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Fig 1.

CPT II activities and thermal instability in CPT II-deficient fibroblasts.

Fibroblast lysates were preincubated at 37°C or 41°C. Enzymatic reactions commenced by the addition of substrates at 37°C. Data are the means of five separate experiments. The average of three independent experiments is shown ± SEM (*P<0.05).

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Fig 2.

CPT II expression and the dominant—negative effect of CPT II variants on substrate-dependent kinetics.

(A) CPT II expression was analyzed by Western Blotting with an anti-CPT II antibody. (B) Dominant—negative effect of CPT II variants was analyzed by substrate-dependent kinetics. (C) Relative protein expression of control and variant CPT II. (D) Real-time PCR analysis of control and variant CPT II expression. Lane 1, control fibroblasts; lane 2, V368I (heterozygous); lane 3, V368I (homozygous); lane 4, F352C (heterozygous) + V368I (homozygous). CPT II protein was expressed relative to β-actin. Vmax and Km values were obtained from kinetic analysis (1/V versus 1/[S] plots) by varying the concentrations of L-[methyl-3H] carnitine between 0–300 μM at a fixed 50 μM palmitoyl-CoA concentration. (●) control, (▲) V368I (Homo), (◆) F352C (Hetero) + V368I (Homo). Data are means of three separate experiments. The average of three independent experiments is shown ± SEM (*P<0.05)

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Fig 3.

Pulse-chase (left) and half-lives (right) of control and variant CPT II in fibroblasts.

Cultured fibroblasts were pulse-labeled with L-[35S] methionine for 2 h and chased for 0, 6, 12, and 18 h. CPT II from fibroblast lysates was immunoprecipitated with anti-CPT II antibodies, then subjected to SDS-PAGE followed by autoradiography. (●) control, (■) V368I (homozygous), (▲) F352C (heterozygous) + V368I (homozygous). The average of three independent experiments is shown ± SEM.

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Fig 3 Expand

Fig 4.

Reduction of mitochondrial membrane potential of control and variant CPT IIs in cultured fibroblasts.

Control (A, D), V368I (homozygous) (B, E), and F352C (heterozygous) + V368I (homozygous) (C, F) fibroblasts were cultured at 37°C and 41°C. Mitochondrial depolarization was monitored by 15 min treatment with 10 μM of JC-1 in the dark and visualized under a fluorescence microscope. Scale bars, 100 μm.

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Fig 5.

Cell apoptosis analysis of CPT II variants in fibroblasts.

(A) Apoptotic fibroblasts were measured by flow cytometry. Fibroblasts incubated with DMSO were used as a control. (B) LDH assay of control and CPT II variants in fibroblasts. (C) Apoptotic factor release was analyzed by Western Blotting with antibodies against caspase-3, caspase-8, cytochrome c, and Bid for control and variant CPT IIs in control and CPT II-deficient fibroblasts. CPT II proteins are expressed relative to β-actin. Data are means of three separate experiments. The average of three independent experiments is shown ± SEM (*P<0.05).

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Fig 5 Expand

Fig 6.

Correlation between CPT II activity and β-oxidation/ATP production at 41°C and 37°C in CPT II-deficient fibroblasts.

(●) control, (■) V368I (homozygous), (△) F352C (heterozygous) + V368I (homozygous). CPT II activity, β-oxidation, and ATP production are expressed as % of control values of control fibroblasts at 37°C. Data areand means of five separate experiments: 0.53 nmol/min/mg protein of CPT II activity; 14.5 nmol of released CO2/h/106 cells; 8.12 nmol of ATP/106 cells. The average of three independent experiments is shown ± SEM.

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Fig 6 Expand

Fig 7.

A proposed energy crisis pathway induced by CPT II deficiency.

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Fig 7 Expand