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Effect of nicotinamide on RNA and DNA synthesis and on poly(ADP‐ribose) polymerase activity in normal and phytohemagglutinin stimulated human lymphocytes
Author(s) -
Rochette-Egly C.,
Ittel M.E.,
Bilen J.,
Mandel P.
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)81033-7
Subject(s) - microbiology and biotechnology , rna polymerase , polymerase , dna , physics , humanities , rna , biology , philosophy , genetics , gene
The nuclei of eukaryotic cells contain the enzyme poly(ADP-ribose) polymerase which converts NAD into poly(ADP-ribose) with the elimination of nicotinamide [1,2]. Several reports suggest that poly(ADP-ribose) polymerase is involved in the regulation of eukaryotic DNA synthesis and in the DNA repair mechanisms (reviewed [3-S]). A higher poly(ADP-ribose) polymerase activity in leukemic leukocytes than in lymphocytes from normal donors was observed [6,7]. Similarly, in human and pig lymphocytes, the activity of poly(ADP-ribose) polymerase increased together with DNA synthesis, induced by phytohemagglutinin PHA [7,8]. Finally, an increase in poly(ADP-ribose) polymerase activity in parallel to cellular NAD decrease after treatment of cells with DNA-damaging agents was reported [9,10]. It is of interest to define whether the well-known decrease in NAD content of proliferating tumoral cells is also correlated with an increase in poly(ADP-ribose) polymerase activity and whether changes in poly(ADP-ribose) polymerase activity correlate with cell proliferation. Nicotinamide at high concentrations, is a well-known competitive inhibitor of poly(ADP-ribose) polymerase [ 11 ,I 21. This study was undertaken in order to determine