Membrane-associated protein kinases in phorbol ester-activated human polymorphonuclear leukocytes.
Membrane-associated protein kinases in human polymorphonuclear leukocytes were studied. In unstimulated polymorphonuclear leukocytes the protein kinase C was predominantly present in the cytosol but in phorbol 12-myristate 13-acetate- (PMA-) activated cells a time and dose-dependent translocation of the kinase to the particulate fraction occurred. Two new protein kinase activities also appeared in the particulate fraction upon PMA activation. The one had a Mr of 40,000 and its activity was independent of phospholipids. The other (Mr 90,000) as partially activated by phospholipids, but separated from protein kinase C on DEAE-cellulose chromatography.
D001692:Biological Transport; D002462:Cell Membrane / Q000201:enzymology; D002848:Chromatography, DEAE-Cellulose; D006801:Humans; D008213:Lymphocyte Activation / Q000187:drug effects; D009504:Neutrophils / Q000201:enzymology*; D010743:Phospholipids / Q000502:physiology; D011494:Protein Kinases / Q000097:blood*; D013347:Subcellular Fractions / Q000201:enzymology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D010743:Phospholipids; D011494:Protein Kinases; D013755:Tetradecanoylphorbol Acetate