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Translocation of protein kinase C (PKC) from the cytosol to the plasma membranes is believed to reflect activation of the enzyme. We have studied translocation of PKC in lactotroph-enriched anterior pituitary cell cultures by measuring the incorporation of -³²P from [-³²P]ATP into a synthetic peptide substrate, MBP_4–14, and by immunoblotting of PKC isozymes. Using cells permeabilized with digitonin the effects of PKC cofactors on the distribution of the enzyme were studied. Ca⁺ (50 nM) and dioctanoyl-sn-glycerol had no effect when tested alone, but in combination they caused a redistribution of PKC from the soluble to the particulate fraction. Arachidonic acid needed Ca⁺ to induce translocation of PKC, while being ineffective under Ca²⁺-free conditions. Western blot analysis of partly purified PKC from lactotroph-enriched pituitary cells revealed the presence of the , β, , and isozymes. 12-O-Tetradecanoylphorbol 13-acetate (TPA) and substance P displayed different patterns of redistribution of PKC isozyme immunoreactivity from soluble to membrane-attached forms. Thus, TPA induced time- and dose-dependent (mean effective concentration (EC₅₀)=1 nM) translocation of the , β and species, while substance P stimulated time- and dose-dependent (EC₅₀=1 nM) redistribution of the and β isozymes. subtype immunoreactivity could not be translocated by either agonist; neither could the immunoreactivity of be down-regulated by long-term treatment (24 h) with TPA.

The results indicate that simultaneous activation of phospholipases C and A₂ induces a synergistic activation of PKC. Finally it is suggested that substance P may exert some of its effects in lactotrophs by translocation of PKC isozymes and β.

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