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1 Department of Pediatric, Vanderbilt University Medical Center, Nashville, TN, USA; Department of Pediatrics, University of Groningen, Groningen, The Netherlands
2 Department of Pediatrics, University of Groningen, Groningen, The Netherlands
3 Cellular Biochemistry, Hannah Research Institute, Ayr, United Kingdom
4 Endocrinology Department, Institut Cochin, Paris, France
* To whom correspondence should be addressed. E-mail: f.r.van.der.ley{at}med.rug.nl.
Carnitine palmitoyltransferase I (CPT I) catalyses the conversion of acyl-CoA to acylcarnitine at the outer mitochondrial membrane and is a key enzyme in the control of long-chain fatty acid (LC-FA) oxidation. Since myocardial LC-FA oxidation (FAO) increases dramatically after birth, we determined the extent to which CPT I expression contributes to these changes in the perinatal lamb. We measured the steady-state level of transcripts of the CPT1A and CPT1B genes, which encode the liver (L) and muscle (M) CPT I isoforms, respectively, as well as the amount of these proteins; their total activity; and the amount of carnitine in left ventricular tissue from fetal and newborn lambs. We compared these data with previously obtained myocardial FAO rates in vivo in the same model. The results showed that CPT1B was already expressed before birth and that total CPT1 expression transiently increased after birth. The protein level of M-CPT I was high throughout development, whereas that of L-CPT I was only transiently upregulated in the first week after birth. The total CPT I activity in vitro also increased after birth. However, the increase in myocardial FAO measured in vivo (112-fold) by far exceeds the increase in gene expression (2.2-fold), protein amount (1.1-fold), and enzyme activity (1.2-fold) in vitro. In conclusion, these results stress the importance of substrate supply per se in the postnatal increase in myocardial FAO. M-CPT I is expressed throughout perinatal development, making it a primary target for metabolic modulation of myocardial fatty acid oxidation.
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