| Literature DB >> 25251739 |
Rosalba Carrozzo1, Alessandra Torraco2, Giuseppe Fiermonte3, Diego Martinelli4, Michela Di Nottia2, Teresa Rizza2, Angelo Vozza3, Daniela Verrigni2, Daria Diodato2, Giovanni Parisi3, Arianna Maiorana4, Cristiano Rizzo5, Ciro Leonardo Pierri3, Stefania Zucano3, Fiorella Piemonte2, Enrico Bertini2, Carlo Dionisi-Vici6.
Abstract
Dihydrolipoamide dehydrogenase (DLD, E3) is a flavoprotein common to pyruvate, α-ketoglutarate and branched-chain α-keto acid dehydrogenases. We found two novel DLD mutations (p.I40Lfs*4; p.G461E) in a 19 year-old patient with lactic acidosis and a complex amino- and organic aciduria consistent with DLD deficiency, manifesting progressive exertional fatigue. Muscle biopsy showed mitochondrial proliferation and lack of DLD cross-reacting material. Riboflavin supplementation determined the complete resolution of exercise intolerance with the partial restoration of the DLD protein and disappearance of mitochondrial proliferation in the muscle. Morphological and functional studies support the riboflavin chaperon-like role in stabilizing DLD protein with rescue of its expression in the muscle.Entities:
Keywords: Branched-chain amino acids; Chaperon; Dihydrolipoamide dehydrogenase deficiency; Mitochondrial myopathy; Riboflavin; α-Keto acids
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Year: 2014 PMID: 25251739 DOI: 10.1016/j.mito.2014.09.006
Source DB: PubMed Journal: Mitochondrion ISSN: 1567-7249 Impact factor: 4.160