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Volume 271, Number 48, Issue of November 29, 1996 pp. 30816-30822
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Expression of the Plasma Membrane Ca²⁺-ATPase in Myogenic Cells

(Received for publication, June 14, 1996, and in revised form, August 30, 1996)

Annette Hammes , Silke Oberdorf-Maass , Susanne Jenatschke , Theo Pelzer , Alexander Maass , Frank Gollnick , Rainer Meyer , Jörn Afflerbach and Ludwig Neyses

From the Department of Medicine, University of Würzburg, D-97080 Würzburg and the  Department of Physiology, University of Bonn, D-53111 Bonn, Germany

To study the physiological function of the plasma membrane calmodulin-dependent calcium ATPase (PMCA) in intact cells, L6 myogenic cell lines stably overexpressing the human PMCA isoform 4CI (= human PMCA isoform 4b) were generated. Several independent L6 clones and controls stably transfected with the empty expression vector were analyzed in detail. The resting cytosolic calcium level in hPMCA4CI-overexpressing muscle cells (measured by the Fura-2 method) was significantly reduced by 20-30% compared with controls. This was shown in a cytosolic window of 1322 single cells (p < 0.01). Furthermore, the differentiation process of these cells was remarkably accelerated compared with control myoblasts and parental nontransfected L6 cells as assessed by multinucleated myotube formation and creatine phosphokinase activity elevation. After 4 and 6 days of differentiation, PMCA-overexpressing L6 cells from four independent clones displayed a 3- and 4-fold higher creatine phosphokinase activity compared with controls (n = 5, p < 0.02). These results may extend the concept of the function of the PMCA from simple prevention of calcium overload to an active involvement in intracellular calcium regulation with potentially important consequences for cellular functions.

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