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Your search keyword '"Valérie Drouin-Garraud"' showing total 4 results
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4 results on '"Valérie Drouin-Garraud"'

1. Type I hyperprolinemia: genotype/phenotype correlations

Author

Valérie Drouin-Garraud, Simona Orcesi, Audrey Guilmatre, Caroline Espil-Taris, Lionel Van Maldergem, Luisa Bonafé, Dominique Campion, David Valle, Thierry Frebourg, Vassili Valayannopoulos, Eric Le Galloudec, Patricia Blanchet, Cyril Mignot, Vincent des Portes, Bernard Echenne, Christine Ioos, Claudia Izzi, Hélène Maurey, Gabriella Di Rosa, Solenn Legallic, Jodi D. Hoffman, Alexandra Afenjar, Alice Goldenberg, Gary Steel, Alecia Willis, Agathe Roubertie, Agnès Guët, Génétique médicale et fonctionnelle du cancer et des maladies neuropsychiatriques, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Estonian Genome and Medicine, University of Tartu, McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Department of Medical and Surgical Pediatrics, University Hospital, Department of Genetics, CHU Trousseau [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Laboratoire sur le langage, le cerveau et la cognition (L2C2), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Department of Neuro-Metabolism, CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Regional Hospital, Tufts Medical Center, Università degli Studi di Brescia = University of Brescia (UniBs), Fondation 'Neurological Institute C. Mondino ', Université de Lausanne = University of Lausanne (UNIL), Beauvais Hospital, AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Raymond-Poincaré Hospital, CHU Pitié-Salpêtrière [AP-HP], Hôpital Arnaud de Villeneuve [CHRU Montpellier], Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier), Hôpital Gui de Chauliac [CHU Montpellier], Service de neuropédiatrie, CHU Hôpital, École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Università degli Studi di Brescia [Brescia], Université de Lausanne (UNIL), Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Hôpital Gui de Chauliac, and Université Montpellier 1 (UM1)-Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)

Subjects
Adult, Male, Adolescent, Proline, Mutation, Missense, Biology, medicine.disease_cause, 03 medical and health sciences, 0302 clinical medicine, Proline dehydrogenase, Genotype, Proline Oxidase, Genetics, medicine, Humans, Missense mutation, Allele, Child, Amino Acid Metabolism, Inborn Errors, Alleles, Genetic Association Studies, Genetics (clinical), 030304 developmental biology, 0303 health sciences, Mutation, Proline oxidase, [SCCO.NEUR]Cognitive science/Neuroscience, Haplotype, Infant, Life Sciences, medicine.disease, Molecular biology, 3. Good health, Case-Control Studies, Child, Preschool, Hyperprolinemia, PRODH, type I hyperprolinemia, 22q11, POX enzymatic activity, Female, 030217 neurology & neurosurgery
Abstract

International audience; Type I hyperprolinemia (HPI) is an autosomal recessive disorder associated with cognitive and psychiatric troubles, caused by alterations of the Proline Dehydrogenase gene (PRODH) at 22q11. HPI results from PRODH deletion and/or missense mutations reducing proline oxidase (POX) activity. The goals of this study were first to measure in controls the frequency of PRODH variations described in HPI patients, second to assess the functional effect of PRODH mutations on POX activity and finally to establish genotype/enzymatic activity correlations in a new series of HPI patients. 8/14 variants occurred at polymorphic frequency in 114 controls. POX activity was determined for 6 novel mutations and 2 haplotypes. The c.1331G>A, p.G444D allele has a drastic effect whereas the c.23C>T, p.P8L allele and the c.[56C>A; 172G>A], p.[Q19P; A58T] haplotype result in a moderate decrease in activity. Among the 19 HPI patients, 10 had a predicted residual activity A, p.T275N allele, which has no detrimental effect on activity but whose frequency in controls is only 3%. Our results suggest that PRODH mutations lead to a decreased POX activity or affect other biological parameters causing hyperprolinemia.

Published
2010
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2. Heterogeneity ofNSD1alterations in 116 patients with Sotos syndrome

Author

Céline Bonnet, Valérie Cormier-Daire, Valérie Drouin-Garraud, Thierry Billette de Villemeur, Muriel Holder-Espinasse, Séverine Fehrenbach, Didier Lacombe, Dominique Bonneau, Nicolas Jeanne, Marie-France Portnoï, Joelle Roume, Valérie Malan, Marion Gérard, Christine Coubes, Lydie Burglen, Alexandra Afenjar, Delphine Héron, Clarisse Baumann, Thierry Frebourg, Albert David, and Pascale Saugier-Veber

Subjects
Adult, Male, Adolescent, Biology, Polymerase Chain Reaction, Genetic Heterogeneity, Gene duplication, Genetics, medicine, Humans, Abnormalities, Multiple, Child, Genetics (clinical), Sotos syndrome, Genetic heterogeneity, Point mutation, Infant, Newborn, Intracellular Signaling Peptides and Proteins, Macrocephaly, Infant, Nuclear Proteins, Bone age, Histone-Lysine N-Methyltransferase, Syndrome, medicine.disease, Phenotype, Child, Preschool, Overgrowth syndrome, Histone Methyltransferases, Female, medicine.symptom
Abstract

Sotos syndrome is an overgrowth syndrome characterized by distinctive facial features, learning difficulties, and macrocephaly with frequent pre- and postnatal overgrowth with advanced bone age. Here, we report on our experience in the molecular diagnostic of Sotos syndrome on 116 patients. Using direct sequencing and a quantitative multiplex PCR of short fluorescent fragments (QMPSF)-based assay allowing accurate detection of both total and partial NSD1 deletions, we identified NSD1 abnormalities in 104 patients corresponding to 102 Sotos families (90%). NSD1 point mutations were detected in 80% of the index cases, large deletions removing the NSD1 gene entirely in 14%, and intragenic NSD1 rearrangements in 6%. Among the 69 detected distinct point mutations, 48 were novel. The QMPSF assay detected an exonic duplication and a mosaic partial deletion. QMPSF mapping of the 15 large deletions revealed the heterogeneity of the deletions, which vary in size from 1 to 4.5 Mb. Clinical features of NSD1-positive Sotos patients revealed that the phenotype in patients with nontruncating mutations was less severe that in patients with truncating mutations. This study confirms the heterogeneity of NSD1 alterations in Sotos syndrome and therefore the need to complete sequencing analysis by screening for partial deletions and duplications to ensure an accurate molecular diagnosis of this syndrome.

Published
2007
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3. Missense mutations of conserved glycine residues in fibrillin-1 highlight a potential subtype of cb-EGF-like domains

Author

Aurélie Plancke, Anne-Françoise Roux, Gwenaëlle Collod-Béroud, Dominique Martin-Coignard, Christophe Béroud, David Baux, Mireille Claustres, Patrick Collignon, Nathalie Pallares-Ruiz, Philippe Khau Van Kien, Corinne Baudoin, Valérie Drouin-Garraud, Alain Hovnanian, Nicolas Chassaing, Laboratoire de génétique des maladies rares. Pathologie moleculaire, etudes fonctionnelles et banque de données génétiques (LGMR), IFR3, Université Montpellier 1 (UM1)-Université Montpellier 1 (UM1)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Genetics, Centre de Référence Maladies Sensorielles Génétiques, Hôpital Gui de Chauliac [Montpellier], Service de génétique médicale, CHU Toulouse [Toulouse]-Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse], Département de génétique médicale [Hôpital de la Timone - APHM], Aix Marseille Université (AMU)-Assistance Publique - Hôpitaux de Marseille (APHM)- Hôpital de la Timone [CHU - APHM] (TIMONE)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de génétique [Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), 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), Service de génétique, Centre Hospitalier Le Mans (CH Le Mans), Institut de génétique humaine (IGH), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université Montpellier 1 (UM1)-IFR3, Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Service Génétique Médicale [CHU Toulouse], Institut Fédératif de Biologie (IFB), Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Pôle Biologie [CHU Toulouse], Centre Hospitalier Universitaire de Toulouse (CHU Toulouse), COLLOD-BEROUD, Gwenaëlle, Institut National de la Santé et de la Recherche Médicale (INSERM)- Hôpital de la Timone [CHU - APHM] (TIMONE)-Assistance Publique - Hôpitaux de Marseille (APHM)-Aix Marseille Université (AMU), Hôpital Gui de Chauliac [CHU Montpellier], and Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)-Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)

Subjects
Male, Models, Molecular, Fibrillin-1, medicine.disease_cause, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Marfan Syndrome, Missense mutation, Child, Genetics (clinical), chemistry.chemical_classification, Genetics, Alanine, wwwhgvsorg, 0303 health sciences, Mutation, 030305 genetics & heredity, Microfilament Proteins, Middle Aged, Amino acid, [SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system, Pedigree, Female, Fibrillin, musculoskeletal diseases, Adult, congenital, hereditary, and neonatal diseases and abnormalities, Adolescent, Sequence analysis, Glycine, Mutation, Missense, Biology, [SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics, Fibrillins, 03 medical and health sciences, Young Adult, [SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system, cb-EGF-like domain, medicine, Humans, Fibrillin 1 (FBN1) gene, Gene, 030304 developmental biology, Aged, Epidermal Growth Factor, fibrillinopathies, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Sequence Analysis, DNA, chemistry, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, OFFICIAL JOURNAL, Calcium
Abstract

In six index cases/families referred for Marfan syndrome (MFS) molecular diagnosis, we identified six novel mutations in the FBN1 gene: c.1753G>C (p.Gly585Arg), c.2456G>A (p.Gly819Glu), c.4981G>A (p.Gly1661Arg), c.5339G>A (p.Gly1780Glu), c.6418G>A (p.Gly2140Arg) and c.6419G>A (p.Gly2140Glu). These variants, predicted to result in Glycine substitutions are located at the third position of a 4 amino acids loop-region of calcium-binding Epidermal Growth Factor-like (cb-EGF) fibrillin-1 domains 5, 9, 24, 25 and 32. Familial segregation studies showing cosegregation with MFS manifestations or de novo inheritance in addition to in silico analyses (conservation, 3D modeling) suggest evidence for a crucial role of the respective Glycine positions. Extending these analyses to all Glycine residue at position 3 of this 4 residues loop in fibrillin-1 cb-EGF with the UMD predictor tool and alignment of 2038 available related sequences strongly support a steric strain that only allows Glycine or even Alanine residues for domain structure maintenance and for the fibrillin functions. Our data compared with those of the literature strongly suggest the existence of a cb-EGF domain subtype with implications for related diseases.

Published
2009
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4. Townes-Brocks syndrome: Detection of a SALL1 mutation hot spot and evidence for a position effect in one patient

Author

F.G. Ferraz, Alain Fourmaintraux, Nicole Philip, Rima Slim, Stéphane Blanchard, Françoise Denoyelle, Valérie Drouin-Garraud, Didier Lacombe, Jean-Edmond Toublanc, Jean-Louis Alessandri, Christine Petit, Elisa Calzolari, and Sandrine Marlin

Subjects
Male, Hearing Loss, Sensorineural, Biology, Translocation, Genetic, Frameshift mutation, Anus, Imperforate, Exon, Chromosome 16, medicine, SALL1, Genetics, Townes–Brocks syndrome, Animals, Humans, Abnormalities, Multiple, Ear, External, Frameshift Mutation, Genetics (clinical), DNA Primers, Base Sequence, Chromosome Mapping, Syndrome, medicine.disease, Penetrance, Pedigree, Position effect, Thumb, Codon, Nonsense, Mutation, Female, Haploinsufficiency, Chromosomes, Human, Pair 16, Transcription Factors
Abstract

Townes-Brocks syndrome (TBS) is an autosomal dominant developmental disorder characterized by anal and thumb malformations and by ear anomalies that can affect the three compartments and usually lead to hearing loss. The gene underlying TBS, SALL1, is a human homolog of the Drosophila spalt gene which encodes a transcription factor. A search for SALL1 mutations undertaken in 11 unrelated affected individuals (five familial and six sporadic cases) led to the detection of mutations in nine of them. One nonsense and six different novel frameshift mutations, all located in the second exon, were identified. Together with the previously reported mutations [Kohlhase et al., 1999], they establish that TBS results from haploinsufficiency. The finding of de novo mutations in the sporadic cases is consistent with the proposed complete penetrance of the disease. Moreover, the occurrence of the same 826C>T transition in a CG dimer, in three sporadic cases from the present series and three sporadic cases from the other series [Kohlhase et al., 1999] (i.e., six of the eight mutations identified in sporadic cases), reveals the existence of a mutation hotspot. Six different SALL1 polymorphisms were identified in the course of the present study, three of which are clustered in a particular region of the gene that encodes a stretch of serine residues. Finally, the chromosome 16 breakpoint of a t(5;16)(p15.3;q12.1) translocation carried by a TBS-affected individual was mapped at least 180 kb telomeric to SALL1, thus indicating that a position effect underlies the disease in this individual.

Published
1999
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