Plasma lactate dehydrogenase and pyruvate kinase activity changes with body mass and age across birds and mammals

Abstract

Birds and mammals produce most adenosine triphosphate (ATP) through mitochondrial oxidative phosphorylation, but when oxygen is not present in sufficient levels, ATP can be produced through anaerobic glycolysis. Pyruvate kinase (PK) catalyzes the final step of glycolysis by converting phosphoenolpyruvate and adenosine diphosphate (ADP) into pyruvate and ATP. Lactate dehydrogenase (LDH) is important for anaerobic glycolysis by catalyzing the conversion of pyruvate into lactate. In this study, we measured LDH and PK activities in plasma from birds and mammals in order to determine the relationship between LDH and PK with respect to body mass and age. Our results show that birds had a higher LDH and PK activity compared with mammals. There is a positive relationship between body mass and plasma LDH activity in birds only. However, this relationship disappears when the data are phylogenetically corrected. We did not observe a significant relationship between plasma LDH and age in birds or mammals. Plasma PK activity was negatively correlated with body mass in birds but not in mammals and positively associated with age in both birds and mammals. The relationship between LDH and PK with respect to body mass and age may be complex due to differences in metabolism in birds and mammals. Increases in LDH and PK activity with body mass in birds may be linked to anaerobic demands of flight, especially in larger birds. A decrease in LDH activity with age/MLSP (maximum lifespan) in mammals may reflect a differing metabolic shift as compared with birds. Increases in PK with age in both mammals and birds may help them cope with greater energetic needs as cells age.