Characterization of protein kinase C and its role in catecholamine secretion from bovine adrenal-medullary cells
- 15 May 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 228 (1), 35-42
- https://doi.org/10.1042/bj2280035
Abstract
Protein kinase C activity towards exogenous histone was detected in a cytosolic fraction of bovine adrenal medulla. The enzyme was dependent on Ca2+ and phosphatidylserine for its activity, with half-maximal activation being achieved at .apprx. 18 .mu.M free Ca2+ and 8 .mu.g of phosphatidylserine/ml. Both diolein and 4.beta.-phorbol 12-myristate 13-acetate (TPA) decreased the Ca2+ requirement of the enzyme, half-maximal activation being obtained at .apprx. 12 .mu.M and 9 .mu.M free Ca2+ respectively in the presence of these agents. Many endogenous proteins in the adrenal-medullary cytosolic fraction were detected whose phosphorylation was dependent on the presence of both Ca2+ and phosphatidylserine. TPA stimulated catecholamine release from cultured bovine adrenal-chromaffin cell in a Ca2+-dependent manner. A23187 [calcimycin] also stimulated catecholamine secretion, and at suboptimal concentrations of TPA and A23187 a synergistic secretory response was obtained. Results are consistent with protein kinase C having a regulatory role in exocytosis in bovine adrenal chromaffin cells.This publication has 38 references indexed in Scilit:
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