title: Regulation of arachidonate-mobilizing phospholipase A2 by phosphorylation via protein kinase C in macrophages.
abstract: Stimulation of 32P-labeled macrophages with phorbol ester caused an increase in phosphorylation of the intracellular, high molecular weight phospholipase A2. This increase in phosphorylation was accompanied by an increase in enzyme activity, but led to no detectable shift in the concentration dependence for Ca(2+)-induced activation. The phosphorylated phospholipase A2 could be dephosphorylated by treatment with acid phosphatase, and such treatment also reduced its catalytic activity. Together with previous data, these results indicate that the arachidonate-mobilizing phospholipase A2 is dually regulated by Ca2+ (membrane interaction) and by phosphorylation (catalytic activity).
authors.affiliation: Department of Medical and Physiological Chemistry, Lund University, Sweden.
authors.forename: J
authors.initials: J
authors.lastname: Wijkander
authors.forename: R
authors.initials: R
authors.lastname: Sundler
mesh_terms: D000818:Animals; D016718:Arachidonic Acid / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D002478:Cells, Cultured; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008264:Macrophages / Q000201:enzymology*; D051379:Mice; D010741:Phospholipases A / Q000302:isolation & purification / Q000378:metabolism*; D054467:Phospholipases A2; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
chemical_list: D007527:Isoenzymes; D016718:Arachidonic Acid; D011493:Protein Kinase C; D010741:Phospholipases A; D054467:Phospholipases A2; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium