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(Received for publication, February 13, 1997, and in revised form, August 8, 1997)
From the Departments of Anaplerotic pyruvate carboxylation was examined
in hearts perfused with physiological concentrations of glucose,
[U-13C3]lactate, and
[U-13C3]pyruvate. Also, a fatty acid,
[1-13C]octanoate, or ketone bodies were added at
concentrations providing acetyl-CoA at a rate resulting in either low
or substantial pyruvate decarboxylation. Relative contributions of
pyruvate and fatty acids to citrate synthesis were determined from the
13C labeling pattern of effluent citrate by gas
chromatography-mass spectrometry (see companion article, Comte, B.,
Vincent, G., Bouchard, B., and Des Rosiers, C. (1997) J. Biol. Chem. 272, 26117-26124). Precision on flux measurements of
anaplerotic pyruvate carboxylation depended on the mix of substrates
supplied to the heart. Anaplerotic fluxes were precisely determined
under conditions where acetyl-CoA was predominantly supplied by
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26125-26131
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A 13C Mass Isotopomer Study of Anaplerotic Pyruvate
Carboxylation in Perfused Rat Hearts
,§
Nutrition and
§ Biochemistry, University of Montréal,
Montréal, Québec H3C 3J7, Canada
-oxidation, as it occurred with 0.2 or 1 mM octanoate.
Then, anaplerotic pyruvate carboxylation provided 3-8% of the OAA
moiety of citrate and was modulated by concentrations of lactate and
pyruvate in the physiological range. Also, the contribution of pyruvate
to citrate formation through carboxylation was equal to or greater than
through decarboxylation. Furthermore, 13C labeling data on
tissue citric acid cycle intermediates and pyruvate suggest that (i)
anaplerosis occurs also at succinate and (ii) cataplerotic malate
decarboxylation is low. Rather, the presence of citrate in the effluent
perfusate of hearts perfused with physiological concentrations of
glucose, lactate, and pyruvate and concentrations of octanoate leading
to maximal oxidative rates suggests a cataplerotic citrate efflux from
mitochondria to cytosol. Taken altogether, our data raise the
possibility of a link between pyruvate carboxylation and mitochondrial
citrate efflux. In view of the proposed feedback regulation of
glycolysis by cytosolic citrate, such a link would support a role of
anaplerosis and cataplerosis in metabolic signal transmission between
mitochondria and cytosol in the normoxic heart.
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