par Smet, Joel;Seneca, Sara;De Paepe, Boel;Meulemans, Ann 
;Verhelst, Helene;Leroy, Jules ;De Meirleir, Linda;Lissens, Willy;Van Coster, Rudy
Référence Electrophoresis, 30, 20, page (3565-3572)
Publication Publié, 2009
;Verhelst, Helene;Leroy, Jules ;De Meirleir, Linda;Lissens, Willy;Van Coster, RudyRéférence Electrophoresis, 30, 20, page (3565-3572)
Publication Publié, 2009
Article révisé par les pairs
| Résumé : | Complex V, site of the final step in oxidative phosphorylation, uses the proton gradient across the inner mitochondrial membrane for the production of ATP. It is a multisubunit complex composed of a catalytic domain (F1) and a membrane domain (F0) linked by two stalks. Subcomplexes of complex V containing the F1 domain have previously been reported in small series of patients. We report the results in tissue samples and/or cultured skin fibroblasts studied by blue native PAGE followed by activity staining in the gel. Catalytically active subcomplexes of complex V were detected in 66 tissues originating from 53 patients. In 29 of the latter (55%), a mitochondrial DNA (mtDNA) defect was identified. Twelve patients had a pathogenic point mutation in a mitochondrial tRNA, one a large mtDNA deletion, 12 showed mtDNA depletion and four had a mutation in the MT-ATP6 gene. We conclude that the presence of subcomplexes of complex V is a valuable indicator in the detection of mtDNA defects. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA. |
