The metabolism of (-) octanoylcarnitine in perfused livers from fed and fasted rats. Evidence for a possible regulatory role of carnitine acyltransferase in the control of ketogenesis

J. D. McGarry, D. W. Foster

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

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 (-)-octanoylcarnitine 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.

Original languageEnglish (US)
Pages (from-to)7984-7990
Number of pages7
JournalJournal of Biological Chemistry
Volume249
Issue number24
StatePublished - 1974

Fingerprint

Carnitine Acyltransferases
Oleic Acid
Metabolism
Liver
Rats
Ketone Bodies
Oxidation
Animals
Fatty Acids
Substrates
octanoic acid
octanoylcarnitine

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{973628beecae4bd99d749c413b055619,
title = "The metabolism of (-) octanoylcarnitine in perfused livers from fed and fasted rats. Evidence for a possible regulatory role of carnitine acyltransferase in the control of ketogenesis",
abstract = "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 (-)-octanoylcarnitine 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.",
author = "McGarry, {J. D.} and Foster, {D. W.}",
year = "1974",
language = "English (US)",
volume = "249",
pages = "7984--7990",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "24",

}

TY - JOUR

T1 - The metabolism of (-) octanoylcarnitine in perfused livers from fed and fasted rats. Evidence for a possible regulatory role of carnitine acyltransferase in the control of ketogenesis

AU - McGarry, J. D.

AU - Foster, D. W.

PY - 1974

Y1 - 1974

N2 - 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 (-)-octanoylcarnitine 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.

AB - 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 (-)-octanoylcarnitine 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.

UR - http://www.scopus.com/inward/record.url?scp=0016163592&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016163592&partnerID=8YFLogxK

M3 - Article

C2 - 4430681

AN - SCOPUS:0016163592

VL - 249

SP - 7984

EP - 7990

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 24

ER -