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Originally published In Press as doi:10.1074/jbc.M002041200 on September 5, 2000

J. Biol. Chem., Vol. 275, Issue 47, 36676-36682, November 24, 2000
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Calreticulin Modulates Capacitative Ca2+ Influx by Controlling the Extent of Inositol 1,4,5-Trisphosphate-induced Ca2+ Store Depletion*

Wen XuDagger , Frank J. Longo§, Mary R. Wintermantel, Xueying JiangDagger , Robert A. Clark||, and Sylvain DeLisleDagger **

From the Dagger  Veterans Affairs Medical Center and Departments of Medicine and Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201, the § Department of Anatomy,  University of Iowa College of Medicine, Iowa City, Iowa 52242, and the || Department of Medicine, South Texas Veterans Health Care System and University of Texas Health Science Center, San Antonio, Texas 78230

Calreticulin (CRT) is a highly conserved Ca2+-binding protein that resides in the lumen of the endoplasmic reticulum (ER). We overexpressed CRT in Xenopus oocytes to determine how it could modulate inositol 1,4,5-trisphosphate (InsP3)-induced Ca2+ influx. Under conditions where it did not affect the spatially complex elevations in free cytosolic Ca2+ concentration ([Ca2+]i) due to InsP3-induced Ca2+ release, overexpressed CRT decreased by 46% the Ca2+-gated Cl- current due to Ca2+ influx. Deletion mutants revealed that CRT requires its high capacity Ca2+-binding domain to reduce the elevations of [Ca2+]i due to Ca2+ influx. This functional domain was also required for CRT to attenuate the InsP3-induced decline in the free Ca2+ concentration within the ER lumen ([Ca2+]ER), as monitored with a "chameleon" indicator. Our data suggest that by buffering [Ca2+]ER near resting levels, CRT may prevent InsP3 from depleting the intracellular stores sufficiently to activate Ca2+ influx.

* This work was supported by grants from the Department of Veterans Affairs (to S. D. and R. A. C.).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.

** Established Investigator at the American Heart Association. To whom correspondence should be addressed: Depts. of Medicine and Physiology, University of Maryland, 3B-185 Veterans Affairs Medical Center, 10 N. Greene St., Baltimore MD 21201. Tel.: 410-605-7000 (ext. 6449); Fax: 410-605-7957; E-mail: sdelisle@umaryland.edu.

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