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Originally published In Press as doi:10.1074/jbc.M206470200 on November 11, 2002

J. Biol. Chem., Vol. 278, Issue 3, 1663-1670, January 17, 2003
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PAC1 Receptor Activation by PACAP-38 Mediates Ca2+ Release from a cAMP-dependent Pool in Human Fetal Adrenal Gland Chromaffin Cells*

Marcel D. PayetDagger §, Lyne BilodeauDagger , Lyne Breault||, Alain Fournier**, Laurent YonDagger Dagger , Hubert VaudryDagger Dagger , and Nicole Gallo-PayetDagger §§

From the Dagger  Department of Physiology and Biophysics,  Service of Endocrinology, Department of Medicine, Faculty of Medicine, University of Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada, ** Institut National de la Recherche Scientifique Santé, University of Quebec, Pointe-Claire, Quebec H9R 1G6, Canada, and the Dagger Dagger  European Institute for Peptide Research (IFRMP 23), Laboratory of Cellular and Molecular Neuroendocrinology, INSERM U413, UA CNRS, University of Rouen, Mont-Saint-Aignan 76821, France

Previous studies have shown that human fetal adrenal gland from 17- to 20-week-old fetuses expressed pituitary adenylate cyclase-activating polypeptide (PACAP) receptors, which were localized on chromaffin cells. The aim of the present study was to identify PACAP receptor isoforms and to determine whether PACAP can affect intracellular calcium concentration ([Ca2+]i) and catecholamine secretion. Using primary cultures and specific stimulation of chromaffin cells, we demonstrate that PACAP-38 induced an increase in [Ca2+]i that was blocked by PACAP (6-38), was independent of external Ca2+, and originated from thapsigargin-insensitive internal stores. The PACAP-triggered Ca2+ increase was not affected by inhibition of PLCbeta (preincubation with U-73122) or by pretreatment of cells with Xestospongin C, indicating that the inositol 1,4,5-triphosphate-sensitive stores were not mobilized. However, forskolin (FSK), which raises cytosolic cAMP, induced an increase in Ca2+ similar to that recorded with PACAP-38. Blockage of PKA by H-89 or (Rp)-cAMPS suppressed both PACAP-38 and FSK calcium responses. The effect of PACAP-38 was also abolished by emptying the caffeine/ryanodine-sensitive Ca2+ stores. Furthermore, treatment of cells with orthovanadate (100 µM) impaired Ca2+ reloading of PACAP-sensitive stores indicating that PACAP-38 can mobilize Ca2+ from secretory vesicles. Moreover, PACAP induced catecholamine secretion by chromaffin cells. It is concluded that PACAP-38, through the PAC1 receptor, acts as a neurotransmitter in human fetal chromaffin cells inducing catecholamine secretion, through nonclassical, recently described, ryanodine/caffeine-sensitive pools, involving a cAMP- and PKA-dependent phosphorylation mechanism.

* This work was supported in part by the Canadian Institute of Health Research (Grants MOP-37891 and MT-6813 to N. G. P. and M. D. P.) and by a France-Quebec Exchange Program with Hubert Vaudry.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.

§ To whom correspondence should be addressed: Dept. of Physiology and Biophysics, Faculty of Medicine, University of Sherbrooke, 3001 12th Ave. North, Sherbrooke, Quebec J1H 5N4, Canada. Tel.: 819-564-5305; Fax: 819-564-5399; E-mail: Marcel.Payet@USherbrooke.ca.

|| A recipient of a studentship from the Medical Research Council of Canada.

§§ Holder of The Canadian Research Chair in Endocrinology of the Adrenal Gland.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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