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Division of Cardiology, Department of Internal Medicine, University of Texas-Houston Medical School, Houston, Texas 77030
Malonyl-CoA decarboxylase (MCD) catalyzes the
degradation of malonyl-CoA, an important modulator of fatty acid
oxidation. We hypothesized that increased fatty acid availability would
increase the expression and activity of heart and skeletal muscle MCD, thereby promoting fatty acid utilization. The results show that high-fat feeding, fasting, and streptozotocin-induced diabetes all
significantly increased the plasma concentration of nonesterified fatty
acids, with a concomitant increase in both rat heart and skeletal
muscle MCD mRNA. Upon refeeding of fasted animals, MCD expression
returned to basal levels. Fatty acids are known to activate
peroxisome proliferator-activated receptor-
(PPAR). Specific
PPAR stimulation, through Wy-14643 treatment, significantly increased the expression of MCD in heart and skeletal muscle. Troglitazone, a specific PPAR
agonist, decreased MCD expression. The
sensitivity of MCD induction by fatty acids and Wy-14643 was soleus > extensor digitorum longus > heart. High plasma
fatty acids consistently increased MCD activity only in solei, whereas MCD activity in the heart actually decreased with high-fat feeding. Pressure overload-induced cardiac hypertrophy, in which PPAR expression is decreased (and fatty acid oxidation is decreased), resulted in decreased MCD mRNA and activity, an effect that was dependent on fatty acids. The results suggest that fatty acids induce
the expression of MCD in rat heart and skeletal muscle. Additional
posttranscriptional mechanisms regulating MCD activity appear to exist.
heart; malonyl-coenzyme A decarboxylase; nonesterified fatty acids; peroxisome proliferator-activated receptor-; skeletal muscle
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