Measuring Ca2+-dependent Ca2+-uptake activity in the mouse heart
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Optical Mapping of Action Potentials and Calcium Transients in the Mouse Heart
Published on: September 13, 2011
Tine Holemans1, Ilse Vandecaetsbeek1, Frank Wuytack1
1Laboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven, B3000 Leuven, Belgium.
Abstract:
The apparent Ca(2+) affinity of the isoforms of the sarco/endoplasmic reticulum Ca(2+) ATPase SERCA2 is controlled primarily by two proteins, phospholamban (PLB) and sarcolipin (SLN). The rate of ATP-driven Ca(2+) uptake into sarcoplasmic reticulum (SR)-derived vesicles can be monitored by a technique in which the net uptake of (45)Ca(2+) in the form of an intravesicular calcium oxalate precipitate is recorded. Here, we present details of a modification of such a protocol for determining the apparent Ca(2+) affinity of the Ca(2+) pump, and its control by various regulators, in crude homogenates of mouse heart.
