Mitochondrial component of the phosphorylcreatine shuttle is enhanced during rat heart perinatal development.
Aerobic metabolism is enhanced during perinatal heart development in parallel with increased cardiac function. The mitochondrial component of the phosphorylcreatine shuttle is important in providing energy for contraction and was examined in weanling and adult rat left ventricle. Creatine kinase activity was enhanced in tissue homogenate and purified cardiac myocytes of adults. Mitochondrial analyses attribute this enhancement to increased creatine kinase activity per milligram mitochondrial protein. Other enzymatic markers of mitochondrial function are not enhanced in activity during perinatal heart growth. The unique response of creatine kinase points to the shuttle mechanism and of mitochondrial creatine kinase, in particular, as a major contributor to heart functional regulation.
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000367:Age Factors; D000818:Animals; D002950:Citrate (si)-Synthase / Q000378:metabolism; D003402:Creatine Kinase / Q000378:metabolism; D006321:Heart / Q000254:growth & development*; D008291:Malate Dehydrogenase / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology*; D010725:Phosphocreatine / Q000378:metabolism*; D051381:Rats
D010725:Phosphocreatine; D015094:3-Hydroxyacyl CoA Dehydrogenases; D008291:Malate Dehydrogenase; D002950:Citrate (si)-Synthase; D003402:Creatine Kinase; D000251:Adenosine Triphosphatases