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Cholinergic regulation of protein phosphorylation in bovine adrenal chromaffin cells



Cholinergic regulation of protein phosphorylation in bovine adrenal chromaffin cells



Proceedings of the National Academy of Sciences of the United States of America 85(5): 1677-1681



Chromaffin cells were isolated from bovine adrenal medullae and maintained in primary culture. After prelabeling with 32PO4, exposure of the chromaffin cells to acetylcholine increased the phosphorylation of a Mr .apprxeq. 100,000 protein and a Mr .apprxeq. 60,000 protein (tyrosine hydroxylase), visualized after separation of total cellular proteins in NaDodSO4/polyacrylamide gels. Immunoprecipitation with antibodies to three known phosphoproteins ("100-kDa," "87-kDa," and protein III) revealed an acetylcholine-dependent phosphorylation of these proteins. These three proteins were also shown to be present in bovine adrenal chromaffin cells by immunolabeling techniques. "100-kDa" is a Mr .apprxeq. 100,000 protein selectively phosphorylated by calcium/calmodulin-dependent protein kinase III, "87-kDa" is a Mr .apprxeq. 87,000 protein selectively phosphorylated by protein kinase C, and protein III is a phosphoprotein doublet of Mr .apprxeq. 74,000 (IIIa) and Mr .apprxeq. 55,000 (IIIb) phosphorlyated by cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase I. Furthermore, 100-kDa was shown to be identical to the Mr .apprxeq. 100,00 protein whose phosphorylation was increased by acetylcholine treatment. The acetylcholine-dependent increase in phosphorylation of tyrosine hydroxylase, 100-kDa, 87-kDa, and protein III required extracellular calcium and was mimicked by nicotine, veratridine, elevated K+, and calcium ionophore A23187, but not by muscarine. In addition, forskolin increase the phosphorylation of tyrosine hydroxylase, 100-kDa, and protein III, but not that of 87-kDa. Phorbol 12,13-dibutyrate increased the phosphorylation of tyrosine hydroxylase, 87-kDa, and protein III, but not that of 100-kDa. The data demonstrate that cholinergic activation of chromaffin cell increases the phosphorylation of several proteins and that several protein kinase systems may be involved in these effects.

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Accession: 004948534

Download citation: RISBibTeXText

PMID: 2894032

DOI: 10.2307/31294


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