Regulation of poly(ADP-ribose) transferase activity by 2',5'-oligoadenylates

• Published in: Biochemistry international Vol. 9; no. 2; p. 143
• Main Authors: Pivazian, A D, Suzuki, H, Vartanian, A A, Zhelkovsky, A M, Farina, B, Leone, E, Karpeisky MYa
• Format: Journal Article
• Language: English
• Published: Australia 01.08.1984
• Subjects: Adenine Nucleotides - chemical synthesis; Adenine Nucleotides - pharmacology; Animals; Cattle; Cell Nucleus - enzymology; Cytoplasm - enzymology; Endoribonucleases - metabolism; In Vitro Techniques; Interferons - pharmacology; Kinetics; L Cells (Cell Line) - enzymology; Male; Mice; NAD+ Nucleosidase - metabolism; Oligonucleotides - pharmacology; Oligoribonucleotides - chemical synthesis; Oligoribonucleotides - pharmacology; Phosphoric Diester Hydrolases - metabolism; Poly(ADP-ribose) Polymerase Inhibitors; Poly(ADP-ribose) Polymerases - metabolism; Testis - enzymology
• ISSN: 0158-5231

pppA2'pA2'pA appears to be a potent natural noncompetitive inhibitor of poly (ADP-ribose) transferase activity in the histone dependent reaction of ADP-ribosylation with Ki=5 microM. Moreover, it is a noncompetitive inhibitor of the Mg2+ dependent reaction of autoADPRT-ribosylation with Ki=20 microM. The activity of ADPRT falls down abruptly both in the cytoplasm and nuclei of mouse L-cells treated with interferon. In contrast, the activities of 2',5'-oligo (A) polymerase and 2'-phosphodiesterase remain virtually unchanged after the treatment with ADPRT preparation. The regulation of ADPRT activity and active form of ADPRT by 2',5-oligoadenylates is presumed to be one of the factors responsible for inducing the antiviral and/or antiproliferative effects of interferon.