Hormonal regulation of a calcium-activated, phospholipid-dependent protein kinase in bovine adrenal cortex.

The calcium-activated, phospholipid-dependent protein kinase (C kinase) and its proteolytic product (M kinase), originally discovered in central nervous tissue (Takai, Y., Kishimoto, A., Inoue, M., and Nishizuka, Y. (1977) J. Biol. Chem. 252, 7603-7610) were characterized in bovine adrenal cortex cytosol. An endogenous calcium-dependent protease able to generate M kinase from the isolated C kinase in vitro was also present in adrenocortical extracts. Bovine adrenocortical cells in suspension as well as in primary culture contain the C and the M kinase activities. Treatment of these cells by steroidogenic concentrations (nM to microM) of ACTH resulted in a time and dose-dependent increase of cytosolic C kinase activity, whereas no change in M kinase activity was detected. This apparent activation appears to result mostly from an intracellular shift of the membrane-associated C kinase to a soluble cytosolic form of the enzyme. These observations open the question of the possible implication of the calcium, phospholipid-dependent protein phosphorylation system in hormone-dependent cellular regulatory processes.