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J Biol Chem, Vol. 273, Issue 28, 17381-17385, July 10, 1998

Diversity of Calcium Signaling by Metabotropic Glutamate Receptors

Shigeki KawabataDagger , Atsuyuki Kohara§, Rie Tsutsumi§, Hirotsune Itahana, Satoshi Hayashibe, Tokio Yamaguchi§, and Masamichi Okada§

From the Dagger  Molecular Medicine Laboratory, § Neuroscience Research Laboratory, and  Chemistry Laboratory, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., Ibaraki 305, Japan

During prolonged application of glutamate (20 min), patterns of increase in intracellular Ca2+ concentration ([Ca2+]i) were studied in HEK-293 cells expressing metabotropic glutamate receptor, mGluR1alpha or mGluR5a. Stimulation of mGluR1alpha induced an increase in [Ca2+]i that consisted of an initial transient peak with a subsequent steady plateau or an oscillatory increase in [Ca2+]i The transient phase was largely attributed to Ca2+ mobilization from the intracellular Ca2+ stores, but the sustained phase was solely due to Ca2+ influx through the mGluR1alpha receptor-operated Ca2+ channel. Prolonged stimulation of mGluR5a continuously induced [Ca2+]i oscillations through mobilization of Ca2+ from the intracellular Ca2+ stores. Studies on mutant receptors of mGluR1alpha and mGluR5a revealed that the coupling mechanism in the sustained phase of Ca2+ response is determined by oscillatory/non-oscillatory patterns of the initial Ca2+ response but not by the receptor identity. In mGluR1alpha -expressing cells, activation of protein kinase C selectively desensitized the pathway for intracellular Ca2+ mobilization, but the mGluR1alpha -operated Ca2+ channel remained active. In mGluR5a-expressing cells, phosphorylation of mGluR5a by protein kinase C, which accounts for the mechanism of mGluR5a-controlled [Ca2+]i oscillations, might prevent desensitization and result in constant oscillatory mobilization of Ca2+ from intracellular Ca2+ stores. Our results provide a novel concept in which oscillatory/non-oscillatory mobilizations of Ca2+ induce different coupling mechanisms during prolonged stimulation of mGluRs.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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