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- W2070329997 abstract "Carnitine palmitoyltransferase (CPT) consists of two activities located in the outer (CPT I) and the inner (CPT II) mitochondrial membranes. CPT II deficiency in the adult as well as in the infantile form of the disease has been shown to result from mutations in the CPT II cDNA. Nothing is known regarding the genetic defect in CPT I deficiency. We carried out complementation experiments between CPT I- and infantile CPT II-deficient cell lines. Restoration of 3H2O release from [9,10(n)-3H]-palmitate was chosen as criterion of complementation. As expected, no complementation was observed in heteropolykaryons resulting from fusions between CPT II-deficient cells. Similar results were obtained in fusions between CPT I-deficient cells, suggesting that the enzymatic defect in these cell lines results from mutations in the same gene. Conversely, complementation was observed in fusions between CPT I- and CPT II-deficient cells. These data support that CPT I and CPT II defects result from mutations in distinct genes. Palmitate oxidation by control or CPT I-deficient cell lines was decreased when cocultured with infantile CPT II-deficient cell lines. This effect, not observed in coculture including an adult CPT II-deficient cell line, was carnitine-dependent. The possible mechanism of this effect, suppressed by a high carnitine concentration, is discussed." @default.
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- W2070329997 date "1996-10-01" @default.
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- W2070329997 title "Complementation Analysis of Carnitine Palmitoyltransferase I and II Defects" @default.
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- W2070329997 doi "https://doi.org/10.1203/00006450-199610000-00005" @default.
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