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6 results on '"Christine Bole-Feysot"'

1. Biallelic PPA2 Mutations Cause Sudden Unexpected Cardiac Arrest in Infancy

Author

Anne Guimier, Richard Redon, Agnès Delahodde, Christopher T. Gordon, Philippe Charron, Myriam Oufadem, Agnès Rötig, Alain Dautant, Patrick Nitschke, Stanislas Lyonnet, Damien Bonnet, Sylvie Di Filippo, Cécile Masson, Patrice Bouvagnet, Loïc de Pontual, Béatrice Kugener, François Godard, Nigel G. Laing, Christine Bole-Feysot, Vincent Probst, Jeanne Amiel, Christelle Vasnier, Stéphane Dauger, Gianina Ravenscroft, Caroline Rambaud, Cheryl Longman, Jean-Paul di Rago, Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Center for Medical Research, University of Western Australia and the Harry Perkins Institute for Medical Research WA 6009, Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Stress Abiotiques et Différenciation des Végétaux Cultivés (SADV), Institut National de la Recherche Agronomique (INRA)-Université de Lille, Sciences et Technologies, Institut Charles Viollette (ICV) - EA 7394 (ICV), Université d'Artois (UA)-Institut National de la Recherche Agronomique (INRA)-Université du Littoral Côte d'Opale (ULCO)-Institut Supérieur d'Agriculture-Université de Lille, Plate Forme Paris Descartes de Bioinformatique (BIP-D), Université Paris Descartes - Paris 5 (UPD5), Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Nutrition, inflammation et dysfonctionnement de l'axe intestin-cerveau (ADEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Neuroprotection du Cerveau en Développement / Promoting Research Oriented Towards Early Cns Therapies (PROTECT), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), West of Scotland Regional Genetics Service, Physiologie integrée du système d'éveil, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-IFR19-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Sommeil Pédiatrique (Hôpital Mère-Enfant), Hospices Civils de Lyon (HCL), CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Laboratoire Cardiogénétique, CHU de Lyon HCL-GH Est-Hôpital Louis Pradel, Hôpital Louis Pradel [CHU - HCL], Hospices Civils de Lyon (HCL)-Hospices Civils de Lyon (HCL), Service de Cardiologie Pédiatrique, Hospices Civils de Lyon (HCL)-Hôpital Louis Pradel [CHU - HCL], unité de recherche de l'institut du thorax UMR1087 UMR6291 (ITX), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), CHU Pitié-Salpêtrière [AP-HP], Fonctions et dysfonctions de la mitochondrie (FDMITO), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Unité de recherche de l'institut du thorax (ITX-lab), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Lille, Sciences et Technologies-Institut National de la Recherche Agronomique (INRA), Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de la Recherche Agronomique (INRA)-Université d'Artois (UA)-Institut Supérieur d'Agriculture, Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), CHU Pitié-Salpêtrière [APHP], Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, 0301 basic medicine, Heterozygote, Saccharomyces cerevisiae Proteins, [SDV]Life Sciences [q-bio], Mitochondrial disease, Mutant, Mutation, Missense, Saccharomyces cerevisiae, Mitochondrion, Biology, Compound heterozygosity, Mitochondrial Proteins, 03 medical and health sciences, 0302 clinical medicine, Report, Genetics, medicine, Humans, Missense mutation, Exome, Genetics(clinical), Alleles, Genetics (clinical), Membrane Potential, Mitochondrial, Genes, Essential, Microbial Viability, Genetic Complementation Test, Infant, Sudden cardiac arrest, Proton Pumps, medicine.disease, Mitochondria, Diphosphates, Inorganic Pyrophosphatase, Death, Sudden, Cardiac, 030104 developmental biology, Essential gene, Mutation, Female, medicine.symptom, Gene Deletion, 030217 neurology & neurosurgery, Orthologous Gene
Abstract

International audience; Sudden unexpected death in infancy occurs in apparently healthy infants and remains largely unexplained despite thorough investigation. The vast majority of cases are sporadic. Here we report seven individuals from three families affected by sudden and unexpected cardiac arrest between 4 and 20 months of age. Whole-exome sequencing revealed compound heterozygous missense mutations in PPA2 in affected infants of each family. PPA2 encodes the mitochondrial pyrophosphatase, which hydrolyzes inorganic pyrophosphate into two phosphates. This is an essential activity for many biosynthetic reactions and for energy metabolism of the cell. We show that deletion of the orthologous gene in yeast (ppa2Δ) compromises cell viability due to the loss of mitochondria. Expression of wild-type human PPA2, but not PPA2 containing the mutations identified in affected individuals, preserves mitochondrial function in ppa2Δ yeast. Using a regulatable (doxycycline-repressible) gene expression system, we found that the pathogenic PPA2 mutations rapidly inactivate the mitochondrial energy transducing system and prevent the maintenance of a sufficient electrical potential across the inner membrane, which explains the subsequent disappearance of mitochondria from the mutant yeast cells. Altogether these data demonstrate that PPA2 is an essential gene in yeast and that biallelic mutations in PPA2 cause a mitochondrial disease leading to sudden cardiac arrest in infants.

Published
2016

2. XYLT1 Mutations in Desbuquois Dysplasia Type 2

Author

Beyhan Tüysüz, Céline Huber, Valérie Cormier-Daire, Christine Bole-Feysot, Catherine Bui, Jules G. Leroy, Geert Mortier, Yasemin Alanay, Arnold Munnich, Patrick Nitschke, Imagine - Institut des maladies génétiques (IMAGINE - U1163), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Genetics Unit, Department of Pediatrics Hacettepe, University School of Medicine, Ankara, Department of Medical Genetics, Ghent University [Belgium] (UGENT), Plateforme de bioinformatique, Université Paris Descartes - Paris 5 (UPD5), Acibadem University Dspace, Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Ankara University School of Medicine [Turkey], and Universiteit Gent = Ghent University [Belgium] (UGENT)

Subjects
Male, Dwarfism, medicine.disease_cause, Craniofacial Abnormalities, Consanguinity, 0302 clinical medicine, Exome, Genetics(clinical), Child, ComputingMilieux_MISCELLANEOUS, Genetics (clinical), Genetics, 0303 health sciences, Mutation, Homozygote, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Female, Proteoglycans, medicine.symptom, Adult, Joint Instability, DNA, Complementary, Adolescent, Xylosyltransferase, Biology, Short stature, Article, Bone and Bones, 03 medical and health sciences, medicine, Humans, Genetic Predisposition to Disease, Pentosyltransferases, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 030304 developmental biology, Ossification, Ossification, Heterotopic, Sequence Analysis, DNA, Fibroblasts, XYLT1, medicine.disease, Molecular biology, Polydactyly, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, Human medicine, 030217 neurology & neurosurgery, Microsatellite Repeats
Abstract

Desbuquois dysplasia (DBQD) is a severe condition characterized by short stature, joint laxity, and advanced carpal ossification. Based on the presence of additional hand anomalies, we have previously distinguished DBQD type 1 and identified CANT1 (calcium activated nucleotidase 1) mutations as responsible for DBQD type 1. We report here the identification of five distinct homozygous xylosyltransferase 1 (XYLT1) mutations in seven DBQD type 2 subjects from six consanguineous families. Among the five mutations, four were expected to result in loss of function and a drastic reduction of XYLT1 cDNA level was demonstrated in two cultured individual fibroblasts. Because xylosyltransferase 1 (XT-I) catalyzes the very first step in proteoglycan (PG) biosynthesis, we further demonstrated in the two individual fibroblasts a significant reduction of cellular PG content. Our findings of XYLT1 mutations in DBQD type 2 further support a common physiological basis involving PG synthesis in the multiple dislocation group of disorders. This observation sheds light on the key role of the XT-I during the ossification process.

Published
2014
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3. Exome Sequencing Identifies INPPL1 Mutations as a Cause of Opsismodysplasia

Author

Christine Bole-Feysot, Deborah Bartholdi, Heloísa G. dos Santos, Martine Le Merrer, Stavit A. Shalev, Valérie Cormier-Daire, Denise P. Cavalcanti, Joelle Roume, Eissa Faqeih, Zvi Borochowitz, Anne-Lise Delezoide, Andrea Superti-Furga, Amandine Frigo, Patrick Nitschke, Arnold Munnich, Céline Huber, University of Zurich, and Cormier-Daire, Valérie

Subjects
2716 Genetics (clinical), 10039 Institute of Medical Genetics, 610 Medicine & health, Biology, Compound heterozygosity, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, 1311 Genetics, medicine, Genetics, Missense mutation, Genetics(clinical), Exome, Genetics (clinical), Exome sequencing, 030304 developmental biology, 0303 health sciences, Mutation, Ossification, medicine.disease, Stop codon, 030220 oncology & carcinogenesis, 570 Life sciences, biology, Opsismodysplasia, medicine.symptom
Abstract

Opsismodysplasia (OPS) is a severe autosomal-recessive chondrodysplasia characterized by pre- and postnatal micromelia with extremely short hands and feet. The main radiological features are severe platyspondyly, squared metacarpals, delayed skeletal ossification, and metaphyseal cupping. In order to identify mutations causing OPS, a total of 16 cases (7 terminated pregnancies and 9 postnatal cases) from 10 unrelated families were included in this study. We performed exome sequencing in three cases from three unrelated families and only one gene was found to harbor mutations in all three cases: inositol polyphosphate phosphatase-like 1 (INPPL1). Screening INPPL1 in the remaining cases identified a total of 12 distinct INPPL1 mutations in the 10 families, present at the homozygote state in 7 consanguinous families and at the compound heterozygote state in the 3 remaining families. Most mutations (6/12) resulted in premature stop codons, 2/12 were splice site, and 4/12 were missense mutations located in the catalytic domain, 5-phosphatase. INPPL1 belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family, a family of signal-modulating enzymes that govern a plethora of cellular functions by regulating the levels of specific phosphoinositides. Our finding of INPPL1 mutations in OPS, a severe spondylodysplastic dysplasia with major growth plate disorganization, supports a key and specific role of this enzyme in endochondral ossification.

Published
2013
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4. TCTN3 Mutations Cause Mohr-Majewski Syndrome

Author

Colin A. Johnson, Valérie Cormier-Daire, Maryse Bonnière, Christel Thauvin-Robinet, Soumaya Mougou-Zerelli, Annick Toutain, Sophie Saunier, Stanislas Lyonnet, Laurence Loeuillet, Bettina Bessières, Sophie Thomas, Christine Bole-Feysot, Marine Legendre, Marie-Anne Barthez, Yves Ville, Tania Attié-Bitach, Caroline Alby, Katarzyna Szymanska, Frédérique Jossic, Patrick Nitschke, Albert David, Dominique Gaillard, M. T. Yacoubi, Michel Vekemans, Férechté Encha-Razavi, and Arnold Munnich

Subjects
Adolescent, Foot Deformities, Congenital, Molecular Sequence Data, Ciliopathies, Joubert syndrome, Young Adult, Fetus, Report, Cerebellum, GLI3, medicine, Genetics, Humans, Exome, Hedgehog Proteins, Genetics(clinical), Sonic hedgehog, Child, Genetics (clinical), Adaptor Proteins, Signal Transducing, Cystic kidney, Base Sequence, biology, Homozygote, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Ciliary transition zone, Sequence Analysis, DNA, Orofaciodigital Syndromes, medicine.disease, Cleft Palate, Ciliopathy, Phenotype, Mutation, biology.protein, Apoptosis Regulatory Proteins, Hand Deformities, Congenital, Signal Transduction
Abstract

Orofaciodigital syndromes (OFDSs) consist of a group of heterogeneous disorders characterized by abnormalities in the oral cavity, face, and digits and associated phenotypic abnormalities that lead to the delineation of 13 OFDS subtypes. Here, by a combined approach of homozygozity mapping and exome ciliary sequencing, we identified truncating TCTN3 mutations as the cause of an extreme form of OFD associated with bone dysplasia, tibial defect, cystic kidneys, and brain anomalies (OFD IV, Mohr-Majewski syndrome). Analysis of 184 individuals with various ciliopathies (OFD, Meckel, Joubert, and short rib polydactyly syndromes) led us to identify four additional truncating TCTN3 mutations in unrelated fetal cases with overlapping Meckel and OFD IV syndromes and one homozygous missense mutation in a family with Joubert syndrome. By exploring roles of TCTN3 in human ciliary related functions, we found that TCTN3 is necessary for transduction of the sonic hedgehog (SHH) signaling pathway, as revealed by abnormal processing of GLI3 in patient cells. These results are consistent with the suggested role of its murine ortholog, which forms a complex at the ciliary transition zone with TCTN1 and TCTN2, both of which are also implicated in the transduction of SHH signaling. Overall, our data show the involvement of the transition zone protein TCTN3 in the regulation of the key SHH signaling pathway and that its disruption causes a severe form of ciliopathy, combining features of Meckel and OFD IV syndromes.

Published
2012
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5. Mainzer-Saldino Syndrome Is a Ciliopathy Caused by IFT140 Mutations

Author

Isabelle Perrault, Albane A. Bizet, Sylvie Gerber, Sophie Saunier, Philip L. Beales, Jamal Goumid, Christine Pietrement, Emilie Filhol, Eduardo Silva, Nora Shannon, Olivier Roche, Nathalie Delphin, Christine Bole-Feysot, Machteld M. Oud, Sylvain Hanein, Corinne Antignac, Jean-Michel Rozet, Mohammed Zahrate, Valérie Cormier-Daire, Karine Bigot, Heleen H. Arts, Felicity Collins, Clarisse Baumann, Martine Le Merrer, Patrick Nitschke, Josseline Kaplan, Christophe Orssaud, Véronique Baudouin, Arnold Munnich, and Mustafa A. Salih

Subjects
Male, Adolescent, Cerebellar Ataxia, Biology, Senior–Løken syndrome, medicine.disease_cause, symbols.namesake, Intraflagellar transport, Report, Ciliogenesis, Retinitis pigmentosa, Genetics, medicine, Humans, Genetics(clinical), Child, Alleles, Genetics (clinical), Sanger sequencing, Mutation, Fibroblasts, medicine.disease, Pedigree, Transport protein, Protein Transport, Ciliopathy, Child, Preschool, symbols, Genetics and epigenetic pathways of disease Renal disorder [NCMLS 6], Female, sense organs, Carrier Proteins, Retinitis Pigmentosa
Abstract

Item does not contain fulltext Mainzer-Saldino syndrome (MSS) is a rare disorder characterized by phalangeal cone-shaped epiphyses, chronic renal failure, and early-onset, severe retinal dystrophy. Through a combination of ciliome resequencing and Sanger sequencing, we identified IFT140 mutations in six MSS families and in a family with the clinically overlapping Jeune syndrome. IFT140 is one of the six currently known components of the intraflagellar transport complex A (IFT-A) that regulates retrograde protein transport in ciliated cells. Ciliary abundance and localization of anterograde IFTs were altered in fibroblasts of affected individuals, a result that supports the pivotal role of IFT140 in proper development and function of ciliated cells.

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6. Combination of Linkage Mapping and Microarray-Expression Analysis Identifies NF-κB Signaling Defect as a Cause of Autosomal-Recessive Mental Retardation

Author

Astrid Carioux, Asma Smahi, Marlène Rio, Patrick Nitschke, Arnold Munnich, Christine Bole-Feysot, Nathalie Boddaert, Laurence Colleaux, Philippe Guigue, Orianne Philippe, Jean-Marc Plaza, Florence Molinari, Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement (Inserm U781), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plateforme de génomique [SFR Necker], Structure Fédérative de Recherche Necker (SFR Necker - UMS 3633 / US24), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme Bioinformatique [SFR Necker] (BIP-D), Plateforme de Génomique [Paris] (Fondation Imagine), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Plateforme de bioinformatique (UNIV Paris Descartes), Université Paris Descartes - Paris 5 (UPD5), This study was supported by the Centre National de la Recherche Scientifique (CNRS), the Agence Nationale de la Recherche (ANR), the Fondation Lejeune, and the Ministère de la Recherche et de l’Enseignement Supérieur., COLLEAUX, Laurence, and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité)

Subjects
Male, Genetic Linkage, MESH: NF-kappa B, IκB kinase, MESH: Base Sequence, MESH: Magnetic Resonance Imaging, Exon, 0302 clinical medicine, Gene expression, Genetics(clinical), Genetics (clinical), Oligonucleotide Array Sequence Analysis, Genetics, Regulation of gene expression, 0303 health sciences, NF-kappa B, Brain, Magnetic Resonance Imaging, MESH: Gene Expression Regulation, I-kappa B Kinase, Pedigree, Female, Adolescent, MESH: Pedigree, Molecular Sequence Data, MESH: Genetic Linkage, Genes, Recessive, [SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics, Biology, MESH: Intellectual Disability, 03 medical and health sciences, MESH: Brain, MESH: Gene Expression Profiling, Gene mapping, Report, Intellectual Disability, Humans, MESH: I-kappa B Kinase, Gene, MESH: Genes, Recessive, 030304 developmental biology, MESH: Adolescent, MESH: Humans, MESH: Molecular Sequence Data, Base Sequence, Tumor Necrosis Factor-alpha, Gene Expression Profiling, I-Kappa-B Kinase, MESH: Male, Gene expression profiling, Gene Expression Regulation, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, MESH: Tumor Necrosis Factor-alpha, MESH: Oligonucleotide Array Sequence Analysis, MESH: Female, 030217 neurology & neurosurgery
Abstract

International audience; Autosomal-recessive inheritance accounts for nearly 25% of nonsyndromic mental retardation (MR), but the extreme heterogeneity of such conditions markedly hampers gene identification. Combining autozygosity mapping and RNA expression profiling in a consanguineous Tunisian family of three MR children with mild microcephaly and white-matter abnormalities identified the TRAPPC9 gene, which encodes a NF-kappaB-inducing kinase (NIK) and IkappaB kinase complex beta (IKK-beta) binding protein, as a likely candidate. Sequencing analysis revealed a nonsense variant (c.1708C>T [p.R570X]) within exon 9 of this gene that is responsible for an undetectable level of TRAPPC9 protein in patient skin fibroblasts. Moreover, TNF-alpha stimulation assays showed a defect in IkBalpha degradation, suggesting impaired NF-kappaB signaling in patient cells. This study provides evidence of an NF-kappaB signaling defect in isolated MR.

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