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10 results on '"Nédelec, B."'

1. METSTOR: A GIS to look for potential CO2 storage zones in France

Author

Bonijoly, D., Ha-Duong, M., Leynet, A., Bonneville, A., Broseta, D., Fradet, A., Le Gallo, Y., Munier, G., Lagny, C., Lagneau, V., Auzende, A.-L., Berthiaud, J., Bialkowski, A., Bossie-Codréanu, D., Brosse, E., Bureau, G., Campos, A.-S., Fillacier, S., Nédelec, B., Pokryszka, Z., Rambourg, D., Rigollet, C., Roux, P., and Saysset, S.

Published
2009
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4. Is the modification of the 13q32.1 regulatory landscape the cause of congenital microcoria?

Author

Fares-Taie, L., Nédelec, B., David, Pierre, Gerber, S., Crippa, S., Passet, Bruno, Vilotte, Jean Luc, Chassaing, N., Kaplan, J., Kostic, C., Calvas, Patrick, Rozet, J. M., Imagine - Institut des maladies génétiques (IMAGINE - U1163), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Ophthalmology, Université de Lausanne (UNIL), Génétique Animale et Biologie Intégrative (GABI), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, CHU Toulouse [Toulouse], and Hôpital Universitaire de Toulouse

Subjects
[SDV.GEN]Life Sciences [q-bio]/Genetics, [SDV.GEN.GA]Life Sciences [q-bio]/Genetics/Animal genetics, [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

National audience

Published
2018

5. D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile

Author

Valleix, S., Guglielmo Verona, Jourde-Chiche, N., Nédelec, B., Mangione, P. P., Bridoux, F., Mangé, A., Dogan, A., Goujon, J. -M, Lhomme, M., Dauteuille, C., Chabert, M., Porcari, R., Waudby, C. A., Relini, A., Talmud, P. J., Kovrov, O., Olivecrona, G., Stoppini, M., Christodoulou, J., Hawkins, P. N., Grateau, G., Delpech, M., Kontush, A., Gillmore, J. D., Kalopissis, A. D., Bellotti, V., Laboratoire de Biochimie et Génétique Moléculaire, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5), Bocconi University, Bocconi University [Milan, Italy], Vascular research center of Marseille (VRCM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Physiopathologie de l'Endothelium, Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Hôpital de la Conception [CHU - APHM] (LA CONCEPTION), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Università degli Studi di Pavia = University of Pavia (UNIPV), Service de Néphrologie CHU Poitiers, Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Mayo Clinic, Service d’Anapathomopathologie, Centre hospitalier universitaire de Poitiers (CHU Poitiers), CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Unité de Recherche sur les Maladies Cardiovasculaires, du Métabolisme et de la Nutrition = Research Unit on Cardiovascular and Metabolic Diseases (ICAN), Université Pierre et Marie Curie - Paris 6 (UPMC)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU), Sorbonne Université (SU), University College of London [London] (UCL), University of London [London], Università degli studi di Genova = University of Genoa (UniGe), Centre For Cardiovascular Genetics, Royal Free and UCL Medical School, Umeå University, Dept Mol Med, Genetic Metabolic Disorders Research Unit, Kids Research Institute-Westmead Hospital [Sydney], Discipline of Paediatrics & Child Health, The University of Sydney, Discipline of Genetic Medicine, Sydney Medical School-The University of Sydney, Western Sydney Genetics Program, Westmead Hospital [Sydney], CHU Tenon [AP-HP], CHU Saint-Antoine [AP-HP], UCL, Ctr Amyloidosis & Acute Phase Prot, University College of London [London] (UCL)-University ofLondon, l’Association Franc ̧aise contre l’Amylose, the Institut Nationalde la Sante ́et de la Recherche Me ́dicale (INSERM) and the French National ReferenceCenter for AL amyloidosis, the UK NHS Research and Development funds, theUniversity College London Amyloidosis Research Fund and grants from the UK MedicalResearch Council (MR/K000187/1), the Rosetrees Trust/Royal Free Charity PhDprogramme (M427), the British Heart Foundation (PG08/008), the Wellcome TrustInvestigator Award (097806/Z/11/Z), the Cariplo Foundation Projects (2014–0700 and2013-0964), the Telethon Grant GG14127, the INBB (National Institute of Biostructuresand Biosystems), the Italian Ministry of Health and the Italian Ministry of University andResearch (Projects FIRB RBFR109EOS), Laboratoire commun de biologie et génétique moléculaires [CHU Saint-Antoine], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Saint-Antoine [AP-HP], DIGNAT-GEORGE, Françoise, Assistance publique - Hôpitaux de Paris (AP-HP)-Université Paris Descartes - Paris 5 ( UPD5 ), Vascular research center of Marseille ( VRCM ), Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Hôpital de la Conception [CHU - APHM] ( LA CONCEPTION ), Université Montpellier 1 ( UM1 ), Centre hospitalier universitaire de Poitiers ( CHU Poitiers ), CHU Pitié-Salpêtrière [APHP], Unité de Recherche sur les Maladies Cardiovasculaires, du Métabolisme et de la Nutrition = Institute of cardiometabolism and nutrition ( ICAN ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Assistance publique - Hôpitaux de Paris (AP-HP)-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -CHU Pitié-Salpêtrière [APHP], University of Genoa ( UNIGE ), University of Pavia, Children's Hospital at Westmead-Kids Research Institute, The University of Sydney [Sydney], Sydney Medical School-The University of Sydney [Sydney], Children's Hospital at Westmead, University College of London [London] ( UCL ) -University ofLondon, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Unité de Recherche sur les Maladies Cardiovasculaires, du Métabolisme et de la Nutrition = Institute of cardiometabolism and nutrition (ICAN), Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), University of Genoa (UNIGE), and Westmead Hospital [Sydney]-Kids Research Institute

Subjects
Adult, Male, Hyperlipoproteinemias, Science, [SDV]Life Sciences [q-bio], Molecular Sequence Data, Mutation, Missense, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy), Lipoproteins, VLDL, bcs, Article, LIPASE ACTIVITY, OF-FUNCTION MUTATIONS, Humans, Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci), Aged, Aged, 80 and over, Apolipoprotein C-III, CELLULAR CHOLESTEROL EFFLUX, [ SDV ] Life Sciences [q-bio], Base Sequence, Amyloidosis, Middle Aged, LIPID-BINDING, ANTIOXIDATIVE ACTIVITY, Pedigree, [SDV] Life Sciences [q-bio], HDL PARTICLES, A-I, ELEVATED OXIDATIVE STRESS, Cardiovascular Diseases, Female, lipids (amino acids, peptides, and proteins), France, Lipoproteins, HDL, DENSE LDL, TRIGLYCERIDE-RICH LIPOPROTEINS
Abstract

Apolipoprotein C-III deficiency provides cardiovascular protection, but apolipoprotein C-III is not known to be associated with human amyloidosis. Here we report a form of amyloidosis characterized by renal insufficiency caused by a new apolipoprotein C-III variant, D25V. Despite their uremic state, the D25V-carriers exhibit low triglyceride (TG) and apolipoprotein C-III levels, and low very-low-density lipoprotein (VLDL)/high high-density lipoprotein (HDL) profile. Amyloid fibrils comprise the D25V-variant only, showing that wild-type apolipoprotein C-III does not contribute to amyloid deposition in vivo. The mutation profoundly impacts helical structure stability of D25V-variant, which is remarkably fibrillogenic under physiological conditions in vitro producing typical amyloid fibrils in its lipid-free form. D25V apolipoprotein C-III is a new human amyloidogenic protein and the first conferring cardioprotection even in the unfavourable context of renal failure, extending the evidence for an important cardiovascular protective role of apolipoprotein C-III deficiency. Thus, fibrate therapy, which reduces hepatic APOC3 transcription, may delay amyloid deposition in affected patients., Decrease in Apolipoprotein C-III (ApoC-III) yields a cardioprotective lipoprotein profile. Here, Valleix et al. reveal a novel ApoC-III variant conferring low plasma ApoC-III concentration and cardioprotection despite renal insufficiency, and, unexpectedly, causing dominant hereditary systemic amyloidosis due to its fibrillogenic nature.

Published
2016

7. METSTOR: A GIS to look for potential CO2 storage zones in France.

Author

Bonijoly, D., Ha-Duong, M., Leynet, A., Bonneville, A., Broseta, D., Fradet, A., Le Gallo, Y., Munier, G., Lagny, C., Lagneau, V., Auzende, A.-L., Berthiaud, J., Bialkowski, A., Bossie-Codréanu, D., Brosse, E., Bureau, G., Campos, A.-S., Fillacier, S., Nédelec, B., and Pokryszka, Z.

Subjects
GEOLOGICAL carbon sequestration, GEOGRAPHIC information systems, METHODOLOGY, RISK assessment, PROTOTYPES
Abstract

Abstract: The METSTOR project offers a methodology to look for potentially interesting CO2 storage areas in France at the initial stage, before the “site selection” step. Our tool, embodied in a Geographic Information System, is based on an interactive map of CO2 storage capacities. Other relevant information layers are included. The geographic layers are complemented with a series of online technical notices. It seems to be the first open online GIS that offers policy makers, businesses and the public at large an integrated access to that necessary information. Our prototype, limited mainly to the Paris Basin, is released online at www.metstor.fr. [Copyright &y& Elsevier]

Published
2009
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8. D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile.

Author

Valleix S, Verona G, Jourde-Chiche N, Nédelec B, Mangione PP, Bridoux F, Mangé A, Dogan A, Goujon JM, Lhomme M, Dauteuille C, Chabert M, Porcari R, Waudby CA, Relini A, Talmud PJ, Kovrov O, Olivecrona G, Stoppini M, Christodoulou J, Hawkins PN, Grateau G, Delpech M, Kontush A, Gillmore JD, Kalopissis AD, and Bellotti V

Subjects
Adult, Aged, Aged, 80 and over, Apolipoprotein C-III chemistry, Apolipoprotein C-III genetics, Base Sequence, Female, France, Humans, Hyperlipoproteinemias genetics, Hyperlipoproteinemias metabolism, Male, Middle Aged, Molecular Sequence Data, Pedigree, Amyloidosis genetics, Amyloidosis metabolism, Apolipoprotein C-III metabolism, Cardiovascular Diseases prevention & control, Lipoproteins, HDL metabolism, Lipoproteins, VLDL metabolism, Mutation, Missense
Abstract

Apolipoprotein C-III deficiency provides cardiovascular protection, but apolipoprotein C-III is not known to be associated with human amyloidosis. Here we report a form of amyloidosis characterized by renal insufficiency caused by a new apolipoprotein C-III variant, D25V. Despite their uremic state, the D25V-carriers exhibit low triglyceride (TG) and apolipoprotein C-III levels, and low very-low-density lipoprotein (VLDL)/high high-density lipoprotein (HDL) profile. Amyloid fibrils comprise the D25V-variant only, showing that wild-type apolipoprotein C-III does not contribute to amyloid deposition in vivo. The mutation profoundly impacts helical structure stability of D25V-variant, which is remarkably fibrillogenic under physiological conditions in vitro producing typical amyloid fibrils in its lipid-free form. D25V apolipoprotein C-III is a new human amyloidogenic protein and the first conferring cardioprotection even in the unfavourable context of renal failure, extending the evidence for an important cardiovascular protective role of apolipoprotein C-III deficiency. Thus, fibrate therapy, which reduces hepatic APOC3 transcription, may delay amyloid deposition in affected patients.

Published
2016
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9. MEFV-Gene analysis in armenian patients with Familial Mediterranean fever: diagnostic value and unfavorable renal prognosis of the M694V homozygous genotype-genetic and therapeutic implications.

Author

Cazeneuve C, Sarkisian T, Pêcheux C, Dervichian M, Nédelec B, Reinert P, Ayvazyan A, Kouyoumdjian JC, Ajrapetyan H, Delpech M, Goossens M, Dodé C, Grateau G, and Amselem S

Subjects
Adolescent, Adult, Armenia, Child, Child, Preschool, Colchicine pharmacology, Cytoskeletal Proteins, Familial Mediterranean Fever ethnology, Female, Genetic Testing, Genotype, Gout Suppressants pharmacology, Humans, Kidney Diseases diagnosis, Male, Middle Aged, Pedigree, Phenotype, Polymorphism, Genetic, Pyrin, Familial Mediterranean Fever diagnosis, Familial Mediterranean Fever genetics, Proteins genetics
Abstract

Familial Mediterranean fever (FMF) is a recessively inherited disorder that is common in patients of Armenian ancestry. To date, its diagnosis, which can be made only retrospectively, is one of exclusion, based entirely on nonspecific clinical signs that result from serosal inflammation and that may lead to unnecessary surgery. Renal amyloidosis, prevented by colchicine, is the most severe complication of FMF, a disorder associated with mutations in the MEFV gene. To evaluate the diagnostic and prognostic value of MEFV-gene analysis, we investigated 90 Armenian FMF patients from 77 unrelated families that were not selected through genetic-linkage analysis. Eight mutations, one of which (R408Q) is new, were found to account for 93% of the 163 independent FMF alleles, with both FMF alleles identified in 89% of the patients. In several instances, family studies provided molecular evidence for pseudodominant transmission and incomplete penetrance of the disease phenotype. The M694V homozygous genotype was found to be associated with a higher prevalence of renal amyloidosis and arthritis, compared with other genotypes (P=.0002 and P=.006, respectively). The demonstration of both the diagnostic and prognostic value of MEFV analysis and particular modes of inheritance should lead to new ways for management of FMF-including genetic counseling and therapeutic decisions in affected families.

Published
1999
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10. Non-founder mutations in the MEFV gene establish this gene as the cause of familial Mediterranean fever (FMF).

Author

Bernot A, da Silva C, Petit JL, Cruaud C, Caloustian C, Castet V, Ahmed-Arab M, Dross C, Dupont M, Cattan D, Smaoui N, Dodé C, Pêcheux C, Nédelec B, Medaxian J, Rozenbaum M, Rosner I, Delpech M, Grateau G, Demaille J, Weissenbach J, and Touitou I

Subjects
Africa, Northern ethnology, Amino Acid Sequence, Cytoskeletal Proteins, Exons genetics, Haplotypes, Humans, Molecular Sequence Data, Pyrin, Sequence Analysis, Familial Mediterranean Fever genetics, Mutation, Proteins genetics
Abstract

Familial Mediterranean fever (FMF) is an autosomal recessive disorder characterized by recurring attacks of fever and serositis. It affects primarily North African Jews, Armenians, Turks and Arabs, in which a founder effect has been demonstrated. The marenostrin-pyrin-encoding gene has been proposed as a candidate gene for the disease ( MEFV ), on the basis of the identification of putative mutations clustered in exon 10 (M680V, M694I, M694V and V726A), each segregating with one ancestral haplotype. In a search for additional MEFV mutations in 120 apparently non-founder FMF chromosomes, we observed eight novel mutations in exon 2 (E148Q, E167D and T267I), exon 5 (F479L) and exon 10 (I692del K695R, A744S and R761H). Except for E148Q and K695R, all mutations were found in a single chromosome. Mutation E148Q was found in all ethnic groups studied and in association with a novel ancestral haplotype in non-Ashkenazi Jews (S2). Altogether, these new findings definitively establish the marenostrin/pyrin-encoding gene as the MEFV locus.

Published
1998
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