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Journal of Lipid Research, Vol. 8, 73-79, March 1967
Copyright © 1967 by Lipid Research, Inc.
Fels Research Institute and Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140
Fatty acid synthesis via the citrate cleavage pathway requires the continual replenishment of oxaloacetate within the mitochondria, probably by carboxylation of pyruvate.
Malic enzyme, although present in adipose tissue, is completely localized in the cytoplasm and has insufficient activity to support lipogenesis. Pyruvate carboxylase was found to be active in both the mitochondria and cytoplasm of epididymal adipose tissue cells; it was dependent on both ATP and biotin. Alteractions in dietary conditions induced no significant changes in mitochondrial pyruvate carboxylase activity, but the soluble activity was depressed in fat-fed animals.
The possible importance of the soluble activity in lipogenesis lies in its participation in a soluble malate transhydrogenation cycle with NAD malate dehydrogenase and malic enzyme, whereby a continual supply of NADPH is produced. Consequently, the pyruvate carboxylase in adipose tissue both generates mitochondrial oxaloacetate for the citrate cleavage pathway and supplies soluble NADPH for the conversion of acetyl-CoA to fatty acid.
Supplementary key words pyruvate carboxylase • adipose tissue • rat • intracellular distribution • dietary changes • oxaloacetate formation • lipogenesis
Submitted on August 10, 1966
Accepted on October 20, 1966
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