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Am J Physiol Cell Physiol (February 26, 2003). doi:10.1152/ajpcell.00377.2002
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Submitted on August 20, 2002
Accepted on February 11, 2003

Ca2+-transients activate calcineurin/NFATc1 and initiate fast-to-slow transformation in a primary skeletal muscle culture

Hans-Peter Kubis1*, Nina Hanke, Renate J Scheibe, Joachim D Meissner2, and Gerolf Gros2

1 Zentrum Physiologie, Medizinische Hochschule Hannover, Hannover, Germany
2 ; Zentrum Physiologie, Medizinische Hochschule Hannover, Hannover, Germany

* To whom correspondence should be addressed. E-mail: Kubis.HansP{at}MH-Hannover.de.

The calcineurin-NFATc1 signal transduction is involved in upregulating slow myosin heavy chain gene expression during fast-to-slow transformation of skeletal muscle cells. This study aims to investigate the Ca2+ signal necessary to activate the calcineurin-NFATc1 cascade in skeletal muscle. Electrostimulation of primary myocytes from rabbit for 24 h induced a distinct fast-to-slow transformation at the MHC mRNA level and a full activation of the calcineurin-NFATc1 pathway, although resting Ca2+ concentration ([Ca2+]i) remained unaltered at 70 nM. During activation, the calcium transients of these myocytes reach a peak concentration of ~500 nM. While 70 nM Ca2+i does not activate calcineurin-NFAT, we show by the use of Ca2+ ionophore that the system is fully activated when Ca2+i is >= 150 nM in a sustained manner. We conclude that the calcineurin signal transduction pathway and the slow MHC gene in cultured skeletal muscle cells are activated by repetition of the rapid high-amplitude calcium transients that are associated with excitation-contraction coupling, rather than by a sustained elevation of resting Ca2+ concentration.




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