MECR Mutations Cause Childhood-Onset Dystonia and Optic Atrophy, a Mitochondrial Fatty Acid Synthesis Disorder.
Клинический случайСтатьяНазвание и аннотация: Перевод пока не подготовлен
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Heimer Gali, Kerätär Juha M, Riley Lisa G, Balasubramaniam Shanti, Eyal Eran, Pietikäinen Laura P, Hiltunen J Kalervo, Marek-Yagel Dina, Hamada Jeffrey, Gregory Allison, Rogers Caleb, Hogarth Penelope, Nance Martha A, Shalva Nechama, Veber Alvit, Tzadok Michal, Nissenkorn Andreea, Tonduti Davide, Renaldo Florence, University of Washington Center for Mendelian Genomics, Kraoua Ichraf, Panteghini Celeste, Valletta Lorella, Garavaglia Barbara, Cowley Mark J, Gayevskiy Velimir, Roscioli Tony, Silberstein Jonathon M, Hoffmann Chen, Raas-Rothschild Annick, Tiranti Valeria, Anikster Yair, Christodoulou John, Kastaniotis Alexander J, Ben-Zeev Bruria, Hayflick Susan J
Аннотация
Mitochondrial fatty acid synthesis (mtFAS) is an evolutionarily conserved pathway essential for the function of the respiratory chain and several mitochondrial enzyme complexes. We report here a unique neurometabolic human disorder caused by defective mtFAS. Seven individuals from five unrelated families presented with childhood-onset dystonia, optic atrophy, and basal ganglia signal abnormalities on MRI. All affected individuals were found to harbor recessive mutations in MECR encoding the mitochondrial trans-2-enoyl-coenzyme A-reductase involved in human mtFAS. All six mutations are extremely rare in the general population, segregate with the disease in the families, and are predicted to be deleterious. The nonsense c.855T>G (p.Tyr285∗), c.247_250del (p.Asn83Hisfs∗4), and splice site c.830+2_830+3insT mutations lead to C-terminal truncation variants of MECR. The missense c.695G>A (p.Gly232Glu), c.854A>G (p.Tyr285Cys), and c.772C>T (p.Arg258Trp) mutations involve conserved amino acid residues, are located within the cofactor binding domain, and are predicted by structural analysis to have a destabilizing effect. Yeast modeling and complementation studies validated the pathogenicity of the MECR mutations. Fibroblast cell lines from affected individuals displayed reduced levels of both MECR and lipoylated proteins as well as defective respiration. These results suggest that mutations in MECR cause a distinct human disorder of the mtFAS pathway. The observation of decreased lipoylation raises the possibility of a potential therapeutic strategy.