Concanavalin A and phorbol ester cause opposite subcellular redistribution of protein kinase C.
Concanavalin A and phorbol ester induce human blood monocytes to produce superoxide. We tested whether activation of human monocytes by these agents is accompanied by a subcellular redistribution of protein kinase C. Phorbol ester predictably caused a profound shift of the enzyme from the cytosol to the particulate fraction. In contrast concanavalin A induced a shift of the enzyme from the particulate fraction to the cytosol. The opposite effect of these agents on kinase C translocation was observed also by analysis of the phosphorylation of cytosolic proteins. Kinase C is either not involved in monocyte activation or does so by distinct pathways determined by the activating agent.
D003067:Coenzymes / Q000097:blood; D003208:Concanavalin A / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D009000:Monocytes / Q000187:drug effects / Q000201:enzymology; D010704:Phorbols / Q000494:pharmacology*; D011493:Protein Kinase C / Q000097:blood / Q000378:metabolism*; D013347:Subcellular Fractions / Q000187:drug effects / Q000201:enzymology*; D013481:Superoxides / Q000097:blood; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D003067:Coenzymes; D010704:Phorbols; D003208:Concanavalin A; D013481:Superoxides; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate