Basal Heat Capacity of Skinned Skeletal Muscle with Selective Removal and Denaturation of Myoproteins: A Study with Differential Scanning Calorimetry

TL;DR

This study uses differential scanning calorimetry to investigate how proteins in muscle tissue affect heat capacity, finding that actin contributes significantly to thermal buffering.

Contribution

The paper identifies actin as a key contributor to basal heat capacity in skinned skeletal muscle, revealing its role in thermal buffering.

Findings

Actin contributes to an extra basal heat capacity of 0.4 J K−1 (g evaporable weight)−1 in skinned muscle.

Myosin partially suppresses actin's thermal contribution under rigor conditions.

Non-freezing water molecules may be involved in the preserved basal heat capacity at sub-zero temperatures.

Abstract

The specific heat capacity of skinned muscle in an adhering rigor solution was studied with differential scanning calorimetry (DSC) heating runs to search for a heat sink in the sarcomere of the muscle. To elucidate the contribution of major myoproteins to heat capacity, myosin and actin were partially removed by high-KCl and gelsolin treatments, respectively. Differential heat denaturation of myosin (together with α-actinin) and actin was induced to confirm their contributions. On the DSC curve, aside from the endothermic peaks representing ice melting and protein denaturation, the steady baseline level showed a significant increase in basal heat capacity in the presence of skinned muscle compared to the rigor solution alone. In the physiological temperature range from 10 to 25 °C, untreated skinned muscle in the native state (non-denatured) introduced an extra basal heat capacity of 0.4 J K−1 (g evaporable weight)−1, which was diminished by both removing and denaturing actin and was additionally increased by removing myosin; myosin denaturation had little effect on the basal heat capacity. Based on these results, we considered actin to be the fundamental source of extra basal heat capacity, which was partly suppressed by the thermally stable region of myosin under rigor conditions. This extra basal heat capacity was roughly preserved at sub-zero temperatures, suggesting the involvement of non-freezing water molecules. The extra basal heat capacity may have contributed to thermal buffering during muscle function via actin-associated hydration. As a supplemental result, we found a small reversible endothermic peak around −21 °C, which was suppressed in the presence of skinned muscle. Heating beyond the denaturing temperatures reduced this suppression effect.

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