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Volume 271, Number 29, Issue of July 19, 1996 pp. 17463-17468
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Phosphorylation of Chromogranin A and Catecholamine Secretion Stimulated by Elevation of Intracellular Ca²⁺ in Cultured Bovine Adrenal Medullary Cells

(Received for publication, August 31, 1995, and in revised form, February 27, 1996)

Nobuyuki Yanagihara , Yasuharu Oishi ^§ , Hideyuki Yamamoto ^§ , Masato Tsutsui ^¶ , Jun Kondoh , Tutomu Sugiura ^'' , Eishichi Miyamoto ^§ and Futoshi Izumi

From the Departments of Pharmacology and ^'' Immunology and the ^¶ 2nd Department of Internal Medicine, University of Occupational and Environmental Health, School of Medicine, Kitakyushu 807, the ^§ Department of Pharmacology, Kumamoto University School of Medicine, Kumamoto 860, and the  Mitsubishi Kagaku Corporation Research Center, Yokohama 224, Japan

We have recently isolated a new endogenous substrate of 70 kDa for Ca²⁺/calmodulin-dependent protein kinase II (CaM kinase II) from bovine adrenal medullary cells (Yanagihara, N., Toyohira, Y., Yamamoto, H., Ohta, Y., Tsutsui, M., Miyamoto, E., and Izumi, F. (1994) Mol. Pharmacol. 46, 423-430). Here we report the sequence analysis of the 70-kDa protein and examine its phosphorylation by various protein kinases in vitro and by depolarization of the cultured cells. Protein sequencing and immunoblotting revealed that the 70-kDa protein is chromogranin A (CgA) or a closely related protein. Partially purified CgA was phosphorylated by cyclic AMP-dependent protein kinase and protein kinase C as well as CaM kinase II. Tryptic phosphopeptide mapping patterns of CgA differed among these protein kinases. In ³²P-labeled bovine adrenal medullary cells, 56 mM K⁺ increased the phosphorylation of CgA and catecholamine secretion in similar time- and concentration-dependent manners, both of which were inhibited by 20 mM MgSO₄, an inhibitor of voltage-dependent Ca²⁺ channels. These findings suggest that CgA serves as a substrate for several multifunctional protein kinases and that the elevation of the intracellular Ca²⁺ stimulates the phosphorylation of CgA associated with catecholamine secretion in cultured adrenal medullary cells.

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