69 results on '"Rötig, Agnes"'
Search Results
52. Unusual presentation of Kearns-Sayre syndrome in early childhood
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Simaan, Eliane M, primary, Mikati, Mohamad A, additional, Touma, Elias H, additional, and Rötig, Agnes, additional
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- 1999
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53. Neonatal and delayed-onset liver involvement in disorders of oxidative phosphorylation
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Cormier-Daire, Valérie, primary, Chretien, Dominique, additional, Rustin, Pierre, additional, Rötig, Agnes, additional, Dubuisson, Claire, additional, Jacquemin, Emmanuel, additional, Hadchouel, Michelle, additional, Bernard, Olivier, additional, and Munnich, Arnold, additional
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- 1997
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54. Hepatic mitochondrial DNA deletion in alcoholics: Association with microvesicular steatosis
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Fromenty, Bernard, primary, Grimbert, Sylvie, additional, Mansouri, Abdellah, additional, Beaugrand, Michel, additional, Erlinger, Serge, additional, Rötig, Agnes, additional, and Pessayre, Dominique, additional
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- 1995
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55. The measurement of the rotenone-sensitive NADH cytochrome c reductase activity in mitochondria isolated from minute amount of human skeletal muscle
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Chretien, Dominique, primary, Bourgeron, Thomas, additional, Rötig, Agnes, additional, Munnich, Anrold, additional, and Rustin, Pierre, additional
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- 1990
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56. Sengers syndrome: six novel AGK mutations in seven new families and review of the phenotypic and mutational spectrum of 29 patients
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Haghighi, Alireza, Haack, Tobias B, Atiq, Mehnaz, Mottaghi, Hassan, Haghighi-Kakhki, Hamidreza, Bashir, Rani A, Ahting, Uwe, Feichtinger, René G, Mayr, Johannes A, Rötig, Agnès, Lebre, Anne-Sophie, Klopstock, Thomas, Dworschak, Andrea, Pulido, Nathan, Saeed, Mahmood A, Saleh-Gohari, Nasrollah, Holzerova, Eliska, Chinnery, Patrick F, Taylor, Robert W, and Prokisch, Holger
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Sengers syndrome ,AGK ,Acylglycerol Kinase ,Mutation ,Genotype-Phenotype Correlation - Abstract
Background: Sengers syndrome is an autosomal recessive condition characterized by congenital cataract, hypertrophic cardiomyopathy, skeletal myopathy and lactic acidosis. Mutations in the acylglycerol kinase (AGK) gene have been recently described as the cause of Sengers syndrome in nine families. Methods: We investigated the clinical and molecular features of Sengers syndrome in seven new families; five families with the severe and two with the milder form. Results: Sequence analysis of AGK revealed compound heterozygous or homozygous predicted loss-of-function mutations in all affected individuals. A total of eight different disease alleles were identified, of which six were novel, homozygous c.523_524delAT (p.Ile175Tyrfs*2), c.424-1G > A (splice site), c.409C > T (p.Arg137*) and c.877 + 3G > T (splice site), and compound heterozygous c.871C > T (p.Gln291*) and c.1035dup (p.Ile346Tyrfs*39). All patients displayed perinatal or early-onset cardiomyopathy and cataract, clinical features pathognomonic for Sengers syndrome. Other common findings included blood lactic acidosis and tachydyspnoea while nystagmus, eosinophilia and cervical meningocele were documented in only either one or two cases. Deficiency of the adenine nucleotide translocator was found in heart and skeletal muscle biopsies from two patients associated with respiratory chain complex I deficiency. In contrast to previous findings, mitochondrial DNA content was normal in both tissues. Conclusion: We compare our findings to those in 21 previously reported AGK mutation-positive Sengers patients, confirming that Sengers syndrome is a clinically recognisable disorder of mitochondrial energy metabolism.
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- 2014
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57. Additional file 5: of Clinical, biochemical and genetic spectrum of 70 patients with ACAD9 deficiency: is riboflavin supplementation effective?
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Repp, Birgit, Mastantuono, Elisa, Alston, Charlotte, Schiff, Manuel, Haack, Tobias, Rötig, Agnes, Ardissone, Anna, Lombès, Anne, Catarino, Claudia, Diodato, Daria, Schottmann, Gudrun, Poulton, Joanna, Burlina, Alberto, Jonckheere, An, Munnich, Arnold, Rolinski, Boris, Ghezzi, Daniele, Rokicki, Dariusz, Wellesley, Diana, Martinelli, Diego, Wenhong, Ding, Lamantea, Eleonora, Ostergaard, Elsebet, Pronicka, Ewa, Pierre, Germaine, Smeets, Hubert, Wittig, Ilka, Scurr, Ingrid, Irenaeus De Coo, Moroni, Isabella, Joél Smet, Mayr, Johannes, Lifang Dai, Meirleir, Linda De, Schuelke, Markus, Zeviani, Massimo, Morscher, Raphael, McFarland, Robert, Seneca, Sara, Klopstock, Thomas, Meitinger, Thomas, Wieland, Thomas, Strom, Tim, Herberg, Ulrike, Ahting, Uwe, Sperl, Wolfgang, Marie-Cecile Nassogne, Ling, Han, Fang, Fang, Freisinger, Peter, Coster, Rudy Van, Strecker, Valentina, Taylor, Robert, Häberle, Johannes, Vockley, Jerry, Prokisch, Holger, and Wortmann, Saskia
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3. Good health - Abstract
Figure S1. Representative picture of Complex I assembly in fibroblasts of individual 1 (A, upper panels) Two-dimensional BN/SDS-PAGE separation and quantification of fluorescent-labelled mitochondrial complexes from 10 mg patient (left) and control fibroblasts (right) are shown. (A, lower panels) show silver stained 2 D gels. (B) Quantified Supercomplexes in 2D gels from control and patient fibroblast with and without bezafibrate treatment for 72 h. (C) Panoramaplots of 2D gels with assignment of signals used for quantification of complexes. Assignment of complexes: O, OGDC, oxoglutarate dehydrogenase complex; V, complex V or ATP synthase; III, complex III or cytochrome c reductase; IV, complex IV or cytochrome c oxidase; S, supercomplexes composed of respiratory chain complexes I, III, and IV. 2-D gels were scanned side by side for direct comparison and are shown as pseudocolors. (pdf). (PDF 1109 kb)
58. Additional file 5: of Clinical, biochemical and genetic spectrum of 70 patients with ACAD9 deficiency: is riboflavin supplementation effective?
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Repp, Birgit, Mastantuono, Elisa, Alston, Charlotte, Schiff, Manuel, Haack, Tobias, Rötig, Agnes, Ardissone, Anna, Lombès, Anne, Catarino, Claudia, Diodato, Daria, Schottmann, Gudrun, Poulton, Joanna, Burlina, Alberto, Jonckheere, An, Munnich, Arnold, Rolinski, Boris, Ghezzi, Daniele, Rokicki, Dariusz, Wellesley, Diana, Martinelli, Diego, Wenhong, Ding, Lamantea, Eleonora, Ostergaard, Elsebet, Pronicka, Ewa, Pierre, Germaine, Smeets, Hubert, Wittig, Ilka, Scurr, Ingrid, Irenaeus De Coo, Moroni, Isabella, Joél Smet, Mayr, Johannes, Lifang Dai, Meirleir, Linda De, Schuelke, Markus, Zeviani, Massimo, Morscher, Raphael, McFarland, Robert, Seneca, Sara, Klopstock, Thomas, Meitinger, Thomas, Wieland, Thomas, Strom, Tim, Herberg, Ulrike, Ahting, Uwe, Sperl, Wolfgang, Marie-Cecile Nassogne, Ling, Han, Fang, Fang, Freisinger, Peter, Coster, Rudy Van, Strecker, Valentina, Taylor, Robert, Häberle, Johannes, Vockley, Jerry, Prokisch, Holger, and Wortmann, Saskia
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3. Good health - Abstract
Figure S1. Representative picture of Complex I assembly in fibroblasts of individual 1 (A, upper panels) Two-dimensional BN/SDS-PAGE separation and quantification of fluorescent-labelled mitochondrial complexes from 10 mg patient (left) and control fibroblasts (right) are shown. (A, lower panels) show silver stained 2 D gels. (B) Quantified Supercomplexes in 2D gels from control and patient fibroblast with and without bezafibrate treatment for 72 h. (C) Panoramaplots of 2D gels with assignment of signals used for quantification of complexes. Assignment of complexes: O, OGDC, oxoglutarate dehydrogenase complex; V, complex V or ATP synthase; III, complex III or cytochrome c reductase; IV, complex IV or cytochrome c oxidase; S, supercomplexes composed of respiratory chain complexes I, III, and IV. 2-D gels were scanned side by side for direct comparison and are shown as pseudocolors. (pdf). (PDF 1109 kb)
59. Clinical, biochemical and genetic spectrum of 70 patients with ACAD9 deficiency: is riboflavin supplementation effective?
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Repp, Birgit M, Mastantuono, Elisa, Alston, Charlotte L, Schiff, Manuel, Haack, Tobias B, Rötig, Agnes, Ardissone, Anna, Lombès, Anne, Catarino, Claudia B, Diodato, Daria, Schottmann, Gudrun, Poulton, Joanna, Burlina, Alberto, Jonckheere, An, Munnich, Arnold, Rolinski, Boris, Ghezzi, Daniele, Rokicki, Dariusz, Wellesley, Diana, Martinelli, Diego, Wenhong, Ding, Lamantea, Eleonora, Ostergaard, Elsebet, Pronicka, Ewa, Pierre, Germaine, Smeets, Hubert JM, Wittig, Ilka, Scurr, Ingrid, De Coo, Irenaeus FM, Moroni, Isabella, Smet, Joél, Mayr, Johannes A, Dai, Lifang, De Meirleir, Linda, Schuelke, Markus, Zeviani, Massimo, Morscher, Raphael J, McFarland, Robert, Seneca, Sara, Klopstock, Thomas, Meitinger, Thomas, Wieland, Thomas, Strom, Tim M, Herberg, Ulrike, Ahting, Uwe, Sperl, Wolfgang, Nassogne, Marie-Cecile, Ling, Han, Fang, Fang, Freisinger, Peter, Van Coster, Rudy, Strecker, Valentina, Taylor, Robert W, Häberle, Johannes, Vockley, Jerry, Prokisch, Holger, and Wortmann, Saskia
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Male ,Electron Transport Complex I ,Mitochondrial Diseases ,Muscle Weakness ,Cardiomyopathy ,Lactic acidosis ,Riboflavin ,Activities of daily living ,Heart transplantation ,Cardiomyopathy, Hypertrophic ,Prognosis ,Vitamin ,Acyl-CoA Dehydrogenase ,3. Good health ,Mitochondrial disorder ,Treatment ,Neonatal ,Complex I ,Humans ,Female ,Acidosis ,Amino Acid Metabolism, Inborn Errors - Abstract
BACKGROUND: Mitochondrial acyl-CoA dehydrogenase family member 9 (ACAD9) is essential for the assembly of mitochondrial respiratory chain complex I. Disease causing biallelic variants in ACAD9 have been reported in individuals presenting with lactic acidosis and cardiomyopathy. RESULTS: We describe the genetic, clinical and biochemical findings in a cohort of 70 patients, of whom 29 previously unpublished. We found 34 known and 18 previously unreported variants in ACAD9. No patients harbored biallelic loss of function mutations, indicating that this combination is unlikely to be compatible with life. Causal pathogenic variants were distributed throughout the entire gene, and there was no obvious genotype-phenotype correlation. Most of the patients presented in the first year of life. For this subgroup the survival was poor (50% not surviving the first 2 years) comparing to patients with a later presentation (more than 90% surviving 10 years). The most common clinical findings were cardiomyopathy (85%), muscular weakness (75%) and exercise intolerance (72%). Interestingly, severe intellectual deficits were only reported in one patient and severe developmental delays in four patients. More than 70% of the patients were able to perform the same activities of daily living when compared to peers. CONCLUSIONS: Our data show that riboflavin treatment improves complex I activity in the majority of patient-derived fibroblasts tested. This effect was also reported for most of the treated patients and is mirrored in the survival data. In the patient group with disease-onset below 1 year of age, we observed a statistically-significant better survival for patients treated with riboflavin.
60. Complex I assembly function and fatty acid oxidation enzyme activity of ACAD9 both contribute to disease severity in ACAD9 deficiency
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Schiff, Manuel, Haberberger, Birgit, Xia, Chuanwu, Mohsen, Al-Walid, Goetzman, Eric S., Wang, Yudong, Uppala, Radha, Zhang, Yuxun, Karunanidhi, Anuradha, Prabhu, Dolly, Alharbi, Hana, Prochownik, Edward V., Haack, Tobias, Häberle, Johannes, Munnich, Arnold, Rötig, Agnes, Taylor, Robert W., Nicholls, Robert D., Kim, Jung-Ja, Prokisch, Holger, Vockley, Jerry, Schiff, Manuel, Haberberger, Birgit, Xia, Chuanwu, Mohsen, Al-Walid, Goetzman, Eric S., Wang, Yudong, Uppala, Radha, Zhang, Yuxun, Karunanidhi, Anuradha, Prabhu, Dolly, Alharbi, Hana, Prochownik, Edward V., Haack, Tobias, Häberle, Johannes, Munnich, Arnold, Rötig, Agnes, Taylor, Robert W., Nicholls, Robert D., Kim, Jung-Ja, Prokisch, Holger, and Vockley, Jerry
- Abstract
Acyl-CoA dehydrogenase 9 (ACAD9) is an assembly factor for mitochondrial respiratory chain Complex I (CI), and ACAD9 mutations are recognized as a frequent cause of CI deficiency. ACAD9 also retains enzyme ACAD activity for long-chain fatty acids in vitro, but the biological relevance of this function remains controversial partly because of the tissue specificity of ACAD9 expression: high in liver and neurons and minimal in skin fibroblasts. In this study, we hypothesized that this enzymatic ACAD activity is required for full fatty acid oxidation capacity in cells expressing high levels of ACAD9 and that loss of this function is important in determining phenotype in ACAD9-deficient patients. First, we confirmed that HEK293 cells express ACAD9 abundantly. Then, we showed that ACAD9 knockout in HEK293 cells affected long-chain fatty acid oxidation along with Cl, both of which were rescued by wild type ACAD9. Further, we evaluated whether the loss of ACAD9 enzymatic fatty acid oxidation affects clinical severity in patients with ACAD9 mutations. The effects on ACAD activity of 16 ACAD9 mutations identified in 24 patients were evaluated using a prokaryotic expression system. We showed that there was a significant inverse correlation between residual enzyme ACAD activity and phenotypic severity of ACAD9-deficient patients. These results provide evidence that in cells where it is strongly expressed, ACAD9 plays a physiological role in fatty acid oxidation, which contributes to the severity of the phenotype in ACAD9-deficient patients. Accordingly, treatment of ACAD9 patients should aim at counteracting both CI and fatty acid oxidation dysfunctions
61. Molecular analysis of ANT1, TWINKLE and POLG in patients with multiple deletions or depletion of mitochondrial DNA by a dHPLC-based assay.
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Naïmi, Mourad, Bannwarth, Sylvie, Procaccio, Vincent, Pouget, Jean, Desnuelle, Claude, Pellissier, Jean-François, Rötig, Agnes, Munnich, Arnold, Calvas, Patrick, Richelme, Christian, Jonveaux, Philippe, Castelnovo, Giovanni, Simon, Mariella, Clanet, Michel, Wallace, Douglas, and Paquis-Flucklinger, Véronique
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MITOCHONDRIAL DNA - Abstract
A correction to the article "Molecular analysis of ANT1, TWINKLE and POLG in patients with multiple deletions or depletion of mitochondrial DNA by a dHPLC-based assay" that was published in a previous issue of the periodical is presented.
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- 2007
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62. Sequence and structure of the human OXA1L gene and its upstream elements
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Rötig, Agnès, Parfait, Béatrice, Heidet, Laurence, Dujardin, Geneviève, Rustin, Pierre, and Munnich, Arnold
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- 1997
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63. Deletion of mitochondrial DNA in patient with chronic tubulointerstitial nephritis
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Rötig, Agnès, Goutières, Françoise, Niaudet, Patrick, Rustin, Pierre, Chretien, Dominique, Guest, Geneviève, Mikol, Jacqueline, Gubler, Marie-Claire, and Munnich, Arnold
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- 1995
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64. An improved spectrophotometric assay of pyruvate dehydrogenase in lactate dehydrogenase contaminated mitochondrial preparations from human skeletal muscle
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Chretien, Dominique, Pourrier, Marc, Bourgeron, Thomas, Séné, Maï, Rötig, Agnès, Munnich, Arnold, and Rustin, Pierre
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- 1995
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65. Macular dystrophy, diabetes, and deafness associated with a large mitochondrial dma deletion
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Souied, Eric H., Salès, Marie-Joelle, Soubrane, Gisèle, Coscas, Gabriel, Bigorie, Basile, Kaplan, Josseline, Munnich, Arnold, and Rötig, Agnès
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- 1998
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66. Loss of MTX2 causes mandibuloacral dysplasia and links mitochondrial dysfunction to altered nuclear morphology
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Christian Kubisch, Robert Rubinsztajn, Arianne Llamos Paneque, Philippe Manivet, Catarina Pereira, Laila Selim, Nathalie Escande-Beillard, Abigail Loh, Peter Bauer, Catherine Bartoli, Song-Hua Lee, Morgane Le Mao, Hϋlya Kayserili, Coraline Airault, Nihal M. Al Menabawy, Lisa Martino, Yosef Gruenbaum, Guy Lenaers, Antoine Muchir, Agnès Rötig, Annachiara De Sandre-Giovannoli, Nicolas Lévy, Sahar Elouej, Sheela Nampoothiri, Chayki Charar, Jean-François Deleuze, Karim Harhouri, Bruno Reversade, Davor Lessel, Geneviève Baujat, ACS - Heart failure & arrhythmias, Marseille medical genetics - Centre de génétique médicale de Marseille (MMG), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), MitoVasc - Physiopathologie Cardiovasculaire et Mitochondriale (MITOVASC), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Amrita Institute of Medical Sciences and Research Center, Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Koç University, Cairo University Children Hospital, Medical Genetics Service Specialties Hospital, Universitaetsklinikum Hamburg-Eppendorf = University Medical Center Hamburg-Eppendorf [Hamburg] (UKE), Hôpital Necker, The Hebrew University of Jerusalem (HUJ), Centre National de Recherche en Génomique Humaine (CNRGH), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), CENTOGENE AG, Institute of Medical Biology A*STAR, Sorbonne Université (SU), CeleScreen SAS, Maladies neurodéveloppementales et neurovasculaires (NeuroDiderot (UMR_S_1141 / U1141)), 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), Centre de ressources biologiques Tissus ADN Cellules [Hôpital de la Timone - APHM] (CRB TAC), 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)-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), ANR-11-IDEX-0001,Amidex,INITIATIVE D'EXCELLENCE AIX MARSEILLE UNIVERSITE(2011), ANR-10-LABX-0013,GENMED,Medical Genomics(2010), ANR-10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010), LENAERS, Guy, INITIATIVE D'EXCELLENCE AIX MARSEILLE UNIVERSITE - - Amidex2011 - ANR-11-IDEX-0001 - IDEX - VALID, Medical Genomics - - GENMED2010 - ANR-10-LABX-0013 - LABX - VALID, Développment d'une infrastructure française distribuée coordonnée - - France-BioImaging2010 - ANR-10-INBS-0004 - INBS - VALID, Physiopathologie Cardiovasculaire et Mitochondriale (MITOVASC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Karabey, Hülya Kayserili (ORCID 0000-0003-0376-499X & YÖK ID 7945), Escande-Beillard, Nathalie, Reversade, Bruno, Elouej,Sahar, Harhouri, Karim, Le Mao, Morgane, Baujat, Genevieve, Nampoothiri, Sheela, Menabawy, Nihal Al, Selim, Laila, Paneque, Arianne Llamos, Kubisch, Christian, Lessel, Davor, Rubinsztajn,Robert, Charar, Chayki, Bartoli, Catherine, Airault, Coraline, Deleuze, Jean-François, Rötig, Agnes, Bauer, Peter, Pereira, Catarina, Loh, Abigail, Muchir, Antoine, Martino, Lisa, Gruenbaum, Yosef, Lee, Song-Hua, Manivet, Philippe, Lenaers, Guy, Lévy, Nicolas, De Sandre-Giovannoli, Annachiara, and School of Medicine
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0301 basic medicine ,Premature aging ,Senescence ,Pathology ,medicine.medical_specialty ,endocrine system ,animal structures ,Science ,[SDV]Life Sciences [q-bio] ,General Physics and Astronomy ,Apoptosis ,General Biochemistry, Genetics and Molecular Biology ,Progeroid syndromes ,Article ,Nuclear envelope ,LMNA ,03 medical and health sciences ,0302 clinical medicine ,Mitophagy ,Genetics research ,medicine ,lcsh:Science ,Multidisciplinary ,business.industry ,Glomerulosclerosis ,General Chemistry ,Energy metabolism ,medicine.disease ,3. Good health ,Mandibuloacral dysplasia ,[SDV] Life Sciences [q-bio] ,030104 developmental biology ,Mitochondrial Membrane Protein ,Next-generation sequencing ,Medicine ,lcsh:Q ,business ,030217 neurology & neurosurgery - Abstract
Mandibuloacral dysplasia syndromes are mainly due to recessive LMNA or ZMPSTE24 mutations, with cardinal nuclear morphological abnormalities and dysfunction. We report five homozygous null mutations in MTX2, encoding Metaxin-2 (MTX2), an outer mitochondrial membrane protein, in patients presenting with a severe laminopathy-like mandibuloacral dysplasia characterized by growth retardation, bone resorption, arterial calcification, renal glomerulosclerosis and severe hypertension. Loss of MTX2 in patients’ primary fibroblasts leads to loss of Metaxin-1 (MTX1) and mitochondrial dysfunction, including network fragmentation and oxidative phosphorylation impairment. Furthermore, patients’ fibroblasts are resistant to induced apoptosis, leading to increased cell senescence and mitophagy and reduced proliferation. Interestingly, secondary nuclear morphological defects are observed in both MTX2-mutant fibroblasts and mtx-2-depleted C. elegans. We thus report the identification of a severe premature aging syndrome revealing an unsuspected link between mitochondrial composition and function and nuclear morphology, establishing a pathophysiological link with premature aging laminopathies and likely explaining common clinical features., Association Française contre les Myopathies (AFM); Deutsche Forschungsgemeinschaft; GENMED Laboratory of Excellence on Medical Genomics, Agence Nationale de la Recherche; Institut National de la Santé et de la Recherche Médicale (INSERM); Aix-Marseille University (AMU) by the RAREMED Amidex Project
- Published
- 2020
67. Iron overload and mitochondrial diseases
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Rustin, Pierre, von Kleist-Retzow, Jürgen-Christoph, Rötig, Agnès, and Munnich, Arnold
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- 1998
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68. The kidney in mitochondrial cytopathies
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Niaudet, Patrick and Rötig, Agnès
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- 1997
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69. Respiratory chain deficiencies.
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Delonlay P, Rötig A, and Sarnat HB
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- Child, Epilepsy genetics, Epilepsy pathology, Humans, Leukoencephalopathies genetics, Leukoencephalopathies pathology, Magnetic Resonance Imaging, Mitochondrial Diseases genetics, Mitochondrial Diseases pathology, Brain pathology, Epilepsy diagnosis, Leukoencephalopathies diagnosis, Mitochondrial Diseases diagnosis, Muscle, Skeletal pathology
- Abstract
Mitochondrial functions are intimately associated with neurological symptoms. Various clinical and biological features are suggestive of energy depletion diseases, such as Leigh syndrome, Alpers syndrome, epilepsy (including myoclonic seizures and status epilepticus), stroke-like episodes, and acute cerebellar ataxia with high lactate peaks on magnetic resonance spectroscopy. Magnetic resonance imaging (MRI) discloses abnormalities in over 90% of the cases presenting with neurological symptoms. Basal ganglionic involvement, the most frequent imaging sign, can be isolated or combined with subtentorial atrophy of both the cerebellum and brainstem. MRS monovoxel proton spectroscopy is useful to reveal high lactate spikes if placed in the putamen and the cerebellar dentate nucleus. Lactate and pyruvate levels are required to exclude pyruvate dehydrogenase deficiency. However, lactate may be normal in the CSF. Clinical and biochemical investigations guide molecular studies, with two major heredities: mtDNA point mutations and autosomal recessive defects that program the majority of respiratory chain subunits. Muscle biopsy is the first test demonstrating the histochemical and ultrastructural alterations in mitochondria, even in diseases in which myopathy is not clinically prominent, and is also a good tissue for biochemical analysis, as the biopsy is not dangerous for the patient. Negative results in skeletal muscle do not exclude respiratory chain deficiency, and a liver biopsy may be necessary whatever the blood AST and ALT levels, to perform biochemical and molecular investigations. Only the identification of nuclear or mitochondrial mutation confirms the diagnosis., (Copyright © 2013 Elsevier B.V. All rights reserved.)
- Published
- 2013
- Full Text
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