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Originally published In Press as doi:10.1074/jbc.C901008199 on March 24, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16134-16138, May 26, 2000
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ACCELERATED PUBLICATION
Involvement of Calmodulin in 1alpha ,25-Dihydroxyvitamin D3 Stimulation of Store-operated Ca2+ Influx in Skeletal Muscle Cells*

Guillermo Vazquez, Ana Russo de Boland, and Ricardo L. BolandDagger

From the Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur, San Juan 670, 8000 Bahía Blanca, Argentina

The steroid hormone 1alpha ,25-dihydroxyvitamin D3 (1,25-(OH)2D3) rapidly modulates Ca2+ homeostasis in avian skeletal muscle cells by driving a complex signal transduction mechanism, which promotes Ca2+ release from inner stores and cation influx from the outside through both L-type and store-operated Ca2+ (SOC) channels. In the present work, we evaluated the involvement of calmodulin (CAM) in 1,25-(OH)2D3 regulation of SOC influx in chick skeletal muscle cells. Treatment with 10-9 M 1,25-(OH)2D3 in Ca2+-free medium resulted in a rapid but transient Ca2+ rise correlated with the sterol-induced inositol 1,4,5-trisphosphate (IP3) production. The SOC influx stimulated by the hormone was insensitive to both CAM antagonists (fluphenazine, trifluoperazine, chlorpromazine, compound 48/80) and the CAM-dependent protein kinase II (CAMKII) inhibitor KN-62 when added after the sterol-dependent Ca2+ transient, but it was completely abolished when added prior to the IP3-induced mobilization of Ca2+ from endogenous stores. Moreover, in cells microinjected with antisense oligonucleotides directed against the CAM mRNA the sterol-stimulated SOC influx was reduced up to 60% respect to uninjected cells. The present results suggest that the 1,25-(OH)2D3-induced (IP3-mediated) cytosolic Ca2+ transient is required for CAM, activation which in turn activates SOC influx in a mechanism that seems to include CAMKII.

* This research was supported by grants from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Agencia Nacional de Promoción Científica y Tecnológica, and Comisión de Investigaciones Científicas de la Provincia de Buenos Aires (Argentina).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.

Dagger To whom correspondence should be addressed. Tel.: 4-291-4595100; Fax: 54-291-4595130; E-mail: rboland@criba.edu.ar.

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