Phosphorylation of myosin light chain in intact pig leukocytes stimulated by phorbol 12-myristate 13-acetate.
Phosphorylation of myosin light chain was investigated in intact pig polymorphonuclear leukocytes. The labeling of the myosin light chain (Mr = 21000) was increased by exposure of the cells to phorbol 12-myristate 13-acetate. Two-dimensional gel electrophoresis revealed three forms of Mr = 21000 light chain, of which two were phosphorylated. The phosphorylation of the myosin light chain was inhibited by neither N-(6-aminohexyl)-5-chloro-1-naphthalene sufonamide nor trifluoperazine, suggesting that calmodulin is not involved in the phosphorylation.
D000818:Animals; D002147:Calmodulin / Q000037:antagonists & inhibitors; D008970:Molecular Weight; D009218:Myosins / Q000378:metabolism*; D009504:Neutrophils / Q000378:metabolism*; D010704:Phorbols / Q000494:pharmacology*; D010766:Phosphorylation; D013481:Superoxides; D013552:Swine; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D002147:Calmodulin; D010704:Phorbols; D013481:Superoxides; D009218:Myosins; D013755:Tetradecanoylphorbol Acetate