Differential response of liver and kidney adenine nucleotide translocase and pyruvate dehydrogenase activity to alloxan diabetes. The possible regulatory role of long chain acyl CoA.
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.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D000226:Mitochondrial ADP, ATP Translocases / Q000378:metabolism*; D009713:Nucleotidyltransferases / Q000378:metabolism*; D009928:Organ Specificity; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D000214:Acyl Coenzyme A; D011768:Pyruvate Dehydrogenase Complex; D000226:Mitochondrial ADP, ATP Translocases; D009713:Nucleotidyltransferases