Activation of cyclic AMP-dependent protein kinase in macrophages.
The activity of cyclic AMP-dependent protein kinase (cyclic AMP-PK) was significantly higher (P less than 0.001) in thioglycollate-elicited than in resident rat peritoneal macrophages. The activity ratio of the enzyme (its activity in the absence of added cyclic AMP divided by that in the presence of 5 microM cyclic AMP) was similar in the two cell types. The divalent ion ionophore A23187 induced a rapid increase in the activity ratio of cyclic AMP-PK in both macrophage types. This effect was blocked by pretreating the cells with indomethacin or aspirin (inhibitors of cyclo-oxygenase) and bromo-phenacyl bromide (an inhibitor of phospholipase A2), implicating the synthesis of a prostanoid as an intermediary step. Prostaglandin (PG) E2, 8-bromo cyclic AMP and cholera toxin, all of which inhibit chemiluminescence and/or PG formation in macrophages, increased the activity ratio of cyclic AMP-PK in these cells. We propose that the activation of cyclic AMP-PK plays a central role in the response of macrophages to both endogenously-generated and exogenously added PGE.
D000098:Acetophenones / Q000494:pharmacology; D000818:Animals; D001241:Aspirin / Q000494:pharmacology; D000001:Calcimycin / Q000494:pharmacology; D004789:Enzyme Activation; D007213:Indomethacin / Q000494:pharmacology; D007700:Kinetics; D008264:Macrophages / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013864:Thioglycolates / Q000494:pharmacology
D000098:Acetophenones; D013864:Thioglycolates; D000001:Calcimycin; D011494:Protein Kinases; C006821:4-bromophenacyl bromide; D001241:Aspirin; D007213:Indomethacin