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2. Feedback-Driven Assembly of the Axon Initial Segment

Author

Fréal, Amélie, Rai, Dipti, Tas, Roderick P., Pan, Xingxiu, Katrukha, Eugene A., van de Willige, Dieudonnée, Stucchi, Riccardo, Aher, Amol, Yang, Chao, Altelaar, A.F. Maarten, Vocking, Karin, Post, Jan Andries, Harterink, Martin, Kapitein, Lukas C., Akhmanova, Anna, and Hoogenraad, Casper C.

Published
2019
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5. The core PCP protein Prickle2 regulates axon number and AIS maturation by binding to AnkG and modulating microtubule bundling

Author

Ana Dorrego-Rivas, Jerome Ezan, Maïté M. Moreau, Sonia Poirault-Chassac, Nathalie Aubailly, Julie De Neve, Camille Blanchard, Francis Castets, Amélie Fréal, Arne Battefeld, Nathalie Sans, Mireille Montcouquiol, Amsterdam Neuroscience - Cellular & Molecular Mechanisms, Functional Genomics, Institut de Biologie du Développement de Marseille (IBDM), and Aix Marseille Université (AMU)-Collège de France (CdF (institution))-Centre National de la Recherche Scientifique (CNRS)

Subjects
Multidisciplinary, [SDV]Life Sciences [q-bio]
Abstract

International audience; Core planar cell polarity (PCP) genes, which are involved in various neurodevelopmental disorders such as neural tube closure, epilepsy, and autism spectrum disorder, have poorly defined molecular signatures in neurons, mostly synapse-centric. Here, we show that the core PCP protein Prickle-like protein 2 (Prickle2) controls neuronal polarity and is a previously unidentified member of the axonal initial segment (AIS) proteome. We found that Prickle2 is present and colocalizes with AnkG480, the AIS master organizer, in the earliest stages of axonal specification and AIS formation. Furthermore, by binding to and regulating AnkG480, Prickle2 modulates its ability to bundle microtubules, a crucial mechanism for establishing neuronal polarity and AIS formation. Prickle2 depletion alters cytoskeleton organization, and Prickle2 levels determine both axon number and AIS maturation. Last, early Prickle2 depletion produces impaired action potential firing.

Published
2022
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6. Sodium channel endocytosis drives axon initial segment plasticity

Author

Fréal, Amélie, Jamann, Nora, Ten Bos, Jolijn, Jansen, Jacqueline, Petersen, Naomi, Ligthart, Thijmen, Hoogenraad, Casper C, Kole, Maarten H P, Fréal, Amélie, Jamann, Nora, Ten Bos, Jolijn, Jansen, Jacqueline, Petersen, Naomi, Ligthart, Thijmen, Hoogenraad, Casper C, and Kole, Maarten H P

Abstract

Activity-dependent plasticity of the axon initial segment (AIS) endows neurons with the ability to adapt action potential output to changes in network activity. Action potential initiation at the AIS highly depends on the clustering of voltage-gated sodium channels, but the molecular mechanisms regulating their plasticity remain largely unknown. Here, we developed genetic tools to label endogenous sodium channels and their scaffolding protein, to reveal their nanoscale organization and longitudinally image AIS plasticity in hippocampal neurons in slices and primary cultures. We find that N-methyl-d-aspartate receptor activation causes both long-term synaptic depression and rapid internalization of AIS sodium channels within minutes. The clathrin-mediated endocytosis of sodium channels at the distal AIS increases the threshold for action potential generation. These data reveal a fundamental mechanism for rapid activity-dependent AIS reorganization and suggests that plasticity of intrinsic excitability shares conserved features with synaptic plasticity.

Published
2023

7. Sodium channel endocytosis drives axon initial segment plasticity

Author

Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Fréal, Amélie, Jamann, Nora, Ten Bos, Jolijn, Jansen, Jacqueline, Petersen, Naomi, Ligthart, Thijmen, Hoogenraad, Casper C, Kole, Maarten H P, Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Fréal, Amélie, Jamann, Nora, Ten Bos, Jolijn, Jansen, Jacqueline, Petersen, Naomi, Ligthart, Thijmen, Hoogenraad, Casper C, and Kole, Maarten H P

Published
2023

8. Sodium channel endocytosis drives axon initial segment plasticity

Author

Amélie Fréal, Nora Jamann, Jolijn Ten Bos, Jacqueline Jansen, Naomi Petersen, Thijmen Ligthart, Casper C. Hoogenraad, and Maarten H. P. Kole

Abstract

Activity-dependent plasticity of the axon initial segment (AIS) endows neurons with the ability to adapt action potential output to changes in network activity. Action potential initiation at the AIS highly depends on the clustering of voltage-gated sodium channels, however the molecular mechanisms regulating their plasticity remain largely unknown. Here, we used novel genetic tools to endogenously label sodium channels and their scaffolding protein, to reveal their nanoscale organization and longitudinally image AIS plasticity in hippocampal neurons, in slices and primary cultures. We find that induction of NMDA receptor-mediated long-term synaptic depression is linked to a rapid and local endocytosis of sodium channels from the distal AIS. These data reveal a novel fundamental mechanism for rapid activity-dependent AIS reorganization sharing conserved features with synaptic plasticity.

Published
2022
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10. The core PCP protein Prickle2 regulates axon number and AIS maturation by binding to AnkG and modulating microtubule bundling

Author

Dorrego-Rivas, Ana, primary, Ezan, Jerome, additional, Moreau, Maïté M., additional, Poirault-Chassac, Sonia, additional, Aubailly, Nathalie, additional, De Neve, Julie, additional, Blanchard, Camille, additional, Castets, Francis, additional, Fréal, Amélie, additional, Battefeld, Arne, additional, Sans, Nathalie, additional, and Montcouquiol, Mireille, additional

Published
2022
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11. Recent thermoresistive material evolutions at LYNRED for improving uncooled microbolometer products thermal sensitivity

Author

Guillaumont, Marc, primary, Altazin, Stéphane, additional, Cardoso, Alexi, additional, Tinnes, Sébastien, additional, Pistre, Claire, additional, Durand, Alain, additional, Dariel, Aurélien, additional, Rossini, Fabio, additional, Laurent, Clémence, additional, Fréal, Christine, additional, Mandran, Gérard, additional, Bellon, Christian, additional, Cortial, Sébastien, additional, Cueff, Matthieu, additional, Pautet, Christophe, additional, Boudou, Nicolas, additional, Gays, Sarah, additional, Zucchi, Xavier, additional, Pelenc, Denis, additional, Yon, Jean-Jacques, additional, Rabaud, Wilfried, additional, Goudon, Valérie, additional, Vialle, Claire, additional, Pocas, Stéphane, additional, Brellier, Delphine, additional, Hida, Rachid, additional, Jullien, Tony, additional, Mehrez, Zouhir, additional, Vermande, Elisa, additional, Schembri, Antoine, additional, and Brianceau, Pierre, additional

Published
2022
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12. Recent thermoresistive material evolutions at LYNRED for improving uncooled microbolometer products thermal sensitivity

Author

Marc Guillaumont, Stéphane Altazin, Alexi Cardoso, Sébastien Tinnes, Claire Pistre, Alain Durand, Aurélien Dariel, Fabio Rossini, Clémence Laurent, Christine Fréal, Gérard Mandran, Christian Bellon, Sébastien Cortial, Matthieu Cueff, Christophe Pautet, Nicolas Boudou, Sarah Gays, Xavier Zucchi, Denis Pelenc, Jean-Jacques Yon, Wilfried Rabaud, Valérie Goudon, Claire Vialle, Stéphane Pocas, Delphine Brellier, Rachid Hida, Tony Jullien, Zouhir Mehrez, Elisa Vermande, Antoine Schembri, and Pierre Brianceau

Published
2022
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14. TRIM46 Organizes Microtubule Fasciculation in the Axon Initial Segment

Author

Harterink, Martin, Vocking, Karin, Pan, Xingxiu, Soriano Jerez, Eva M., Slenders, Lotte, Fréal, Amélie, Tas, Roderick P., Van De Wetering, Willine J., Timmer, Karina, Motshagen, Jasmijn, Van Beuningen, Sam F.b., Kapitein, Lukas C., Geerts, Willie J.c., Post, Jan A., Hoogenraad, Casper C., Sub Cell Biology, Sub Cryo - EM, Celbiologie, Cryo-EM, Sub Cell Biology, Sub Cryo - EM, Celbiologie, and Cryo-EM

Subjects
0301 basic medicine, Male, Biology, Hippocampal formation, Hippocampus, Microtubules, Fasciculation, Tripartite Motif Proteins, 03 medical and health sciences, 0302 clinical medicine, Microtubule, Taverne, axon intial segment (AIS), medicine, Animals, Axon, Axon Fasciculation, Axon Initial Segment, Cells, Cultured, Cytoskeleton, Research Articles, Neurons, General Neuroscience, Cell Polarity, Correlative light and electron microscopy (CLEM), Axon initial segment, Transport protein, Cell biology, Rats, Somatodendritic compartment, 030104 developmental biology, medicine.anatomical_structure, nervous system, Female, TRIM46, Neuron, medicine.symptom, 030217 neurology & neurosurgery, microtubule
Abstract

Selective cargo transport into axons and dendrites over the microtubule network is essential for neuron polarization. The axon initial segment (AIS) separates the axon from the somatodendritic compartment and controls the microtubule-dependent transport into the axon. Interestingly, the AIS has a characteristic microtubule organization; it contains bundles of closely spaced microtubules with electron dense cross-bridges, referred to as microtubule fascicles. The microtubule binding protein TRIM46 localizes to the AIS and when overexpressed in non-neuronal cells forms microtubule arrays that closely resemble AIS fascicles in neurons. However, the precise role of TRIM46 in microtubule fasciculation in neurons has not been studied. Here we developed a novel correlative light and electron microscopy approach to study AIS microtubule organization. We show that in cultured rat hippocampal neurons of both sexes, TRIM46 levels steadily increase at the AIS during early neuronal differentiation and at the same time closely spaced microtubules form, whereas the fasciculated microtubules appear at later developmental stages. Moreover, we localized TRIM46 to the electron dense cross-bridges and show that depletion of TRIM46 causes loss of cross-bridges and increased microtubule spacing. These data indicate that TRIM46 has an essential role in organizing microtubule fascicles in the AIS. SIGNIFICANCE STATEMENT The axon initial segment (AIS) is a specialized region at the proximal axon where the action potential is initiated. In addition the AIS separates the axon from the somatodendritic compartment, where it controls protein transport to establish and maintain neuron polarity. Cargo vesicles destined for the axon recognize specialized microtubule tracks that enter the AIS. Interestingly the microtubules entering the AIS form crosslinked bundles, called microtubule fascicules. Recently we found that the microtubule-binding protein TRIM46 localizes to the AIS, where it may organize the AIS microtubules. In the present study we developed a novel correlative light and electron microscopy approach to study the AIS microtubules during neuron development and identified an essential role for TRIM46 in microtubule fasciculation.

Published
2019

15. Feedback-Driven Mechanisms between Microtubules and the Endoplasmic Reticulum Instruct Neuronal Polarity

Author

Farías, Ginny G., Fréal, Amélie, Tortosa, Elena, Stucchi, Riccardo, Pan, Xingxiu, Portegies, Sybren, Will, Lena, Altelaar, Maarten, Hoogenraad, Casper C., Celbiologie, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Celbiologie, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, and Afd Biomol.Mass Spect. and Proteomics

Subjects
0301 basic medicine, MT-driven motors, neurons, Kinesins, axon specification, Endoplasmic Reticulum, Hippocampus, Microtubules, Mice, 0302 clinical medicine, Taverne, Chlorocebus aethiops, Axon, Cells, Cultured, Cytoskeleton, Cerebral Cortex, Neurons, Chemistry, General Neuroscience, Cell Polarity, ER retention, microtubule dynamics, ER cisternae, Cell biology, endoplasmic reticulum, ER tubules, Tubule, medicine.anatomical_structure, COS Cells, Microtubule-Associated Proteins, neuronal polarity, Neurite, Neuroscience(all), Feedback, microtubules, 03 medical and health sciences, Microtubule, medicine, Neurites, Animals, ER-shaping proteins, Endoplasmic reticulum, Dyneins, Axons, Rats, 030104 developmental biology, nervous system, Neuronal polarity, 030217 neurology & neurosurgery, Entire cell
Abstract

Establishment of neuronal polarity depends on local microtubule (MT) reorganization. The endoplasmic reticulum (ER) consists of cisternae and tubules and, like MTs, forms an extensive network throughout the entire cell. How the two networks interact and control neuronal development is an outstanding question. Here we show that the interplay between MTs and the ER is essential for neuronal polarity. ER tubules localize within the axon, whereas ER cisternae are retained in the somatodendritic domain. MTs are essential for axonal ER tubule stabilization, and, reciprocally, the ER is required for stabilizing and organizing axonal MTs. Recruitment of ER tubules into one minor neurite initiates axon formation, whereas ER retention in the perinuclear area or disruption of ER tubules prevent neuronal polarization. The ER-shaping protein P180, present in axonal ER tubules, controls axon specification by regulating local MT remodeling. We propose a model in which feedback-driven regulation between the ER and MTs instructs neuronal polarity. Farías et al. report that the localization of the endoplasmic reticulum (ER) in the axon is controlled by the interaction between ER-shaping proteins and the microtubule cytoskeleton. Local ER and microtubule crosstalk promotes ER tubule-microtubule stabilization and drives neuronal polarity.

Published
2018

16. Motor axon navigation relies on Fidgetin-like 1–driven microtubule plus end dynamics

Author

Jean-Christophe Larcher, Leticia Peris, Christian Delphin, Stéphanie De Gois, Coralie Fassier, Amélie Fréal, Laïla Gasmi, Daniel Ten Martin, Jamilé Hazan, Christophe Bosc, Philippe Mailly, Corinne Houart, Annie Andrieux, Fatiha Nothias, Céline Revenu, Susanne Bolte, Sylvie Schneider-Maunoury, Monica Tambalo, Développement et dégénérescence des neurones moteurs spinaux = Development and Degeneration of Spinal Motor neurons in the zebrafish (NPS-08), Neuroscience Paris Seine (NPS), Centre National de la Recherche Scientifique (CNRS)-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)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-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)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC), Department of Genetics, Universitat de València (UV), Mécanismes d'expression cellulaire des effecteurs humoraux, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des maladies psychiatriques = Pathophysiology of Psychiatric Disorders (NPS-07), [GIN] Grenoble Institut des Neurosciences, Physiopathologie des Maladies du Système Nerveux Central, 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), Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC), Organisation Fonctionnelle du Cytosquelette, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR27, Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Regionalisation du cerveau des vertébrés - Organogenèse précoce chez la souris et maladies génétiques associées, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), King‘s College London, Laboratoire de Biologie du Développement (LBD), 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)-Centre National de la Recherche Scientifique (CNRS), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Neurosciences Paris Seine (NPS), 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)-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)-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)-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), [GIN] Grenoble Institut des Neurosciences (GIN), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), 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), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-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), 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)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-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)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-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)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Biologie Paris Seine (IBPS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Growth Cones, Biology, Microtubules, Article, Polymerization, 03 medical and health sciences, 0302 clinical medicine, Microtubule, Cell cortex, medicine, Animals, Humans, Protein Isoforms, Axon, Growth cone, Cytoskeleton, Zebrafish, Research Articles, ComputingMilieux_MISCELLANEOUS, Adenosine Triphosphatases, Motor Neurons, Nuclear Proteins, Cell Biology, biology.organism_classification, Axons, Microtubule plus-end, Cell biology, Axon Guidance, 030104 developmental biology, medicine.anatomical_structure, Spinal Cord, Gene Knockdown Techniques, Larva, Axon guidance, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Microtubule-Associated Proteins, 030217 neurology & neurosurgery, Locomotion
Abstract

Fassier et al. identify Fidgetin-like 1 (Fignl1) as a key growth cone (GC)-enriched microtubule (MT)-associated protein in motor circuit wiring. They show that Fignl1 modulates motor GC morphology and steering behavior by down-regulating EB binding at MT plus ends and promoting MT depolymerization beneath the cell cortex., During neural circuit assembly, extrinsic signals are integrated into changes in growth cone (GC) cytoskeleton underlying axon guidance decisions. Microtubules (MTs) were shown to play an instructive role in GC steering. However, the numerous actors required for MT remodeling during axon navigation and their precise mode of action are far from being deciphered. Using loss- and gain-of-function analyses during zebrafish development, we identify in this study the meiotic clade adenosine triphosphatase Fidgetin-like 1 (Fignl1) as a key GC-enriched MT-interacting protein in motor circuit wiring and larval locomotion. We show that Fignl1 controls GC morphology and behavior at intermediate targets by regulating MT plus end dynamics and growth directionality. We further reveal that alternative translation of Fignl1 transcript is a sophisticated mechanism modulating MT dynamics: a full-length isoform regulates MT plus end–tracking protein binding at plus ends, whereas shorter isoforms promote their depolymerization beneath the cell cortex. Our study thus pinpoints Fignl1 as a multifaceted key player in MT remodeling underlying motor circuit connectivity.

Published
2018
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17. Feedback-Driven Assembly of the Axon Initial Segment

Author

Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Celbiologie, Fréal, Amélie, Rai, Dipti, Tas, Roderick P, Pan, Xingxiu, Katrukha, Eugene A, van de Willige, Dieudonnée, Stucchi, Riccardo, Aher, Amol, Yang, Chao, Altelaar, A F Maarten, Vocking, Karin, Post, Jan Andries, Harterink, Martin, Kapitein, Lukas C, Akhmanova, Anna, Hoogenraad, Casper C, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Celbiologie, Fréal, Amélie, Rai, Dipti, Tas, Roderick P, Pan, Xingxiu, Katrukha, Eugene A, van de Willige, Dieudonnée, Stucchi, Riccardo, Aher, Amol, Yang, Chao, Altelaar, A F Maarten, Vocking, Karin, Post, Jan Andries, Harterink, Martin, Kapitein, Lukas C, Akhmanova, Anna, and Hoogenraad, Casper C

Published
2019

18. TRIM46 Organizes Microtubule Fasciculation in the Axon Initial Segment

Author

Sub Cell Biology, Sub Cryo - EM, Celbiologie, Cryo-EM, Harterink, Martin, Vocking, Karin, Pan, Xingxiu, Soriano Jerez, Eva M., Slenders, Lotte, Fréal, Amélie, Tas, Roderick P., Van De Wetering, Willine J., Timmer, Karina, Motshagen, Jasmijn, Van Beuningen, Sam F.b., Kapitein, Lukas C., Geerts, Willie J.c., Post, Jan A., Hoogenraad, Casper C., Sub Cell Biology, Sub Cryo - EM, Celbiologie, Cryo-EM, Harterink, Martin, Vocking, Karin, Pan, Xingxiu, Soriano Jerez, Eva M., Slenders, Lotte, Fréal, Amélie, Tas, Roderick P., Van De Wetering, Willine J., Timmer, Karina, Motshagen, Jasmijn, Van Beuningen, Sam F.b., Kapitein, Lukas C., Geerts, Willie J.c., Post, Jan A., and Hoogenraad, Casper C.

Published
2019

19. Feedback-Driven Mechanisms between Microtubules and the Endoplasmic Reticulum Instruct Neuronal Polarity

Author

Celbiologie, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Farías, Ginny G., Fréal, Amélie, Tortosa, Elena, Stucchi, Riccardo, Pan, Xingxiu, Portegies, Sybren, Will, Lena, Altelaar, Maarten, Hoogenraad, Casper C., Celbiologie, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Biomolecular Mass Spectrometry and Proteomics, Farías, Ginny G., Fréal, Amélie, Tortosa, Elena, Stucchi, Riccardo, Pan, Xingxiu, Portegies, Sybren, Will, Lena, Altelaar, Maarten, and Hoogenraad, Casper C.

Published
2019

20. Feedback-Driven Mechanisms between Microtubules and the Endoplasmic Reticulum Instruct Neuronal Polarity

Author

Cell Biology, Neurobiology and Biophysics, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Farías, Ginny G., Fréal, Amélie, Tortosa, Elena, Stucchi, Riccardo, Pan, Xingxiu, Portegies, Sybren, Will, Lena, Altelaar, Maarten, Hoogenraad, Casper C., Cell Biology, Neurobiology and Biophysics, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Farías, Ginny G., Fréal, Amélie, Tortosa, Elena, Stucchi, Riccardo, Pan, Xingxiu, Portegies, Sybren, Will, Lena, Altelaar, Maarten, and Hoogenraad, Casper C.

Published
2019

21. Motor axon navigation relies on Fidgetin-like 1–driven microtubule plus end dynamics

Author

Fassier, Coralie, primary, Fréal, Amélie, additional, Gasmi, Laïla, additional, Delphin, Christian, additional, Ten Martin, Daniel, additional, De Gois, Stéphanie, additional, Tambalo, Monica, additional, Bosc, Christophe, additional, Mailly, Philippe, additional, Revenu, Céline, additional, Peris, Leticia, additional, Bolte, Susanne, additional, Schneider-Maunoury, Sylvie, additional, Houart, Corinne, additional, Nothias, Fatiha, additional, Larcher, Jean-Christophe, additional, Andrieux, Annie, additional, and Hazan, Jamilé, additional

Published
2018
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23. Cooperative Interactions between 480 kDa Ankyrin-G and EB Proteins Assemble the Axon Initial Segment

Author

Amélie Fréal, Barbara Le Bras, Coralie Fassier, Stéphanie De Gois, Erika Bullier, Casper C. Hoogenraad, François Couraud, Jamilé Hazan, Physiopathologie des maladies psychiatriques = Pathophysiology of Psychiatric Disorders (NPS-07), Neurosciences Paris Seine (NPS), 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)-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)-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)-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), Fondation pour la Recherche Medicale, Agence Nationale pour la Recherche (HYPER-MND) [ANR-2010-BLAN-1429-01], Netherlands Organization for Scientific Research (NWO-ALW-VICI), Neuroscience Paris Seine (NPS), 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)-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)-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)-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), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-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)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-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)-Centre National de la Recherche Scientifique (CNRS), Celbiologie, and Sub Cell Biology

Subjects
0301 basic medicine, Scaffold protein, cell migration, complementary DNA, Video microscopy, animal cell, Ankyrin-G, axon initial segment, Western blotting, Rats, Sprague-Dawley, Mice, immunocytochemistry, video microscopy, Chlorocebus aethiops, Cell polarity, Ankyrin, Axon, Cells, Cultured, Neurons, chemistry.chemical_classification, General Neuroscience, adult, Neuronal polarity, article, Cell Polarity, Articles, Axon initial segment, End-binding protein, Cell biology, medicine.anatomical_structure, female, priority journal, COS Cells, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], fluorescence, Microtubule-Associated Proteins, Protein Binding, microtubule, Ankyrins, end-binding protein, neuronal polarity, Microtubule-associated protein, phenotype, animal experiment, fluorescence recovery after photobleaching, rabbit, embryo, Microtubule, Biology, animal tissue, 03 medical and health sciences, ankyrin, medicine, Animals, controlled study, mouse, nonhuman, ankyrin-G, animal model, embryo development, Axons, Rats, 030104 developmental biology, chemistry, nervous system, genetic transfection
Abstract

The axon initial segment (AIS) is required for generating action potentials and maintaining neuronal polarity. Significant progress has been made in deciphering the basic building blocks composing the AIS, but the underlying mechanisms required for AIS formation remains unclear. The scaffolding protein ankyrin-G is the master-organizer of the AIS. Microtubules and their interactors, particularly end-binding proteins (EBs), have emerged as potential key players in AIS formation. Here, we show that the longest isoform of ankyrin-G (480AnkG) selectively associates with EBs via its specific tail domain and that this interaction is crucial for AIS formation and neuronal polarity in cultured rodent hippocampal neurons. EBs are essential for 480AnkG localization and stabilization at the AIS, whereas 480AnkG is required for the specific accumulation of EBs in the proximal axon. Our findings thus provide a conceptual framework for understanding how the cooperative relationship between 480AnkG and EBs induces the assembly of microtubule-AIS structures in the proximal axon.SIGNIFICANCE STATEMENTNeuronal polarity is crucial for the proper function of neurons. The assembly of the axon initial segment (AIS), which is the hallmark of early neuronal polarization, relies on the longest 480 kDa ankyrin-G isoform. The microtubule cytoskeleton and its interacting proteins were suggested to be early key players in the process of AIS formation. In this study, we show that the crosstalk between 480 kDa ankyrin-G and the microtubule plus-end tracking proteins, EBs, at the proximal axon is decisive for AIS assembly and neuronal polarity. Our work thus provides insight into the functional mechanisms used by 480 kDa ankyrin-G to drive the AIS formation and thereby to establish neuronal polarity.

Published
2016
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24. In vivo assembly of the axon initial segment in motor neurons

Author

Masayuki Komada, François Couraud, Barbara Le Bras, Antonny Czarnecki, Amélie Fréal, Pascal Legendre, Peter J. Brophy, Marc Davenne, Erika Bullier, Développement de l'organisation spinale = Development of the spinal cord organization (NPS-10), Neuroscience Paris Seine (NPS), 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)-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)-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)-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), Association Francaise contre les Myopathies (AFM), Fondation pour le Recherche Medicale (FRM), Centre National de la Recherche Scientifique (CNRS)-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)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-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)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC), Neurosciences Paris Seine (NPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Biologie Paris Seine (IBPS), and 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)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Ankyrins, Histology, Neuroscience(all), Population, Action Potentials, Biology, Development, Axonogenesis, Mice, 03 medical and health sciences, 0302 clinical medicine, AnkyrinG, medicine, Animals, Ankyrin, Spectrin, Nerve Growth Factors, Axon, education, 030304 developmental biology, Mice, Knockout, Motor Neurons, chemistry.chemical_classification, 0303 health sciences, education.field_of_study, General Neuroscience, Sodium channel, Axon initial segment, Axons, Nerve growth factor, medicine.anatomical_structure, nervous system, chemistry, Original Article, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Anatomy, Cell Adhesion Molecules, Neuroscience, 030217 neurology & neurosurgery
Abstract

The axon initial segment (AIS) is responsible for both the modulation of action potentials and the maintenance of neuronal polarity. Yet, the molecular mechanisms controlling its assembly are incompletely understood. Our study in single electroporated motor neurons in mouse embryos revealed that AnkyrinG (AnkG), the AIS master organizer, is undetectable in bipolar migrating motor neurons, but is already expressed at the beginning of axonogenesis at E9.5 and initially distributed homogeneously along the entire growing axon. Then, from E11.5, a stage when AnkG is already apposed to the membrane, as observed by electron microscopy, the protein progressively becomes restricted to the proximal axon. Analysis on the global motor neurons population indicated that Neurofascin follows an identical spatio-temporal distribution, whereas sodium channels and β4-spectrin only appear along AnkG+ segments at E11.5. Early patch-clamp recordings of individual motor neurons indicated that at E12.5 these nascent AISs are already able to generate spikes. Using knock-out mice, we demonstrated that neither β4-spectrin nor Neurofascin control the distal-to-proximal restriction of AnkG. Electronic supplementary material The online version of this article (doi:10.1007/s00429-013-0578-7) contains supplementary material, which is available to authorized users.

Published
2014
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25. Cooperative Interactions between 480 kDa Ankyrin-G and EB proteins assemble the axon initial segment

Author

Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., Couraud, François, Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., and Couraud, François

Abstract

The axon initial segment (AIS) is required for generating action potentials and maintaining neuronal polarity. Significant progress has been made in deciphering the basic building blocks composing the AIS, but the underlying mechanisms required for AIS formation remains unclear. The scaffolding protein ankyrin-G is the master-organizer of the AIS. Microtubules and their interactors, particularly end-binding proteins (EBs), have emerged as potential key players in AIS formation. Here, we show that the longest isoform of ankyrin-G (480AnkG) selectively associates with EBs via its specific tail domain and that this interaction is crucial for AIS formation and neuronal polarity in cultured rodent hippocampal neurons. EBs are essential for 480AnkG localization and stabilization at the AIS, whereas 480AnkG is required for the specific accumulation of EBs in the proximal axon. Our findings thus provide a conceptual framework for understanding how the cooperative relationship between 480AnkG and EBs induces the assembly of microtubule-AIS structures in the proximal axon. Significance Statement Neuronal polarity is crucial for the proper function of neurons. The assembly of the axon initial segment (AIS), which is the hallmark of early neuronal polarization, relies on the longest 480 kDa ankyrin-G isoform. The microtubule cytoskeleton and its interacting proteins were suggested to be early key players in the process of AIS formation. In this study, we show that the crosstalk between 480 kDa ankyrin-G and the microtubule plus-end tracking proteins, EBs, at the proximal axon is decisive for AIS assembly and neuronal polarity. Our work thus provides insight into the functional mechanisms used by 480 kDa ankyrin-G to drive the AIS formation and thereby to establish neuronal polarity.

Published
2016

26. Cooperative Interactions between 480 kDa Ankyrin-G and EB proteins assemble the axon initial segment

Author

Celbiologie, Sub Cell Biology, Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., Couraud, François, Celbiologie, Sub Cell Biology, Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., and Couraud, François

Published
2016

27. Cooperative Interactions between 480 kDa Ankyrin-G and EB proteins assemble the axon initial segment

Author

Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., Couraud, François, Cell Biology, Neurobiology and Biophysics, Sub Cell Biology, Fréal, Amélie, Fassier, Coralie, Le Bras, Barbara, Bullier, Erika, de Gois, Stéphanie, Hazan, Jamilé, Hoogenraad, Casper C., and Couraud, François

Published
2016

31. Recent thermoresistive material evolutions at LYNRED for improving uncooled microbolometer products thermal sensitivity.

Author

Guillaumont, Marc, Altazin, Stéphane, Cardoso, Alexi, Tinnes, Sébastien, Pistre, Claire, Durand, Alain, Dariel, Aurélien, Rossini, Fabio, Laurent, Clémence, Fréal, Christine, Mandran, Gérard, Bellon, Christian, Cortial, Sébastien, Cueff, Matthieu, Pautet, Christophe, Boudou, Nicolas, Gays, Sarah, Zucchi, Xavier, Pelenc, Denis, and Yon, Jean-Jacques

Published
2022
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32. Recent thermoresistive material evolutions at LYNRED for improving uncooled microbolometer products thermal sensitivity

Author

Andresen, Bjørn F., Fulop, Gabor F., Zheng, Lucy, Kimata, Masafumi, Miller, John Lester, Kim, Young-Ho, Guillaumont, Marc, Altazin, Stéphane, Cardoso, Alexi, Tinnes, Sébastien, Pistre, Claire, Durand, Alain, Dariel, Aurélien, Rossini, Fabio, Laurent, Clémence, Fréal, Christine, Mandran, Gérard, Bellon, Christian, Cortial, Sébastien, Cueff, Matthieu, Pautet, Christophe, Boudou, Nicolas, Gays, Sarah, Zucchi, Xavier, Pelenc, Denis, Yon, Jean-Jacques, Rabaud, Wilfried, Goudon, Valérie, Vialle, Claire, Pocas, Stéphane, Brellier, Delphine, Hida, Rachid, Jullien, Tony, Mehrez, Zouhir, Vermande, Elisa, Schembri, Antoine, and Brianceau, Pierre

Published
2022
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33. La saisie directe des informations lors d'un don de sang en collecte mobile

Author

J. Ahr, J.C. Diot, and C. Fréal

Subjects
Identification (information), Blood donor, Multimedia, Computer science, Hematology, General Medicine, Line (text file), computer.software_genre, computer, Past history
Abstract

Direct data storage, in the presence of the donor, ensures a realistic reliability and erases any deferred interpretation of the essential information for a good donation identification. Computers can help relieve this restraint. Indeed the evolution of microcomputers (increased capacity and power, decreased weight and volume, and good performance in any use makes them more and more accurate. Associated use of barcodes and microcomputers gives a nonmanual non-human line of words: donor-donation-analysis-blood products-patient. We found, working that way, the following advantages: Information secured. No deferred inputs. Instart comparison of the information on the donor's past history. Accurate donation-donor connection. Such a system represents one more step towards a continuous line of treatment from Donor to Patient in regard of Blood Transfusion Safety.

Published
1987
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36. [The Lewis blood group is more frequently nonexpressed in psychiatry than in the general population]

Author

G, Pascalis, J, Ahr, J L, Rincent, E, Rincent, and C, Fréal

Subjects
Adult, Male, Lewis Blood Group Antigens, Gene Frequency, Neurotic Disorders, Psychotic Disorders, Mental Disorders, Blood Group Antigens, Humans, Blood Donors, Female, France
Abstract

The Lewis-negative blood group seems to occur more frequently in psychiatry than in the overall population. The Lewis group is not genetically determined at birth as Lewis-positive or negative; the latter occurs significantly more often among 219 "overall" psychiatric patients than in the overall population: 47% instead of 10%. As a first approximation, the absence of transition from its negativity to positivity seems to constitute a favoring factor for the subsequent clinical development of a psychiatric syndrome, without allowing to predict its nature or severity. For the other blood groups, the genetic determination of which is irreversible, the same sample shows the same repartition as in the overall population.

Published
1983

37. Le Nord / texte de Jacques Fréal ; illustrations de Mathieu Ravaux

Author

Ravaux, Mathieu. Illustrateur, Fréal, Jacques. Auteur du texte, Ravaux, Mathieu. Illustrateur, and Fréal, Jacques. Auteur du texte

Abstract

Collection : Témoins de la vie paysanne ; 1, Collection : Témoins de la vie paysanne ; 1, Contient une table des matières, Avec mode texte, Catalogues d'exposition

Published
1980

42. [Prevention of Rh disease by anti-D plasma. A 2-year study]

Author

G, Potron, C, Quéreux, and C, Fréal

Subjects
Clinical Trials as Topic, Rh-Hr Blood-Group System, Immune Sera, Immunization, Passive, Delivery, Obstetric, Fetomaternal Transfusion, ABO Blood-Group System, Abortion, Spontaneous, Erythroblastosis, Fetal, Parity, Isoantibodies, Pregnancy, Blood Group Incompatibility, Antibody Formation, Methods, Humans, Female, Follow-Up Studies
Published
1973

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