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14 results on '"Chafai, Magda"'

1. Missense mutation of Fmr1 results in impaired AMPAR-mediated plasticity and socio-cognitive deficits in mice

Author

Prieto, Marta, Folci, Alessandra, Poupon, Gwénola, Schiavi, Sara, Buzzelli, Valeria, Pronot, Marie, François, Urielle, Pousinha, Paula, Lattuada, Norma, Abelanet, Sophie, Castagnola, Sara, Chafai, Magda, Khayachi, Anouar, Gwizdek, Carole, Brau, Frédéric, Deval, Emmanuel, Francolini, Maura, Bardoni, Barbara, Humeau, Yann, Trezza, Viviana, and Martin, Stéphane

Published
2021
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2. η-secretase processing of APP inhibits neuronal activity in the hippocampus

Author

Willem, Michael, Tahirovic, Sabina, Busche, Marc Aurel, Ovsepian, Saak V., Chafai, Magda, Kootar, Scherazad, Hornburg, Daniel, Evans, Lewis D.B., Moore, Steven, Daria, Anna, Hampel, Heike, Muller, Veronika, Giudici, Camilla, Nuscher, Brigitte, Wenninger-Weinzierl, Andrea, Kremmer, Elisabeth, Heneka, Michael T., Thal, Dietmar R., Giedraitis, Vilmantas, Lannfelt, Lars, Muller, Ulrike, Livesey, Frederick J., Meissner, Felix, Herms, Jochen, Konnerth, Arthur, Marie, Helene, and Haass, Christian

Subjects
Hippocampus (Brain) -- Health aspects, Neural circuitry -- Health aspects, Proteases -- Health aspects, Amyloid beta-protein -- Health aspects, Alzheimer's disease -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Alzheimer disease (AD) is characterized by the accumulation of amyloid plaques, which are predominantly composed of amyloid-β peptide (1). Two principal physiological pathways either prevent or promote amyloid-β generation from its precursor, β-amyloid precursor protein (APP), in a competitive manner (1). Although APP processing has been studied in great detail, unknown proteolytic events seem to hinder stoichiometric analyses of APP metabolism in vivo (2). Here we describe a new physiological APP processing pathway, which generates proteolytic fragments capable of inhibiting neuronal activity within the hippocampus. We identify higher molecular mass carboxy-terminal fragments (CTFs) of APP, termed CTF-η, in addition to the long-known CTF-α and CTF-β fragments generated by the α- and β-secretases ADAM10 (a disintegrin and metalloproteinase 10) and BACE1 (β-site APP cleaving enzyme 1), respectively. CTF-η generation is mediated in part by membrane-bound matrix metalloproteinases such as MT5-MMP, referred to as η-secretase activity. η-Secretase cleavage occurs primarily at amino acids 504-505 of [APP.sub.695], releasing a truncated ectodomain. After shedding of this ectodomain, CTF-η is further processed by ADAM10 and BACE1 to release long and short Aη peptides (termed Aη-α and Aη-β). CTFs produced by η-secretase are enriched in dystrophic neurites in an AD mouse model and in human AD brains. Genetic and pharmacological inhibition of BACE1 activity results in robust accumulation of CTF-η and Aη-α. In mice treated with a potent BACE1 inhibitor, hippocampal long-term potentiation was reduced. Notably, when recombinant or synthetic Aη-α was applied on hippocampal slices exvivo, long-term potentiation was lowered. Furthermore, in vivo single-cell two-photon calcium imaging showed that hippocampal neuronal activity was attenuated by Aη-α. These findings not only demonstrate a major functionally relevant APP processing pathway, but may also indicate potential translational relevance for therapeutic strategies targeting APP processing., To identify new proteolytic pathways of APP, we searched for CTFs other than those giving rise to P3 fragment (CTF-α) or amyloid-β (CTF-β) (3-5). A new CTF with an approximate [...]

Published
2015

3. Influenza vaccination and prognosis of COVID ‐19 in hospitalized patients with diabetes: Results from the CORONADO study

Author

Diallo, A, Pichelin, Matthieu, Wargny, Matthieu, Gourdy, Pierre, Bonnet, JB, Hadjadj, Samy, Cariou, Bertrand, Sultan, Ariane, Galtier, Florence, Mahot, Pascale, Fournier‐Guilloux, Anne‐Laure, Mauduit, Nicolas, Bigot‐corbel, Edith, Boureau, Anne‐Sophie, Dekcer, Laure, Ernould, Audrey, Primot, Claire, Seguin, Anne, Joliveau, Marielle, Pouvreau, Sonia, FOURNIER, Chloé, Thureau, Jeremy, Fonteneau, Edith, Hublain, Pamela, Nantes, Chu, Agasse, Carole, Kergaradec, Mathilde DE, Minville, Vincent, Vardon‐Bounes, Fanny, Martin‐Blondel, Guillaume, Tramunt, Blandine, Turnin, Marie‐Christine, Hanaire, Hélène, Mansuy, Jean‐Michel, Fabre, Didier, Arhainx, Marie‐Blanche, Cazals, Laurent, Combes, Laure, Lami, Emmanuelle, Cianferani, Mallory, Megarbane, Bruno, Leroy, Pierre, Gautier, Jean‐François, Vidal‐Trecan, Tiphaine, Riveline, Jean‐Pierre, Laplanche, Jean‐Louis, Mouly, Stéphane, Potier, Louis, Roussel, Ronan, Taher, Malak, Abouleka, Yawa, Yaker, Fetta, Carlier, Aurelie, Boutten, Anne, Hallot‐Feron, Marilyne, Mourah, Fadila, Thivolet, Charles, Blond, Emilie, Rolland, Muriel, Mendez, Josep Verdecho, Alexandre, Marine, Pottecher, Julien, Richer, Emilie, Meyer, Laurent, Luca, Florina, Lessinger, Jean‐Marc, Bahougne, Thibault, Guerci, Bruno, Ludwig, Lisa, Benzirar, Siham, Malaplate, Catherine, Matton, Thierry, Poissy, Julien, Faure, Karine, Fontaine, Pierre, Baudoux, Florence, Vambergue, Anne, Pekar, Jean David, Lambert, Marc, Yelnik, Cécile, Bruandet, Amélie, Petit, Laurent, Neau, Didier, Rigalleau, Vincent, Berard, Annie, Galioot, Amandine, Coudroy, Remy, Thille, Arnaud, Robert, René, Roblot‐Cazenave, France, Rammaert, Blandine, Saulnier, Pierre Jean, Piguel, Xavier, Benhenda, Nesrine, Husson, Camille, Olivier, Celine, Torremocha, Florence, Fraty, Mathilde, d'assigny, Marie Flamen, Miot, Aurelie, Bossard, Valentin, Klouche, Kada, Makinson, Alain, Bonnet, Jean‐Baptiste, Foulongne, Vincent, Aubron, Cécile, Ansart, Séverine, Kerlan, Véronique, Quiniou, Pascale, Carre, Jean‐Luc, Quesnot, Stéphane, Laviolle, Bruno, Schwebel, Carole, Epaulard, Olivier, Benhamou, Pierre‐Yves, Betry, Cécile, Borel, Anne‐Laure, Lablanche, Sandrine, Guergour, Dorra, Duclos, Catherine, Cosson, Emmanuel, Guyot, Erwan, Deniau, Aurore, Nguyen, Phucthutrang, Reznik, Yves, Joubert, Michael, Allouche, Stéphane, Guittet, Lydia, Grange, Steven, Etienne, Manuel, Prévost, Gaëtan, Brunel, Valéry, Lagier, Jean‐Christophe, Raoult, Didier, Dutour, Anne, Gaborit, Bénédicte, Boulllu, Sandrine, Darmon, Patrice, Lasbleiz, Adèle, Cerino, Mathieu, Romain, Fanny, Houssays, Marie, Quenot, Jean Pierre, Piroth, Lionel, Vergès, Bruno, Duvillard, Laurence, Bonnotte, Bernard, Mercat, Alain, Dubee, Vincent, Allix, Ingrid, Rodien, Patrice, Dhersin, Robin, Lebeault, Maylis, Trzepizur, Wojciech, Loison, Jocelyne, Brangier, Antoine, Asfar, Pierre, Reynier, Pascal, Larcher, Françoise, Joubaud, Françoise, Andreu, Marie‐Rita, Urbanski, Geoffrey, Hubert, Laurent, Annweiler, Cedric, Dellamonica, Jean, Courjon, Johan, Chevalier, Nicolas, Chinetti, Giulia, Chafai, Magda, Mourvillier, Bruno, Bani‐Sadr, Firouze, Barraud, Sarra, Delemer, Brigitte, Gillery, Philippe, Labedade, Pascale, Chabrol, Amélie, Penfornis, Alfred, Petit, Catherine, Amadou, Coralie, Adler, Maxime, Dubost, Clément, Conan, Pierre‐Louis, Bordier, Lyse, Ceppa, Franck, Garcia, Cyril, Sollier, Mathilde, Dupuy, Olivier, Laplance, Sophie, Billuart, Olivier, Aroulanda, Marie Joseph, Olivier, Frédérique, Ayon, Florence, Wilhelm, Nathalie, Epelboin, Loic, Sabbah, Nadia, Charpin, Aurelie, Squara, Pierre, Belliard, Olivier, Dubois, Claude, Marre, Michel, Auchabie, Johann, Courtois, Roxane, Duriez, Thierry, Mergey, Tiphaine, Vallee, Laura, Seguin, Laetitia, Al‐Salameh, Abdallah, Lanoix, Jean‐Philippe, Soriot‐Thomas, Sandrine, Bourgeois‐Descouls, Anne‐Marie, Desailloud, Rachel, Germain, Natacha, Galusca, Bogdan, Belleton, Gwenaelle, Marouani, Nesrine, Palaghiu, Delia, Hammour, Amira, Berdaguer, Fernando, Klopfenstein, Thimothée, Zayet, Hajer, Winiszewski, Patrice, Zanusso, Marie, Garnier, Pauline, Julier, Ingrid, Hamzaoui, Karim, Marty‐Gres, Sophie, Sadki, Tarik, Cadot, Lucile, Dubost, Jean‐Louis, Gonfroy, Céline, Campinos, Catherine, Martres, Pascale, Coulhon, Marie Pierre, Allou, Nicolas, Bachir, Marwa, Hoang, Stella, Kembellec, Candice, Suply, Olivia, Kharcha, Fatima, Devouge, Anne‐Claire, Flaus‐Furmanuk, Anna, Madeline, Isabelle, Ehinger, Vincent, Bastard, Sophie, Raffray, Loic, Renou, Frederic, Bojarski, Aude, Paul, Caroline, Borsu, Karine, Gorlin, Angelique, Bernardo, Servane, Ut, Carole Truong, Renaud, Stephane, Vignoles, Antoine, Foch, Emilie, Masse, Laurie, Grand, Hubert, Ferrand, Helene, Raffaitin‐Cardin, Christelle, Zellagui, Hadjer, Castang‐Brachet, Celine, Boury, Frederique, Tena, Ana Alvarez, Moura, Isabelle, Kalfon, Pierre, Darasteanu, Juliana, Monier, Arnaud, Foucault, Pascal, Depuille, Alexandra, Laugier‐Robiolle, Stéphanie, Caneiro, Patrick, Basso, Maud, Larger, Etienne, Bouam, Samir, Benzenati, Wahiba, Bachir, Leila Ait, Pillegand, Camille Cussac, Vasse, Marc, Michard, Christophe, Montanier, Nathanaëlle, Millot, Luc, Crepet, Françoise, Ratsimba, Danielle, Bouiller, Kevin, Borot, Sophie, Bruckert, Isabelle, Clergeot, Annie, Schillo, Franck, Vignes, Dorothée, Bourgeon‐Ghittori, Muriel, Lachgar, Hamoud, Cursay, Claire Lambert DE, Levante, Stéphane, Auregan, Jean Charles, Merlet, Antoine, Zaragoza, Cécile, Arnault, Gwénaëlle, Loupp, Anne‐Gaëlle, Lesieur, Olivier, Roncato‐Saberan, Mariam, Gouet, Didier, Lemarie, Romain, Allano, Hong_an, Vivier, Emmanuel, Pariset, Caroline, Luyton, Cédric, Marchand, Lucien, Doroszewski, Fanny, Pecquet, Matthieu, Perard, Laurent, Vuillermoz‐Blas, Sylvie, Kacki, Nicolas, Charrier, Patricia, Ducet‐Boiffard, Amélie, Roure, Françoise Desroys, Bourron, Olivier, Bonnefont‐Rousselot, Dominique, Laroche, Suzanne, Phan, Franck, Hartemann, Agnès, CAUSSY, Cyrielle, Disse, Emmanuel, Guerin, Claude, Perpoint, Thomas, Moulin, Philippe, CARTIER, RÉGINE, Hariri, Geoffroy, Chopin, Dorothée, Vatier, Camille, Bourcigaux, Nathalie, Chaigneau, Emmanuelle, Christin‐Maitre, Sophie, Donadille, Bruno, Feve, Bruno, Lamothe, Sophie, Sarfati, Julie, Pernet, Pascal, Chambon, Anne, Demarsy, Delphine, Campagne, Hugo, Latil‐Plat, Françoise, Berne, Monica, Grinand, Marilyne, Touzet, Marion, Zabulon, Aydrey, Craspag, Jocelyne, Ledoux, Catherine, Contaret, Cedric, Janand‐Delenne, Blandine, Giraud, Anaïs, Lacrimini, Marie Lou, Arrivie, Joëlle, Ancelle, Deborah, Guillois, Carine, Fremy, Bénédicte, Chaalal, Amina, Barrande, Gaëlle, Dorange, Anne, Rouanet, Eglantine, Seret‐Begue, Dominique, Saoud, Audrey, Guedj, Anne‐Marie, Bedos, Nathalie, Velayoudom, Fritz‐Line, Dumas, Marie, Gonda, Benoite, Coffin, Christine, Gibiat, Stéphanie, Lungo, Myriam, Bully, Chantal, Serusclat, Pierre, Bully, Stella, Carre, Patricia, Leberre, Jean‐Philippe, Elkhoury, Carlos, THIEUX, Marine, Paradisi‐Prieur, Laetitia, Physiologie & médecine expérimentale du Cœur et des Muscles [U 1046] (PhyMedExp), Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)

Subjects
2019-20 coronavirus outbreak, medicine.medical_specialty, Coronavirus disease 2019 (COVID-19), Hospitalized patients, Influenza vaccine, Endocrinology, Diabetes and Metabolism, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), [SDV]Life Sciences [q-bio], 03 medical and health sciences, 0302 clinical medicine, Endocrinology, Internal medicine, Diabetes mellitus, Influenza, Human, Internal Medicine, Diabetes Mellitus, Research Letter, Medicine, Humans, 030212 general & internal medicine, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, business.industry, SARS-CoV-2, Vaccination, COVID-19, medicine.disease, Prognosis, Research Letters, 3. Good health, Hospitalization, Propensity score matching, business
Abstract

International audience

Published
2021

4. Abnormal AMPAR-mediated synaptic plasticity, cognitive and autistic-like behaviors in a missense Fmr1 mutant mouse model of Fragile X syndrome

Author

Prieto, Marta, primary, Folci, Alessandra, additional, Poupon, Gwénola, additional, Schiavi, Sara, additional, Buzzelli, Valeria, additional, Pronot, Marie, additional, François, Urielle, additional, Pousinha, Paula, additional, Lattuada, Norma, additional, Abelanet, Sophie, additional, Castagnola, Sara, additional, Chafai, Magda, additional, Khayachi, Anouar, additional, Gwizdek, Carole, additional, Brau, Frédéric, additional, Deval, Emmanuel, additional, Francolini, Maura, additional, Bardoni, Barbara, additional, Humeau, Yann, additional, Trezza, Viviana, additional, and Martin, Stéphane, additional

Published
2020
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6. Neuroanatomical distribution and function of the vasopressin V1B receptor in the rat brain deciphered using specific fluorescent ligands

Author

Corbani, Maithé, primary, Marir, Rafik, additional, Trueba, Miguel, additional, Chafai, Magda, additional, Vincent, Anne, additional, Borie, Amélie M., additional, Desarménien, Michel G., additional, Ueta, Yoichi, additional, Tomboly, Csaba, additional, Olma, Aleksandra, additional, Manning, Maurice, additional, and Guillon, Gilles, additional

Published
2018
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7. Sumoylation regulates FMRP-mediated dendritic spine elimination and maturation

Author

Khayachi, Anouar, primary, Gwizdek, Carole, additional, Poupon, Gwénola, additional, Alcor, Damien, additional, Chafai, Magda, additional, Cassé, Frédéric, additional, Maurin, Thomas, additional, Prieto, Marta, additional, Folci, Alessandra, additional, De Graeve, Fabienne, additional, Castagnola, Sara, additional, Gautier, Romain, additional, Schorova, Lenka, additional, Loriol, Céline, additional, Pronot, Marie, additional, Besse, Florence, additional, Brau, Frédéric, additional, Deval, Emmanuel, additional, Bardoni, Barbara, additional, and Martin, Stéphane, additional

Published
2018
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8. eta-Secretase processing of APP inhibits neuronal activity in the hippocampus

Author

Willem, Michael, Tahirovic, Sabina, Busche, Marc Aurel, Ovsepian, Saak V., Chafai, Magda, Kootar, Scherazad, Hornburg, Daniel, Evans, Lewis D. B., Moore, Steven, Daria, Anna, Hampel, Heike, Mueller, Veronika, Giudici, Camilla, Nuscher, Brigitte, Wenninger-Weinzierl, Andrea, Kremmer, Elisabeth, Heneka, Michael T., Thal, Dietmar R., Giedraitis, Vilmantas, Lannfelt, Lars, Mueller, Ulrike, Livesey, Frederick J., Meissner, Felix, Herms, Jochen, Konnerth, Arthur, Marie, Helene, Haass, Christian, Willem, Michael, Tahirovic, Sabina, Busche, Marc Aurel, Ovsepian, Saak V., Chafai, Magda, Kootar, Scherazad, Hornburg, Daniel, Evans, Lewis D. B., Moore, Steven, Daria, Anna, Hampel, Heike, Mueller, Veronika, Giudici, Camilla, Nuscher, Brigitte, Wenninger-Weinzierl, Andrea, Kremmer, Elisabeth, Heneka, Michael T., Thal, Dietmar R., Giedraitis, Vilmantas, Lannfelt, Lars, Mueller, Ulrike, Livesey, Frederick J., Meissner, Felix, Herms, Jochen, Konnerth, Arthur, Marie, Helene, and Haass, Christian

Abstract

Alzheimer disease (AD) is characterized by the accumulation of amyloid plaques, which are predominantly composed of amyloid-beta peptide(1). Two principal physiological pathways either prevent or promote amyloid-beta generation from its precursor, beta-amyloid precursor protein (APP), in a competitive manne(r)1. Although APP processing has been studied in great detail, unknown proteolytic events seem to hinder stoichiometric analyses of APP metabolism in vivo(2). Here we describe a new physiological APP processing pathway, which generates proteolytic fragments capable of inhibiting neuronal activity within the hippocampus. We identify higher molecular mass carboxy-terminal fragments (CTFs) of APP, termed CTF-eta, in addition to the long-known CTF-alpha and CTF-beta fragments generated by the alpha- and beta-secretases ADAM10 (a disintegrin and metalloproteinase 10) and BACE1 (beta-site APP cleaving enzyme 1), respectively. CTF-eta generation is mediated in part by membrane-bound matrix metalloproteinases such as MT5-MMP, referred to as g-secretase activity. g-Secretase cleavage occurs primarily at amino acids 504-505 of APP(695), releasing a truncated ectodomain. After shedding of this ectodomain, CTF-eta is further processed by ADAM10 and BACE1 to release long and short A eta peptides (termed A eta-alpha and A eta-beta). CTFs produced by g-secretase are enriched in dystrophic neurites in an AD mouse model and in human AD brains. Genetic and pharmacological inhibition of BACE1 activity results in robust accumulation of CTF-eta and A eta-alpha. In mice treated with a potent BACE1 inhibitor, hippocampal long-term potentiation was reduced. Notably, when recombinant or synthetic A eta-alpha was applied on hippocampal slices ex vivo, long-term potentiation was lowered. Furthermore, in vivo single-cell two-photon calcium imaging showed that hippocampal neuronal activity was attenuated by A eta-alpha. These findings not only demonstrate a major functionally relevant APP pr

Published
2015
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9. Vasopressin depresses long term potentiation in the mouse hippocampus

Author

Chafai Magda, Guillon Gilles, and Desarmenien Michel

Subjects
Mouse Hippocampus, Behavioral Neuroscience, Psychiatry and Mental health, medicine.medical_specialty, Vasopressin, Neuropsychology and Physiological Psychology, Endocrinology, Neurology, Chemistry, Internal medicine, medicine, Long-term potentiation, Biological Psychiatry
Published
2013

14. Neuroanatomical distribution and function of the vasopressin V 1B receptor in the rat brain deciphered using specific fluorescent ligands.

Author

Corbani M, Marir R, Trueba M, Chafai M, Vincent A, Borie AM, Desarménien MG, Ueta Y, Tomboly C, Olma A, Manning M, and Guillon G

Subjects
Animals, Arginine Vasopressin metabolism, Astrocytes metabolism, CHO Cells, Cricetinae, Cricetulus, HEK293 Cells, Humans, Hypothalamus metabolism, Ligands, Male, Neuroanatomy, Neurons metabolism, Pituitary Gland cytology, Rats, Sprague-Dawley, Receptors, GABA metabolism, Staining and Labeling, Vasopressins metabolism, Brain anatomy & histology, Brain metabolism, Fluorescent Dyes metabolism, Receptors, Vasopressin metabolism
Abstract

It is now accepted that vasopressin, through V 1A /V 1B receptors, centrally regulates cognitive functions such as memory, affiliation, stress, fear and depression. However, the respective roles of these receptor isoforms and their contribution to stress-related pathologies remain uncertain. The development of new therapeutic treatments requires a precise knowledge of the distribution of these receptors within the brain, which has been so far hampered by the lack of selective V 1B markers. In the present study, we have determined the pharmacological properties of three new potent rat V 1B fluorescent ligands and demonstrated that they constitute valuable tools for simultaneous visualization and activation of native V 1B receptors in living rat brain tissue. Thus, d[Leu 4 ,Lys-Alexa 647) 8 ]VP (analogue 3), the compound with the best affinity-selectivity/fluorescence ratio for the V 1B receptor emerged as the most promising. The rat brain regions most concerned by stress such as hippocampus, olfactory bulbs, cortex and amygdala display the highest V 1B fluorescent labelling with analogue 3. In the hippocampus CA 2 , V 1B receptors are located on glutamatergic, not GABAergic neurones, and are absent from astrocytes. Using AVP-EGFP rats, we demonstrate the presence of V 1B autoreceptors on AVP-secreting neurones not only in the hypothalamus, but also sparsely in the hippocampus. Finally, using both electrophysiology and visualization of ERK phosphorylation, we show analogue 3-induced activation of the V 1B receptor in situ. This will help to analyse expression and functionality of V 1B receptors in the brain and contribute to further explore the AVPergic circuitry in normal and pathological conditions., (Copyright © 2017 Elsevier Inc. All rights reserved.)

Published
2018
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