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ORIGINAL RESEARCH article

Front. Cardiovasc. Med.

Sec. Heart Failure and Transplantation

Effects of cooling on pig heart excitation and contraction

  • 1. Lunds universitet Institutionen for kliniska vetenskaper Lund, Lund, Sweden

  • 2. Lunds universitet Fysiska institutionen, Lund, Sweden

  • 3. German Electron Synchrotron, Helmholtz Association of German Research Centres (HZ), Hamburg, Germany

  • 4. Lunds Tekniska Hogskola, Lund, Sweden

  • 5. MAX IV-laboratoriet, Lund, Sweden

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Abstract

Although variations in temperature have a profound impact on cardiac function, little is known regarding the excitation and contractile parameters over a broad temperature interval. In view of the clinical implications of lowered temperature in resuscitation and in cardiac preservation/evaluation for transplantation, we have examined the contractile function using Langendorff perfused hearts and isolated trabecular muscle from pig, in combination with electrophysiology and X-ray diffraction. Lowered temperature in the range 37 to 22oC was associated with an increase in systolic pressure and active force. In permeabilized preparations, force and Ca2+ sensitivity decreased with temperature, showing that the increased force down to 22oC in the intact heart and trabeculae was not due to changes in thin filament regulation, but most likely to increased activator [Ca2+]. At lower temperature (<22oC), force of the heart decreased, suggesting that the temperature effects in the regulatory system became dominating. ECG analysis showed that frequency was lowered and that PQ-, QS-and QT-times were prolonged at lower temperature. This was associated with a gradual depolarization of the cell membrane, prolonged action potential and an attenuation of the fast upstroke phase. These changes in rise time and amplitude of the action potential would predispose for uneven propagation and arrhythmia as temperature is lowered. At the same time, the prolonged action potential can be associated with an increased [Ca2+] at lower temperature. Small angle X-ray diffraction showed that the filament lattice of intact trabecular muscle tended to swell at low temperature (10 vs 22oC) and revealed a mass transfer from myosin to actin filaments, which would reflect changes in cellular physiology and contractile system structure at low temperature.

Summary

Keywords

Electrophysiology, Hypothermia, Langendorff, Skinned fibers, X-Ray Diffraction

Received

24 November 2025

Accepted

12 February 2026

Copyright

© 2026 Li, Persson, Schwartzkopf, Steen, Terry, Wohlfart, Steen and Arner. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Anders Arner

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