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J. Biol. Chem., Vol. 279, Issue 1, 547-555, January 2, 2004

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Calcium-binding Protein 1 Is an Inhibitor of Agonist-evoked, Inositol 1,4,5-Trisphosphate-mediated Calcium Signaling^*

Lee P. Haynes, Alexei V. Tepikin, and Robert D. Burgoyne

From the Physiological Laboratory, Crown Street, University of Liverpool, Liverpool L69 3BX, United Kingdom

Intracellular calcium signals are responsible for initiating a spectrum of physiological responses. The caldendrins/calcium-binding proteins (CaBPs) represent mammal-specific members of the CaM superfamily. CaBPs display a restricted pattern of expression in neuronal/retinal tissues, suggesting a specialized role in Ca²⁺ signaling in these cell types. Recently, it was reported that a splice variant of CaBP1 functionally interacts with inositol 1,4,5-trisphosphate (InsP₃) receptors to elicit channel activation in the absence of InsP₃ (Yang, J., McBride, S., Mak, D.-O. D., Vardi, N., Palczewski, K., Haeseleer, F., and Foskett, J. K. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 7711–7716). These data indicate a new mode of InsP₃ receptor modulation and hence control of intracellular Ca²⁺ concentration ([Ca²⁺]_i) in neuronal tissues. We have analyzed the biochemistry of the long form splice variant of CaBP1 (L-CaBP1) and show that, in vitro, a recombinant form of the protein is able to bind Ca²⁺ with high affinity and undergo a conformational change. We also describe the localization of endogenous and overexpressed L-CaBP1 in the model neuroendocrine PC12 cell system, where it was associated with the plasma membrane and Golgi complex in a myristoylation-dependent manner. Furthermore, we show that overexpressed L-CaBP1 is able to substantially suppress rises in [Ca²⁺]_i in response to physiological agonists acting on purinergic receptors and that this inhibition is due in large part to blockade of release from intracellular Ca²⁺ stores. The related protein neuronal calcium sensor-1 was without effect on the [Ca²⁺]_i responses to agonist stimulation. Measurement of [Ca²⁺] within the ER of permeabilized PC12 cells demonstrated that LCaBP1 directly inhibited InsP₃-mediated Ca²⁺ release. Expression of L-CaBP1 also inhibited histamine-induced [Ca²⁺]_i oscillations in HeLa cells. Together, these data suggest that L-CaBP1 is able to specifically regulate InsP₃ receptor-mediated alterations in [Ca²⁺]_i during agonist stimulation.

Received for publication, August 29, 2003 , and in revised form, October 7, 2003.

^* This work was supported by grants from the Wellcome Trust (to R. D. B.) and the Medical Research Council (A. V. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two additional figures.

To whom all correspondence should be addressed. Tel.: 44-151-794-5305; Fax: 44-151-794-5337; E-mail: burgoyne{at}liverpool.ac.uk.

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