Long-Chain Acyl-Coenzyme A Dehydrogenase Deficiency: Biochemical Studies in Fibroblasts from Three Patients

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Abstract
We studied fibroblasts from three patients with long-chain acyl-coenzyme A dehydrogenase (LCADH) deficiency; siblings H.C. and J.C. had milder clinical phenotypes than unrelated patient R-1. In H.C, J.C, and R-1 oxidation of [9,10(n)-3H]palmitate was 50, 48, and 28% of control, respectively, with R-l having significantly less activity than H.C. and J.C. (p < 0.05). Assays of mitochondrial short-chain and medium-chain acyl-coenzyme A dehydrogenases were normal in H.C. and J.C. However, mitochondrial LCADH activities in all three ranged from 17 to 21% of control. Flavin adenine dinucle-otide addition increased LCADH activities in all three to 27–36% of control. In the presence of monospecific medium-chain acyl-coenzyme A dehydrogenase antiseria, LCADH activity decreased 17% in controls, and fell to ≤11% of control in J.C. and R-1. The heterogeneity observed in the [3H]palmitate oxidation studies was not explained by differences in LCADH activities under any assay condition.

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