Mitochondrial coupling defect in Charcot-Marie-Tooth type 2A disease
| Autor: | Arnaud Chevrollier, Marc Ferré, Marie-Anne Pou de Crescenzo, Pascal Reynier, Dominique Loiseau, Naïg Gueguen, Agnès Guichet, Yves Malthièry, Marie-Claire Malinge, Dominique Bonneau, Guillaume Nicolas, Patrizia Amati-Bonneau, Christophe Verny, Virginie Guillet |
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| Rok vydání: | 2007 |
| Předmět: |
Adult
Male Mitochondrial Diseases DNA Mutational Analysis Mutation Missense MFN2 Apoptosis Oxidative phosphorylation Biology Mitochondrion medicine.disease_cause Statistics Nonparametric GTP Phosphohydrolases Mitochondrial Proteins Adenosine Triphosphate Charcot-Marie-Tooth Disease medicine Humans Missense mutation Genetic Predisposition to Disease Gene Cells Cultured Skin Membrane Potential Mitochondrial Mutation Membrane Proteins Fibroblasts Middle Aged Cell biology Neurology Membrane protein DNAJA3 Female Neurology (clinical) Reactive Oxygen Species Neuroscience Metabolic Networks and Pathways |
| Zdroj: | Annals of Neurology. 61:315-323 |
| ISSN: | 0364-5134 |
| DOI: | 10.1002/ana.21086 |
| Popis: | Objective Mutations of the mitofusin 2 gene (MFN2) may account for at least a third of the cases of Charcot–Marie–Tooth disease type 2 (CMT2). This study investigates mitochondrial cellular bioenergetics in MFN2-related CMT2A. Methods Mitochondrial network morphology and metabolism were studied in cultures of skin fibroblasts obtained from four CMT2A patients harboring novel missense mutations of the MFN2 gene. Results Although the mitochondrial network appeared morphologically unaltered, there was a significant defect of mitochondrial coupling associated with a reduction of the mitochondrial membrane potential. Interpretation Our results suggest that the sharply reduced efficacy of oxidative phosphorylation in MFN2-related CMT2A may contribute to the pathophysiology of the axonal neuropathy. Ann Neurol 2007;61:315–323 |
| Databáze: | OpenAIRE |
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