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Volume 272, Number 44, Issue of October 31, 1997 pp. 27694-27699
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Dynamics of [Ca²⁺] in the Endoplasmic Reticulum and Cytoplasm of Intact HeLa Cells
A COMPARATIVE STUDY

(Received for publication, July 29, 1997, and in revised form, August 28, 1997)

From the Departamento de Bioquímica y Biología Molecular y Fisiología, Instituto de Biologia y Genética Molecular, Facultad de Medicina, Universidad de Valladolid and Consejo Superior de Investigaciones Científicas, E-47005 Valladolid, Spain

We have measured the [Ca²⁺] in the endoplasmic reticulum ([Ca²⁺]_er) of intact HeLa cells at both 22 °C and 37 °C using endoplamsic reticulum-targeted, low Ca²⁺ affinity aequorin reconstituted with coelenterazine n. Aequorin consumption was much slower at 22 °C, and this allowed performing a much longer study of the dynamics of [Ca²⁺]_er. The steady-state [Ca²⁺]_er (500-600 µM) was not modified by the temperature, although both the rates of pumping and leak were decreased at 22 °C. The behavior of both [Ca²⁺]_er and cytoplasmic [Ca²⁺] ([Ca²⁺]_c) after the addition of increasing concentrations of agonists and/or Ca²⁺-ATPase inhibitors, or following incubation in Ca²⁺-free medium were compared. We show that agonists induce a fast but relatively small decrease in [Ca²⁺]_er, which is enough to produce a sharp increase in [Ca²⁺]_c. Termination of Ca²⁺ release is controlled by feedback inhibition of the inositol 1,4,5-trisphosphate receptors by [Ca²⁺]_c, a mechanism that appears to be designed to release the minimum amount of Ca²⁺ necessary to produced the required [Ca²⁺]_c signal. We also show that Ca²⁺ release is inhibited progressively when [Ca²⁺]_er decreases below a threshold of about 150 µM, even in the absence of Ca²⁺ pumping or [Ca²⁺]_c increase. This effect is consistent with a regulation of the inositol 1,4,5-trisphosphate-gated channels by [Ca²⁺]_er.

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