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J Biol Chem, Vol. 275, Issue 19, 14476-14481, May 12, 2000

Absence of the gamma  Subunit of the Skeletal Muscle Dihydropyridine Receptor Increases L-type Ca2+ Currents and Alters Channel Inactivation Properties*

Doris FreiseDagger , Brigitte HeldDagger , Ulrich WissenbachDagger , Alexander Pfeifer§, Claudia TrostDagger , Nina HimmerkusDagger , Uli SchweigDagger , Marc FreichelDagger , Martin Biel§, Franz Hofmann§, Markus Hoth, and Veit FlockerziDagger

From the Dagger  Institut für Pharmakologie und Toxikologie, Universität des Saarlandes, D-66421 Homburg, § Institut für Pharmakologie und Toxikologie, Technische Universität, D-80802 München, and  Institut für Physiologie, Universität des Saarlandes, D-66421 Homburg, Germany

In skeletal muscle the oligomeric alpha 1S, alpha 2/delta -1 or alpha 2/delta -2, beta 1, and gamma 1 L-type Ca2+ channel or dihydropyridine receptor functions as a voltage sensor for excitation contraction coupling and is responsible for the L-type Ca2+ current. The gamma 1 subunit, which is tightly associated with this Ca2+ channel, is a membrane-spanning protein exclusively expressed in skeletal muscle. Previously, heterologous expression studies revealed that gamma 1 might modulate Ca2+ currents expressed by the pore subunit found in heart, alpha 1C, shifting steady state inactivation, and increasing current amplitude. To determine the role of gamma 1 assembled with the skeletal subunit composition in vivo, we used gene targeting to establish a mouse model, in which gamma 1 expression is eliminated. Comparing litter-matched mice with control mice, we found that, in contrast to heterologous expression studies, the loss of gamma 1 significantly increased the amplitude of peak dihydropyridine-sensitive ICa in isolated myotubes. Whereas the activation kinetics of the current remained unchanged, inactivation of the current was slowed in gamma 1-deficient myotubes and, correspondingly, steady state inactivation of ICa was shifted to more positive membrane potentials. These results indicate that gamma 1 decreases the amount of Ca2+ entry during stimulation of skeletal muscle.

* This work was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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