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A Semi-Automated and Reproducible Biological-Based Method to Quantify Calcium Deposition In Vitro

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Calcium Uptake in Crude Tissue Preparation.

Philip A Bidwell¹, Evangelia G Kranias²

¹Department of Pharmacology and Cell Biophysics, College of Medicine, University of Cincinnati, 231 Albert Sabin Way, Cincinnati, OH, 45267-0575, USA.

Methods in Molecular Biology (Clifton, N.J.)

|December 24, 2015

Summary

This study details a method to measure sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) activity. The protocol quantifies Ca(2+) uptake rates, aiding research into SERCA function and regulation.

Keywords:

45Ca Calcium affinity Calcium uptake K m Oxalate Phospholamban SERCA Sarcolipin V max

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Area of Science:

Biochemistry
Molecular Biology
Physiology

Background:

Sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) pumps are crucial for cellular calcium homeostasis.
SERCA activity is modulated by regulatory proteins like phospholamban and sarcolipin in certain tissues.
Understanding SERCA kinetics, including Ca(2+) affinity and maximal velocity, is vital for physiological research.

Purpose of the Study:

To present a reliable and adaptable protocol for measuring SERCA activity.
To enable the characterization of SERCA's apparent affinity for Ca(2+) and maximal enzymatic velocity.
To provide a method applicable to various tissues, animal models, and cell cultures.

Main Methods:

Measurement of oxalate-facilitated (45)Ca uptake into the sarcoplasmic reticulum (SR).
Utilizing crude mouse ventricular homogenates for SR isolation.
Quantification of Ca(2+) uptake rates to determine kinetic parameters.

Main Results:

The described protocol effectively determines the apparent affinity for Ca(2+) and maximal enzymatic velocity of SERCA.
The method allows for quantitative assessment of SERCA activity in SR preparations.
The protocol's adaptability across different biological samples was demonstrated.

Conclusions:

The presented protocol offers a robust method for assessing SERCA enzyme kinetics.
This technique facilitates the study of SERCA function and its regulation by binding partners.
The protocol's versatility supports broad applications in calcium signaling and muscle physiology research.