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Originally published In Press as doi:10.1074/jbc.M201558200 on June 18, 2002

J. Biol. Chem., Vol. 277, Issue 34, 30738-30745, August 23, 2002
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Calcium and Calpain as Key Mediators of Apoptosis-like Death Induced by Vitamin D Compounds in Breast Cancer Cells*

Ida Stenfeldt MathiasenDagger §, Igor N. Sergeev, Lone Bastholm||, Folmer Elling||, Anthony W. Norman**, and Marja JäätteläDagger Dagger Dagger

From the Dagger  Apoptosis Laboratory, Danish Cancer Society, DK 2100 Copenhagen Ø, Denmark, the  Department of Chemistry and Biochemistry, South Dakota State University, Brookings, South Dakota 57006, the || Institute of Molecular Pathology, Faculty of Health Sciences, University of Copenhagen, DK 1353 Copenhagen K, Denmark, and the ** Department of Biochemistry, University of California, Riverside, California 92521

The active form of vitamin D3 (1,25(OH)2D3) induces an increase in the intracellular free calcium ([Ca2+]i) and caspase-independent cell death in human breast cancer cells. Here we show that the treatment of MCF-7 breast cancer cells with 1,25(OH)2D3 or its chemotherapeutic analog, EB 1089, releases Ca2+ from the endoplasmic reticulum. The increase in [Ca2+]i was associated with the activation of a calcium-dependent cysteine protease, µ-calpain. Interestingly, ectopic expression of a calcium-binding protein, calbindin-D28k, in MCF-7 cells not only attenuated the elevation in [Ca2+]i and calpain activation, but also reduced death triggered by vitamin D compounds. Similarly, the inhibition of calpain activity by structurally unrelated chemical inhibitors increased the survival of the cells and reduces the amount of annexin V-positive cells. Despite the complete absence of effector caspase activation, transmission electron microscopy of MCF-7 cells treated with 1,25(OH)2D3 or EB 1089 revealed apoptosis-like morphology characterized by the condensed cytoplasm, nuclei, and chromatin. Overall, these results suggest that calpain may take over the role of the major execution protease in apoptosis-like death induced by vitamin D compounds. Thus, these compounds may prove useful in the treatment of tumors resistant to therapeutic agents dependent on the classical caspase cascade.

* This work was supported by the Danish Medical Research Council, the Danish Cancer Society (to I. S. M. and M. J.), and by Grant CA67317 from the NCI, National Institutes of Health (to I. N. S.).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.

§ Present address: Molecular Biology, Novo Nordisk A/S, Bagsværd DK 2880, Denmark.

Dagger Dagger To whom correspondence should be addressed: Apoptosis Laboratory, Danish Cancer Society, Strandboulevarden 49, DK 2100 Copenhagen Ø, Denmark. Tel.: 45-35-257 318; Fax: 45-35-257-721; E-mail: mhj@biobase.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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