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Originally published In Press as doi:10.1074/jbc.M209900200 on October 10, 2002

J. Biol. Chem., Vol. 277, Issue 52, 50776-50779, December 27, 2002
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Cardiac-specific Expression of Calcineurin Reverses Embryonic Lethality in Calreticulin-deficient Mouse*

Lei GuoDagger §, Kimitoshi NakamuraDagger , Jeffery LynchDagger ||, Michal Opas**, Eric N. OlsonDagger Dagger , Luis B. Agellon§§¶¶, and Marek MichalakDagger ||||

From the Dagger  Canadian Institutes of Health Research Membrane Protein Research Group, §§ Canadian Institutes of Health Research Molecular and Cell Biology of Lipids Research Group, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada, ** Department of Pathology and Laboratory Medicine, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and the Dagger Dagger  Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148

Calreticulin is an endoplasmic reticulum resident Ca2+-binding chaperone. The importance of the protein is illustrated by embryonic lethality because of impaired cardiac development in calreticulin-deficient mice. The molecular details underlying this phenotype are not understood. In this study, we show that overexpression of activated calcineurin reverses the defect in cardiac development observed in calreticulin-deficient mice and rescues them from embryonic lethality. The surviving mice show no defect in cardiac development but exhibited growth retardation, hypoglycemia, increased levels of serum triacylglycerols, and cholesterol. Reversal of embryonic lethality because of calreticulin deficiency by activated calcineurin underscores the impact of the calreticulin-calcineurin functions on the Ca2+-dependent signaling cascade during early cardiac development. These findings show that calreticulin and calcineurin play fundamental roles in Ca2+-dependent pathways essential for normal cardiac development and explain the molecular basis for the rescue of calreticulin-deficient phenotype.

* This work was supported by the Canadian Institutes of Health Research and the Heart and Stroke Foundation of Ontario.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.

§ Postdoctoral fellow of the Heart and Stroke Foundation of Canada.

Both authors contributed equally to this work.

|| Recipient of a Studentship from the Heart and Stroke Foundation of Canada and the Alberta Heritage Foundation for Medical Research.

¶¶ Alberta Heritage Foundation for Medical Research Senior Scholar.

|||| Canadian Institutes of Health Research Senior Investigator and a Medical Scientist of the Alberta Heritage Foundation for Medical Research. To whom correspondence should be addressed: Dept. of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Tel.: 780-492-2256; Fax: 780-492-0886; E-mail: Marek.Michalak@ualberta.ca.

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