Inhibitors of nuclear ADP‐ribosyl transferase retard DNA repair after <i>N</i>‐methyl‐<i>N</i>‐nitroso‐urea

Gray, Douglas A.; Durkacz, Barbara W.; Shall, Sydney

doi:10.1016/0014-5793(81)80913-1

Cited by 39 publications

(2 citation statements)

References 18 publications

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“…(21) Early study with PARP-1 inhibitors also suggested that PARP-1 facilitated DNA repair, since putative PARP-1 inhibitors delayed the process. (22) Analysis of gene expression patterns in the PARP-1 ''knock-out'' mice also revealed an alteration in the expression of many genes, particularly growth-related cellcycle genes essential for tumor growth. (23) This suggested a physiological role of PARP-1 in direct or indirect gross regulation of gene expression.…”

Section: Introductionmentioning

confidence: 97%

Are poly(ADP‐ribosyl)ation by PARP‐1 and deacetylation by Sir2 linked?

Zhang

2003

BioEssays

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Poly(ADP-ribose) polymerase-1 (PARP-1) safeguards genomic integrity by limiting sister chromatid exchanges. Overstimulation of PARP-1 by extensive DNA damage, however, can result in cell death, as prolonged PARP-1 activation depletes NAD(+), a substrate, and elevates nicotinamide, a product. The decline of NAD(+) and the rise of nicotinamide may downregulate the activity of Sir2, the NAD(+)-dependent deacetylases, because deacetylation by Sir2 is dependent on high concentration of NAD(+) and inhibited by physiologic level of nicotinamide. The Sir2 deacetylase family has been implicated in mediating gene silencing, longevity and genome stability. It is conceivable that poly(ADP-ribosyl)ation by PARP-1, which is induced by DNA damage, could modulate protein deacetylation by Sir2 via the NAD(+)/nicotinamide connection. The possible linkage of the two ancient pathways that mediate broad biological activities may spell profound evolutionary roles for the conserved PARP-1 and Sir2 gene families in multicellular eukaryotes.

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Section: Introductionmentioning

confidence: 97%

Are poly(ADP‐ribosyl)ation by PARP‐1 and deacetylation by Sir2 linked?

Zhang

2003

BioEssays

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“…Recently it was reported that inhibitors of poly(ADP-ribose) synthetase such as ?-aminobenzamide retard DNA repair from damages due to alkylating agents [10,20]. We therefore analyzed velocity sedimentation in an al- kaline sucrose gradient of DNA from In1 1 lR1 cells treated with streptozotocin alone or with streptozotocin and nicotinamide.…”

Section: Concentration (M)mentioning

confidence: 99%

Poly(ADP‐ribose) synthetase inhibitors enhance streptozotocin‐induced killing of insulinoma cells by inhibiting the repair of DNA strand breaks

Yamamoto

Okamoto

1982

FEBS Letters

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Influence of the poly (ADP‐ribose) polymerase inhibitor 3‐aminobenzamide on macrophage and granulocyte differentiation of HL‐60 cells

et al. 1986

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We investigated the influence of the poly(ADP-ribose) polymerase inhibitor 3-aminobenzamide (ABA) on induction of phenotypic markers of granulocyte differentiation by retinoic acid and markers of macrophage differentiation by TPA in HL-60 cells. The differentiation of HL-60 cells towards the granulocyte lineage was assessed by hexose monophosphate shunt activity, proportion of cells capable of reducing NBT dye, and the appearance of recognizable neutrophils and bands. The effect of ABA and retinoic acid on NBT dye reduction and appearance of mature neutrophils and bands was synergistic, whereas the effects of these agents on hexose monophosphate shunt activity were additive. The differentiation inducing capacity of ABA in the presence of retinoic acid was dose-related. The influence of ABA on TPA-induced markers of macrophage differentiation was assessed by determining the proportion of adherent cells produced after treatment and by measuring acid phosphatase activity in the adherent cell fraction. In the presence of ABA, the number of cells adhering to plastic declined after day 2 of exposure to TPA, and acid phosphatase activity in adherent cells was inhibited fourfold (p = 0.01). The influence of ABA on the phenotypic markers of granulocyte and macrophage differentiation was detectable at concentrations that were not cytotoxic. The influence of ABA on HL-60 differentiation is similar to that previously reported for human bone marrow CFU-GM. Our data suggest that poly(ADP-ribose) polymerase plays a role in differentiation of HL-60 cells and that HL-60 might provide a useful model for evaluating control mechanisms involved in the differentiation of CFU-GM.

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Inhibitors of nuclear ADP‐ribosyl transferase retard DNA repair after N‐methyl‐N‐nitroso‐urea

Cited by 39 publications

References 18 publications

Are poly(ADP‐ribosyl)ation by PARP‐1 and deacetylation by Sir2 linked?

Are poly(ADP‐ribosyl)ation by PARP‐1 and deacetylation by Sir2 linked?

Poly(ADP‐ribose) synthetase inhibitors enhance streptozotocin‐induced killing of insulinoma cells by inhibiting the repair of DNA strand breaks

Influence of the poly (ADP‐ribose) polymerase inhibitor 3‐aminobenzamide on macrophage and granulocyte differentiation of HL‐60 cells

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