The operation of the malate-aspartate shuttle in the reoxidation of glycolytic NADH in slices of fetal rat liver.
Lactate production by liver slices from fetal rats (17th--18th day of gestation) is enhanced about two fold by aminooxyacetate, an inhibitor of aspartate transaminase (EC 2.6.1.1). Such an effect is consistent with an increase of the cytosolic NAD-redox state owing to the parallel fall in the pyruvate level, whereas the glycolytic flux does not seem to be influenced appreciably. Indeed, although the inhibitor causes a marked increase of fructose 1,6-diphosphate, glucose-6-phosphate decreases only slightly. These results suggest that in fetal rat liver the malate-aspartate shuttle is operative in the reoxidation of cytosolic NADH produced during aerobic glycolysis.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000332:Aerobiosis; D000625:Aminooxyacetic Acid / Q000494:pharmacology; D000818:Animals; D001224:Aspartic Acid / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D005333:Fetus / Q000378:metabolism; D006019:Glycolysis; D066298:In Vitro Techniques; D007773:Lactates / Q000096:biosynthesis; D008099:Liver / Q000378:metabolism*; D008293:Malates / Q000378:metabolism*; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats
D007773:Lactates; D008293:Malates; D009243:NAD; D000625:Aminooxyacetic Acid; D001224:Aspartic Acid; D000255:Adenosine Triphosphate