Unique acceptors for poly(ADP-ribose) in resting, proliferating and DNA-damaged human lymphocytes.
Acceptor proteins for poly(adenosine diphosphoribosyl)ation were determined in resting human lymphocytes, in lymphocytes with N-methyl-N'-nitro-N-nitrosoguanidine-induced DNA damage and in lymphocytes stimulated to proliferate by phytohemagglutinin. Kinetic studies showed that the increase in ADP-ribosylation which occurred in response to N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) treatment was greater in magnitude but more transient in duration than that which occurred in phytohemagglutinin-stimulated cells. Gel electrophoretic analyses revealed that MNNG treatment and phytohemagglutinin stimulation both caused an increase in ADP-ribosylation of poly(ADP-ribose) polymerase and core histones. In MNNG-treated cells, an increase in ADP-ribosylation of histone H1 was also observed. In contrast, phytohemagglutinin-stimulated cells showed no increase in ADP-ribosylation of histone H1. In MNNG-treated cells there was also ADP-ribosylation of a protein of molecular weight 62 000, while in phytohemagglutinin-stimulated cells there was a marked increase in ADP-ribosylation of a protein of molecular weight 96 000. MNNG treatment of phytohemagglutinin-stimulated cells produced a pattern of ADP-ribosylation that appeared to be due to the combined effects of the individual treatments. 3-Aminobenzamide effectively inhibited ADP-ribosylation under all treatment conditions.
D002455:Cell Division; D002463:Cell Membrane Permeability; D004260:DNA Repair; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008214:Lymphocytes / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D008769:Methylnitronitrosoguanidine / Q000494:pharmacology; D008970:Molecular Weight; D009702:Nucleoside Diphosphate Sugars / Q000097:blood*; D011064:Poly Adenosine Diphosphate Ribose / Q000097:blood*
D009702:Nucleoside Diphosphate Sugars; D008769:Methylnitronitrosoguanidine; D011064:Poly Adenosine Diphosphate Ribose