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Updated: Apr 26, 2026

Optical Mapping of Action Potentials and Calcium Transients in the Mouse Heart

Optical Mapping of Action Potentials and Calcium Transients in the Mouse Heart

Published on: September 13, 2011

Measuring Ca2+-dependent Ca2+-uptake activity in the mouse heart.

Tine Holemans¹, Ilse Vandecaetsbeek¹, Frank Wuytack¹

¹Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, B3000 Leuven, Belgium.

Cold Spring Harbor Protocols

|August 3, 2014

Summary

Researchers modified a method to measure calcium affinity in mouse heart tissue. This technique helps understand how proteins like phospholamban and sarcolipin regulate the SERCA2 calcium pump.

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Area of Science:

Biochemistry
Molecular Biology
Cardiovascular Physiology

Background:

The sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA2) pump is crucial for cardiac muscle relaxation by removing calcium from the cytoplasm.
The activity of SERCA2 is modulated by regulatory proteins, primarily phospholamban (PLB) and sarcolipin (SLN), affecting calcium affinity.
Understanding these regulatory mechanisms is vital for comprehending cardiac function and dysfunction.

Purpose of the Study:

To present a modified protocol for determining the apparent Ca(2+) affinity of SERCA2.
To assess the influence of regulatory proteins (PLB and SLN) on SERCA2 activity in mouse heart homogenates.
To provide a reliable method for studying SERCA2 regulation in crude tissue preparations.

Main Methods:

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Published on: September 7, 2014

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Last Updated: Apr 26, 2026

Optical Mapping of Action Potentials and Calcium Transients in the Mouse Heart

Optical Mapping of Action Potentials and Calcium Transients in the Mouse Heart

Published on: September 13, 2011

Measuring Fast Calcium Fluxes in Cardiomyocytes

Measuring Fast Calcium Fluxes in Cardiomyocytes

Published on: November 29, 2011

Isolation and Physiological Analysis of Mouse Cardiomyocytes

Isolation and Physiological Analysis of Mouse Cardiomyocytes

Published on: September 7, 2014

Utilized a modified radioactive tracer technique involving the measurement of (45)Ca(2+) uptake.

The uptake was quantified by the formation of an intravesicular calcium oxalate precipitate in sarcoplasmic reticulum (SR)-derived vesicles.

Applied the protocol to crude homogenates of mouse heart tissue.

Main Results:

Successfully adapted a protocol to measure the apparent Ca(2+) affinity of the SERCA2 calcium pump.
The modified method is suitable for analyzing SERCA2 regulation by proteins like PLB and SLN in complex biological samples.
Demonstrated the feasibility of using crude mouse heart homogenates for these measurements.

Conclusions:

The presented modified protocol offers a robust approach for investigating SERCA2 function and its regulation.
This method facilitates the study of factors influencing calcium handling in the heart.
Provides a valuable tool for cardiovascular research, particularly in understanding SERCA2-mediated calcium transport.