Phosphorylation of poly(ADP-ribose)polymerase protein in human peripheral lymphocytes stimulated with phytohemagglutinin.
Intracellular phosphorylation of poly(ADP-ribose)polymerase was assayed in streptolysin-O-permeabilized human lymphocytes. Whereas 32P incorporation from [gamma-32P]ATP into immunoprecipitated enzyme protein was undetectable in resting cells, significant phosphorylation of this enzyme was observed in lymphocytes treated with phytohemagglutinin. The phosphorylation of poly(ADP-ribose)polymerase in permeabilized cells was not stimulated by phorbol ester, while phorbol-induced phosphorylation of other proteins and of a specific oligopeptide substrate of protein kinase C was observed. However, the specific inhibitory pseudosubstrate peptide of protein kinase C blocked the phosphorylation of poly(ADP-ribose)polymerase induced by phytohemagglutinin. Therefore, a potential role of a member of the protein kinase C family in the phytohemagglutinin stimulated intracellular phosphorylation of poly(ADP-ribose)polymerase is conceivable.
Bauer
P I
PI
Department of Biochemistry I, Semmelweis University Medical School, Budapest, Hungary.
Farkas
G
G
Mihalik
R
R
Kopper
L
L
Kun
E
E
Faragó
A
A
D001426:Bacterial Proteins; D002478:Cells, Cultured; D006801:Humans; D008214:Lymphocytes / Q000187:drug effects* / Q000378:metabolism; D010766:Phosphorylation; D010835:Phytohemagglutinins / Q000494:pharmacology*; D011065:Poly(ADP-ribose) Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors; D013301:Streptolysins
D001426:Bacterial Proteins; D010835:Phytohemagglutinins; D013301:Streptolysins; C025964:streptolysin O; D011065:Poly(ADP-ribose) Polymerases; D011493:Protein Kinase C