ArticleEuropean biophysics journal : EBJ2008
Is the Ca2+-ATPase from sarcoplasmic reticulum also a heat pump?
Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- Natural bioactive compounds and their mechanisms of action in the management of obesity: a narrative review.Frontiers in nutrition · 2025Review
- Isolation of the Sarcoplasmic Reticulum CaMethods and protocols · 2023Article
- Recent advancements in pharmacological strategies to modulate energy balance for combating obesity.RSC medicinal chemistry · 2023Review
- Is Upregulation of Sarcolipin Beneficial or Detrimental to Muscle Function?Frontiers in physiology · 2021Article
- Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- The role of skeletal-muscle-based thermogenic mechanisms in vertebrate endothermy.Biological reviews of the Cambridge Philosophical Society · 2015Review
- Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals.Nature medicine · 2012Article
- On the thermodynamic efficiency of Ca²⁺-ATPase molecular machines.Biophysical journal · 2012Article
- Kinetic and mesoscopic non-equilibrium description of the Ca(2+) pump: a comparison.European biophysics journal : EBJ · 2012Article
- Coefficients for active transport and thermogenesis of Ca2+-ATPase isoforms.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We calculate, using the first law of thermodynamics, the membrane heat fluxes during active transport of Ca(2+) in the Ca(2+)-ATPase in leaky and intact vesicles, during ATP hydrolysis or synthesis conditions. The results show that the vesicle interior may cool down during hydrolysis and Ca(2+)-uptake, and heat up during ATP synthesis and Ca(2+)-efflux. The heat flux varies with the SERCA isoform. Electroneutral processes and rapid equilibration of water were assumed. The results are consistent with the second law of thermodynamics for the overall processes. The expression for the heat flux and experimental data, show that important contributions come from the enthalpy of hydrolysis for the medium in question, and from proton transport between the vesicle interior and exterior. The analysis give quantitative support to earlier proposals that certain, but not all, Ca(2+)-ATPases, not only act as Ca(2+)-pumps, but also as heat pumps. It can thus help explain why SERCA 1 type enzymes dominate in tissues where thermal regulation is important, while SERCA 2 type enzymes, with their lower activity and better ability to use the energy from the reaction to pump ions, dominate in tissues where this is not an issue.
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