Inhibition of protein kinase C phosphorylation by mono- and divalent cations

Abstract

The effect of a matrix of concentrations of Ca 2+ (0.01, 0.1, 0.5, 5 mM), Mg 2+ (0.2, 0.5, 1, 2, 5, 10 mM), and Na + (50, 100, 150 mM) on the phosphorylation of histone H-1 by protein kinase C was measured in the presence of 5 mol % diacylglycerol and Mg-ATP in both phosphatidylserine micelles and liposomes formed from a 1:4 mixture of phosphatidylserine and phosphatidylcholine. Monovalent cations (150 mM) reduced activity by 60 and 84% in the micelle and liposome assay systems, respectively. Inhibition was also observed with 5 mM Ca 2+ and 10 mM Mg 2+. The phosphorylating activity was compared with computer calculations of the negative electrostatic potentials (ψ o) of the phospholipid membranes in the presence of the cations.