Oxalate synthesis from [14C1]glycollate and [14C1]glyoxylate in the hepatectomized rat.

Hepatectomy significantly altered the metabolism of [1-14C]glyoxylate and [1-14C]glycollate in the rat. The production of 14CO2 was reduced by 47% and 77-86%, respectively, indicating the involvement of the liver in the oxidation of both substrates. Unidentified intermediates, assumed to be primarily glycine, serine and ethanolamine, were also reduced by over 50%, as would be expected from the removal of the aminotransferase enzymes through the hepatectomy. The biosynthesis of [14C]oxalate from [1-14C]glycollate was reduced by more than 80% in the hepatectomized rat. This suggests that this oxidation is primarily catalyzed by the liver enzymes, glycolic acid oxidase and glycolic acid dehydrogenase, in the intact rat. The limited formation of [14C]oxalate from [14C1]glycollate observed in the hepatectomized rat is probably catalyzed by lactate dehydrogenase or extrahepatic glycolic acid oxidase. Hepatectomy did not significantly alter the rate of formation of [14C]oxalate from [14C1]glyoxylate. However, since saturating concentrations of glyoxylate could not be used because of the toxicity of this substrate, the involvement of glycollic acid oxidase in this oxidation reaction in the intact rat can not be ruled out. In the hepatectomized rat, lactate dehydrogenase appears to be the enzyme making the major contribution, although other as yet not identified enzymes may be contributing. The increased deposition of oxalate in the tissues, oxalosis, may result from the shift in oxalate synthesis from the liver to the extrahepatic tissues.