The activity of a beta subtype of protein kinase C purified from nuclei of human neutrophils is enhanced by treatment with phorbol 12-myristate 13-acetate.
Two protein kinase C isoenzymes were partially purified from the nuclei of human neutrophils, and identified as beta and alpha subtypes. Treatment of neutrophils with phorbol 12-myristate 13-acetate (PMA) caused a 3.8-fold increase of nuclear beta PKC activity, while a minor increase of alpha PKC was observed. This selective activation of beta PKC could help to understand the molecular events involved in phorbol ester-induced cellular modifications.
Perletti
G
G
Istituto di Farmacologia, Università degli Studi di Milano, Italy.
Ghessi
A
A
Raffaldoni
E
E
Piccinini
F
F
D000906:Antibodies; D002467:Cell Nucleus / Q000201:enzymology*; D002845:Chromatography; D002852:Chromatography, Ion Exchange; D017886:Durapatite; D004789:Enzyme Activation; D006801:Humans; D006882:Hydroxyapatites; D007527:Isoenzymes / Q000097:blood* / Q000302:isolation & purification; D007700:Kinetics; D009504:Neutrophils / Q000201:enzymology*; D011493:Protein Kinase C / Q000097:blood* / Q000302:isolation & purification; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D000906:Antibodies; D006882:Hydroxyapatites; D007527:Isoenzymes; D017886:Durapatite; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate