Regulation by protein kinase C of platelet-activating factor- and thapsigargin-induced calcium entry in rabbit neutrophils.

12-O-Tetradecanoylphorbol-13-acetate (TPA) time-dependently inhibited the platelet-activating factor (PAF)-induced rise in cytosolic free calcium concentration ([Ca2+]i) in rabbit neutrophils, whereas staurosporine significantly enhanced it. Inositol 1,4,5-trisphosphate (IP3) induced Ca2+ release in digitonin-permeabilized cells but not in PAF-pretreated permeabilized cells. IP3-induced Ca2+ release was not affected by protein kinase C activators or inhibitors. In the cells pretreated with PAF and thapsigargin in Ca(2+)-deficient medium, stimulated Ca2+ entry was evoked by the subsequent addition of CaCl2. TPA inhibited the Ca2+ entry induced by PAF and thapsigargin in a staurosporine-reversible manner but not thapsigargin-induced [Ca2+]i elevation. These results suggest that protein kinase C negatively regulates PAF- and thapsigargin-induced rise in [Ca2+]i possibly by inhibiting Ca2+ store depletion-induced Ca2+ entry.