Mitochondrial Acyl-CoA, adenine nucleotide translocase activity and oxidative phosphorylation in myocardial ischaemia
Date
1981
Authors
Lochner A.
Van Niekerk I.
Kotze J.C.N.
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Abstract
The hypothesis that inhibition of mitochondrial adenine nucleotide translocase activity by accumulation of long chain acyl-CoA esters might be responsible for the depression in mitochondrial energy metabolism in myocardial ischaemia was reinvestigated. Hypoxic, low flow perfusion (substrate free) of the isolated rat heart resulted in increases in tissue and mitochondrial acyl-CoA contents together with a reduction in adenine nucleotide translocase activity and oxidative phosphorylation function of mitochondria isolated from the tissue. Addition of exogenous substrates together with insulin or propranolol to the perfusate (glucose and insulin; glucose, glycerol and insulin; glucose, propranolol and insulin) caused significant further increases in tissue and mitochondrial acyl-CoA contents. In contrast, the mitochondrial adenine nucleotide translocase activity and oxidative phosphorylation function improved and were similar to those of control perfused hearts. The difference between the in vivo and in vitro effects of acyl-CoA on mitochondrial adenine and nucleotide translocase and oxidative phosphorylation could be due to in vivo binding to intracellular fatty acid binding proteins.
Description
Keywords
acyl coenzyme a, adenine nucleotide translocase, enzyme, potassium cyanide, radioisotope, adenosine triphosphate c 14, animal experiment, heart, heart mitochondrion, heart muscle, heart muscle ischemia, ischemia, mitochondrion, oxidative phosphorylation, rat, regional perfusion, Acyl Coenzyme A, Animal, Coronary Disease, Female, Heart, Insulin, Mitochondria, Heart, Mitochondrial ADP, ATP Translocases, Nucleotidyltransferases, Oxidative Phosphorylation, Oxygen Consumption, Perfusion, Propranolol, Rats, Rats, Inbred Strains
Citation
Journal of Molecular and Cellular Cardiology
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11
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