Thermal dependence of cardiac SR Ca2+-ATPase from fish and mammals

The thermal sensitivity of metabolic performance in vertebrates requires a better understanding of the temperature sensitivity of cardiac function. The cardiac sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2) is vital for excitation-contraction (E-C) coupling and intracellular Ca2+ homeostasis in heart cells. To better understand the thermal dependency of cardiac output in vertebrates, we present comparative analyses of the thermal kinetics properties of SERCA2 from ectothermic and endothermic vertebrates. We directly compare SR ventricular microsomal preparations using similar experimental conditions from sarcoplasmic reticulum isolated from cardiac tissues of mammals and fish. The experiments were designed to delineate the thermal sensitivity of SERCA2 and its role in thermal sensitivity Ca2+ uptake and E-C coupling. Ca2+ transport in the microsomal SR fractions from rabbit and bigeye tuna (Thunnus obesus) ventricles were temperature dependent. In contrast, ventricular SR preparations from coho salmon (Onchorhychus kisutch) were less temperature dependent and cold tolerant, displaying Ca2+ uptake as low as 5 degrees C. As a consequence, the Q(10) values in coho salmon were low over a range of different temperature intervals. Maximal Ca2+ transport activity for each species occurred in a different temperature range, indicating species-specific thermal preferences for SERCA2 activity. The mammalian enzyme displayed maximal Ca2+ uptake activity at 35 degrees C, whereas the fish (tuna and salmon) had maximal activity at 30 degrees C. At 35 degrees C, the rate of Ca2+ uptake catalyzed by the bigeye tuna SERCA2 decreased, but not the rate of ATP hydrolysis. In contrast, the salmon SERCA2 enzyme lost its activity at 35 degrees C, and ATP hydrolysis was also impaired. We hypothesize that SERCA2 catalysis is optimized for species-specific temperatures experienced in natural habitats and that cardiac aerobic scope is limited when excitation-contraction coupling is impaired allow or high temperatures due to loss of SERCA2 enzymatic function. (C) 2012 Elsevier Ltd. All rights reserved.