The Metabolism of (- ) -0ctanoylcarnitine in Perfused Livers from Fed and Fasted Rats EVIDENCE FOR A POSSIBLE REGULATORY ROLE OF CARNITINE ACYLTRANSFERASE IN THE CONTROL OF KETOGENESIS*
نویسنده
چکیده
In confirmation of previous findings it was shown that perfused livers from fasted rats converted oleic acid into ketone bodies far more efficiently than did livers from fed animals, whereas differences in rates of ketogenesis from octanoate were much less pronounced. However, relative rates of ketone body production from (-)-octanoylcamitine resembled those seen with oleic acid rather than those obtained with free octanoic acid as substrate. In addition, ( +)-octanoylcarnitine, an inhibitor of carnitine acyltransferase, was without effect on the oxidation of octanoic acid, but caused a profound and quantitatively similar depression in the oxidation of both oleic acid and ( -)-octanoylcarnitine. The data support the concept that the carnitine acyltransferase system of liver is under strict dietary, or hormonal control, or both, and that it may constitute a primary site for the regulation of hepatic fatty acid oxidation and ketogenesis.
منابع مشابه
The metabolism of (minus)-octanoylcarnitine in perfused livers from fed and fasted rats. Evidence for a possible regulatory role of carnitine acyltransferase in the control of ketogenesis.
In confirmation of previous findings it was shown that perfused livers from fasted rats converted oleic acid into ketone bodies far more efficiently than did livers from fed animals, whereas differences in rates of ketogenesis from octanoate were much less pronounced. However, relative rates of ketone body production from (-)-octanoylcamitine resembled those seen with oleic acid rather than tho...
متن کاملA possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis.
Studied on the oxidation of oleic and octanoic acids to ketone bodies were carried out in homogenates and in mitochondrial fractions of livers taken from fed and fasted rats. Malonyl-CoA inhibited ketogenesis from the former but not from the latter substrate. The site of inhibition appeared to be the carnitine acyltransferase I reaction. The effect was specific and easily reversible. Inhibitory...
متن کاملIn support of the roles of malonyl-CoA and carnitine acyltransferase I in the regulation of hepatic fatty acid oxidation and ketogenesis.
The rate of fatty acid synthesis in hepatocytes from meal-fed rats was manipulated over a wide range using glucose, lactate, and pyruvate to drive the system maximally, and glucagon, 5-(tetradecyloxy)-2-furoic acid (RMI 14,514), or a combination of both agents to inhibit lipogenesis. Measurements were made of cellular malonyl-CoA levels, long chain acylcarnitine concentration, and [l-‘4C]oleate...
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The diffusion of H2O2 into the cytoplasm from peroxisomes during high rates of peroxisomal beta oxidation of fatty acids was studied in perfused livers from rats treated with the hepatocarcinogenic peroxisome proliferator, nafenopin. Efflux of oxidized glutathione (GSSG) into the bile was used as a measure of increased H2O2 supply for cytoplasmic glutathione peroxidase. Male F-344 rats were giv...
متن کاملHormonal control of ketogenesis. Rapid activation of hepatic ketogenic capacity in fed rats by anti-insulin serum and glucagon.
The enhanced capacity for long-chain fatty acid oxidation and ketogenesis that develops in the rat liver between 6 and 9 h after the onset of starvation was shown to be inducible much more rapidly by administration of anti-insulin serum or glucagon to fed rats. After only 1 h of treatment with either agent, the liver had clearly switched from a "nonketogenic" to a "ketogenic" profile, as determ...
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تاریخ انتشار 2002