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The expression pattern of mitochondrial carnitine
palmitoyltransferase (CPT) enzymes was examined in the developing rat
heart. Whereas the specific activity of CPT II increased
Because the myocardial carnitine
content is very low at birth and rises dramatically over the next
several weeks, it can be estimated that L-CPT I
( K
Volume 270,
Number 15,
Issue of April 14, pp. 8952-8957, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
3-fold
during the first month of life, the profile for CPT I, which is
composed of both liver (L) and muscle (M) isoforms, was more complex.
Exposure of mitochondria to [
H]etomoxir (a
covalent ligand for CPT I), followed by fluorographic analysis of the
membrane proteins, established that while in the adult heart L-CPT I
represents a very minor constituent, its contribution is much greater
in the newborn animal. Use of the related inhibitor,
2-[6-(2,4-dinitrophenoxy)hexyl]oxirane-2-carboxylic acid
(specific for L-CPT I), allowed the activities of the two CPT I
variants to be quantified separately. The results showed that in the
neonatal heart, L-CPT I contributes 25% to total CPT I activity
(in V
terms), the value falling during growth of
the pups (with concomitant increasing expression of the M isoform) to
its adult level of 2-3%.
for carnitine of only 30
µ
M compared with a value of 500 µ
M for M-CPT
I) is responsible for some 60% of total cardiac fatty acid oxidation in
the newborn rat; the value falls to
4% in adult animals. Should
these findings have a parallel in humans, they could have important
implications for understanding the pathophysiological consequences of
inherited L-CPT I deficiency syndromes.
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