (GABI), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Biomarqueurs CArdioNeuroVASCulaires (BioCANVAS), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Pharma Research Department, Hoffmann-La Roche Ltd, Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), ProdInra, Archive Ouverte, F. Hoffmann-La Roche [Basel], Toxicologie, Pharmacologie et Signalisation Cellulaire (U1124), Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA) - AgroParisTech, and Université Paris Diderot - Paris 7 (UPD7) - Université Paris 13 (UP13) - Institut National de la Santé et de la Recherche Médicale (INSERM)
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prion ,[SDV] Life Sciences [q-bio] ,[SDV]Life Sciences [q-bio] - Abstract
absent
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- 2014
13. Neuritogenesis: the prion protein controls β1 integrin signaling activity
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Loubet, Damien, primary, Dakowski, Caroline, additional, Pietri, Mathéa, additional, Pradines, Elodie, additional, Bernard, Sophie, additional, Callebert, Jacques, additional, Ardila‐Osorio, Hector, additional, Mouillet‐Richard, Sophie, additional, Launay, Jean‐Marie, additional, Kellermann, Odile, additional, and Schneider, Benoit, additional
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- 2011
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14. TRAF interactions with raft-like buoyant complexes, better than TRAF rates of degradation, differentiate signaling by CD40 and EBV latent membrane protein 1
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Ardila-Osorio, Hector, primary, Pioche-Durieu, Catherine, additional, Puvion-Dutilleul, Francine, additional, Clausse, Bernard, additional, Wiels, Jo�lle, additional, Miller, William, additional, Raab-Traub, Nancy, additional, and Busson, Pierre, additional
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- 2004
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15. Evidence of LMP1-TRAF3 interactions in glycosphingolipid-rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells
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Ardila-Osorio, Hector, primary, Clausse, Bernard, additional, Mishal, Zohair, additional, Wiels, Jo�lle, additional, Tursz, Thomas, additional, and Busson, Pierre, additional
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- 1999
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16. Neuritogenesis: the prion protein controls β1 integrin signaling activity.
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Loubet, Damien, Dakowski, Caroline, Pietri, Mathéa, Pradines, Elodie, Bernard, Sophie, Callebert, Jacques, Ardila-Osorio, Hector, Mouillet-Richard, Sophie, Launay, Jean-Marie, Kellermann, Odile, and Schneider, Benoit
- Subjects
CYTOSKELETON ,STEM cells ,NEURAL stem cells ,PRIONS ,ACTIN - Abstract
Cytoskeleton modifications are required for neuronal stem cells to acquire neuronal polarization. Little is known, however, about mechanisms that orchestrate cytoskeleton remodeling along neuritogenesis. Here, we show that the silencing of the cellular prion protein (PrP
C ) impairs the initial sprouting of neurites upon induction of differentiation of the 1C11 neuroectodermal cell line, indicating that PrPC is necessary to neuritogenesis. Such PrPC function relies on its capacity to negatively regulate the clustering, activation, and signaling activity of β1 integrins at the plasma membrane. β1 Integrin aggregation caused by PrPC depletion triggers overactivation of the RhoA-Rho kinase-LIMK-cofilin pathway, which, in turn, alters the turnover of focal adhesions, increases the stability of actin microfilaments, and in fine impairs neurite formation. Inhibition of Rho kinases is sufficient to compensate for the lack of PrPC and to restore neurite sprouting. We also observe an increased secretion of fibronectin in the surrounding milieu of PrPC -depleted 1C11 cells, which likely self-sustains β1 integrin signaling overactivation and contributes to neuritogenesis defect. Our overall data reveal that PrPC contributes to the acquisition of neuronal polarization by modulating β1 integrin activity, cell interaction with fibronectin, and cytoskeleton dynamics. [ABSTRACT FROM AUTHOR]- Published
- 2012
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17. TRAF interactions with raft-like buoyant complexes, better than TRAF rates of degradation, differentiate signaling by CD40 and EBV latent membrane protein 1.
- Author
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Ardila-Osorio, Hector, Pioche-Durieu, Catherine, Puvion-Dutilleul, Francine, Clausse, Bernard, Wiels, Joëlle, Miller, William, Raab-Traub, Nancy, and Busson, Pierre
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- 2005
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18. Evidence of LMP1TRAF3 interactions in glycosphingolipid-rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells
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Ardila-Osorio, Hector, Clausse, Bernard, Mishal, Zohair, Wiels, Joëlle, Tursz, Thomas, and Busson, Pierre
- Abstract
Latent membrane protein 1 (LMP1) is an Epstein-Barr virus (EBV) protein expressed in EBV-transformed B lymphocytes and in approximately 50% of nasopharyngeal carcinomas (NPCs). LMP1 signaling involves several cellular signaling intermediates, especially TNF receptorassociated factors (TRAFs). We have shown previously that LMP1 is highly concentrated in a cell fraction called glycosphingolipid-rich membrane complexes (GSL complexes). We report here that parallel accumulation of LMP1 and TRAF3, but not TRAF1 or TRADD, was observed in GSL complexes from lymphoblastoid and LMP1-positive NPC cells. In contrast, TRAF3 was not concentrated in GSL complexes from LMP1-negative cells. Binding of LMP1 and TRAF3 in GSL complexes was demonstrated in lymphoblastoid and NPC cells, by co-immunoprecipitation with both anti-LMP1 and anti-TRAF3 antibodies. Int. J. Cancer 81:645649, 1999. © 1999 Wiley-Liss, Inc.
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- 1999
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19. Pathogenic prions deviate PrPC signaling in neuronal cells and cause imbalances in A beta clearance
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Sophie MOUILLET-RICHARD, Pradines, Elodie, Hernandez-Rapp, Julia, Villa-Diaz, Ana, Dakowski, Caroline, Ardila-Osorio, Hector, Haik, Stephane, Schneider, Benoit, Launay, Jean-Marie, Kellermann, Odile, and Torres, Juan-Maria
20. O.01: The cellular prion protein controls Notch signalling and neuroectodermal stem cell architecture.
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Martin-Lannerée, Séverine, Hernandez-Rapp, Julia, Halliez, Sophie, Hirsch, Théo Z., Passet, Bruno, Ardila-Osorio, Hector, Launay, Jean-Marie, Béringue, Vincent, Vilotte, Jean-Luc, and Mouillet-Richard, Sophie
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- 2014
21. Double-Edge Sword of Sustained ROCK Activation in Prion Diseases through Neuritogenesis Defects and Prion Accumulation.
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Alleaume-Butaux A, Nicot S, Pietri M, Baudry A, Dakowski C, Tixador P, Ardila-Osorio H, Haeberlé AM, Bailly Y, Peyrin JM, Launay JM, Kellermann O, and Schneider B
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- Animals, Blotting, Western, Disease Models, Animal, Fluorescent Antibody Technique, Immunoprecipitation, Lab-On-A-Chip Devices, Mice, Mice, Inbred C57BL, Neurites metabolism, Neurogenesis, PrPC Proteins metabolism, PrPSc Proteins metabolism, Prion Diseases metabolism, Prion Diseases pathology, rho-Associated Kinases metabolism
- Abstract
In prion diseases, synapse dysfunction, axon retraction and loss of neuronal polarity precede neuronal death. The mechanisms driving such polarization defects, however, remain unclear. Here, we examined the contribution of RhoA-associated coiled-coil containing kinases (ROCK), key players in neuritogenesis, to prion diseases. We found that overactivation of ROCK signaling occurred in neuronal stem cells infected by pathogenic prions (PrPSc) and impaired the sprouting of neurites. In reconstructed networks of mature neurons, PrPSc-induced ROCK overactivation provoked synapse disconnection and dendrite/axon degeneration. This overactivation of ROCK also disturbed overall neurotransmitter-associated functions. Importantly, we demonstrated that beyond its impact on neuronal polarity ROCK overactivity favored the production of PrPSc through a ROCK-dependent control of 3-phosphoinositide-dependent kinase 1 (PDK1) activity. In non-infectious conditions, ROCK and PDK1 associated within a complex and ROCK phosphorylated PDK1, conferring basal activity to PDK1. In prion-infected neurons, exacerbated ROCK activity increased the pool of PDK1 molecules physically interacting with and phosphorylated by ROCK. ROCK-induced PDK1 overstimulation then canceled the neuroprotective α-cleavage of normal cellular prion protein PrPC by TACE α-secretase, which physiologically precludes PrPSc production. In prion-infected cells, inhibition of ROCK rescued neurite sprouting, preserved neuronal architecture, restored neuronal functions and reduced the amount of PrPSc. In mice challenged with prions, inhibition of ROCK also lowered brain PrPSc accumulation, reduced motor impairment and extended survival. We conclude that ROCK overactivation exerts a double detrimental effect in prion diseases by altering neuronal polarity and triggering PrPSc accumulation. Eventually ROCK emerges as therapeutic target to combat prion diseases.
- Published
- 2015
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