Changes in poly(adenosine diphosphate-ribose) and poly(adenosine diphosphate-ribose) polymerase in synchronous HeLa cells.
An antibody has been prepared which is highly specific for poly(adenosine diphosphate-ribose). Neither poly(A), DNA, nor a variety of adenine-containing nucleosides or nucleotides were effective in competing with poly(ADP-ribose) for binding to the antibody. Of all compounds tested, only adenosine diphosphate-ribose competed for binding to the antibody. Unlabeled poly(adenosine diphosphate-ribose) was about 10 000 times more effective in competing with labeled polymer for antibody binding than was adenosine diphosphate-ribose. Using the antibody, the amount of poly(adenosine diphosphate-ribose) was found to increase from early S phase to a peak at mid S with a second, even larger increase seen at the S-G2 transition point in synchronously dividing HeLa cells. Pulse labeling of the polymer with [2-3H]adenosine was also maximal at the same time points. Changes in the levels of poly(adenosine diphosphate-ribose) polymerase activity measured in isolated nuclei coincided with the changes in amounts of polymer present in intact cells during progression from S phase into G2.
D000227:Adenine Nucleotides / Q000494:pharmacology; D001665:Binding Sites; D002455:Cell Division; D004247:DNA / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009244:NAD+ Nucleosidase / Q000378:metabolism*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011061:Poly A / Q000494:pharmacology; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D013997:Time Factors
D000227:Adenine Nucleotides; D009702:Nucleoside Diphosphate Sugars; D011061:Poly A; D011064:Poly Adenosine Diphosphate Ribose; D004247:DNA; D009699:N-Glycosyl Hydrolases; D009244:NAD+ Nucleosidase