Differential Response of Liver and Kidney Adenine Nucleotide Translocase and Pyruvate Dehydrogenase Activity to Alloxan Diabetes
- 1 July 1983
- journal article
- research article
- Published by S. Karger AG in Enzyme
- Vol. 29 (1) , 15-20
- https://doi.org/10.1159/000469599
Abstract
Adenine nucleotide translocase (EC 3.6.1.3.), pyruvate dehydrogenase (active and total forms, EC 1.2.4.1) and the long chain acyl CoA content were measured in liver and kidney from normal and alloxan-diabetic rats. The long chain acyl CoA content was significantly increased in liver, but not in kidney, in the diabetic group. Adenine nucleotide translocase activity was decreased in liver and raised in the kidney of alloxan-diabetic rats relative to the control group. Pyruvate dehydrogenase (active) was inhibited to a similar degree in both tissues in diabetes. The results are discussed in the light of the possible regulatory role of long chain acyl CoA and the diverse metabolic demands of the two tissues in diabetes.Keywords
This publication has 3 references indexed in Scilit:
- Interrelationship in the Regulation of Pyruvate Dehydrogenase and Adenine-Nucleotide Translocase by Palmitoyl-CoA in Isolated MitochondriaEuropean Journal of Biochemistry, 1977
- Appearance of Energy Conservation System in Rat Liver Mitochondria during DevelopmentThe Role of Adenine Nucleotide TranslocationThe Journal of Biochemistry, 1973
- Metabolic Control of Enzymes Involved in Lipogenesis and Gluconeogenesis*Biochemistry, 1964