(ADP-ribose)n participates in DNA excision repair

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

doi:10.1038/283593a0

Cited by 1,059 publications

(492 citation statements)

References 25 publications

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“…This uncertainty is even greater for NAM, since it is both a precursor of NAD +, the ADPRT substrate, and an inhibitor of ADPRT activity. Therefore, both NAM starvation and addition have been used to inhibit the enzyme activity [31].…”

Section: Discussionmentioning

confidence: 99%

Inhibition of poly(ADP‐ribosyl)ation does not prevent lymphocyte entry into the cell cycle

Marini

Zunica

Monti³

et al. 1989

FEBS Letters

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The enzyme poly(ADP-ribosyl)transferase (ADPRT) becomes activated soon after a mitogenic stimulus is applied to lymphocyte cultures. It has also been reported that ADPRT inhibitors prevent cell proliferation when added to cultures at the same time as the mitogen. While this has been ascribed to the need to seal physiologically present DNA strand breaks before cells enter S phase, the presence of DNA strand breaks in quiescent human lymphocytes has been recently questioned. We demonstrate here that non-toxic concentrations of ADPRT inhibitors do not affect lymphocyte blastization and proliferation, as measured by thymidine incorporation and cytofluorimetry. We therefore suggest that ADPRT activation is required for late functions which are not needed for cell cycle progression.

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Section: Discussionmentioning

confidence: 99%

Inhibition of poly(ADP‐ribosyl)ation does not prevent lymphocyte entry into the cell cycle

Marini

Zunica

Monti³

et al. 1989

FEBS Letters

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“…PCNA, one of the p53 downstream target gene products [40], is an essential component of DNA repair and replication machinery [43]. The induction of protein modification via ADP-ribosylation has also been recognized as an important event in DNA repair [44,45]. Cells exposed to γ-rays (6 Gy) exhibited an increased expression of ADP-ribosylated and phosphorylated species of NPM/B23, 4 h after exposure [46].…”

Section: Role Of Npm In Pbrmentioning

confidence: 99%

Proteome analysis of proliferative response of bystander cells adjacent to cells exposed to ionizing radiation

Gerashchenko

Yamagata²,

Oofusa³

et al. 2007

Proteomics

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Recently (Cytometry 2003, 56A, 71-80), we reported that direct cell-to-cell contact is required for stimulating proliferation of bystander rat liver cells (WB-F344) cocultured with irradiated cells, and neither functional gap junction intercellular communication nor long-range extracellular factors appear to be involved in this proliferative bystander response (PBR). The molecular basis for this response is unknown. Confluent monolayers of WB-F344 cells were exposed to 5-Gray (Gy) of γ-rays. Irradiated cells were mixed with unirradiated cells and co-cultured for 24 h. Cells were harvested and protein expression was examined using 2-DE. Protein expression was also determined in cultures of unirradiated and 5-Gy irradiated cells. Proteins were identified by MS. Nucleophosmin (NPM)-1, a multifunctional nucleolar protein, was more highly expressed in bystander cells than in either unirradiated or 5-Gy irradiated cells. Enolase-α, a glycolytic enzyme, was present in acidic and basic variants in unirradiated cells. In bystander and 5-Gy irradiated cells, the basic variant was weakly expressed, whereas the acidic variant was overwhelmingly present. These data indicate that the presence of irradiated cells can affect NPM-1 and enolase-α in adjacent bystander cells. These proteins appear to participate in molecular events related to the PBR and suggest that this response may involve cellular defense, proliferation, and metabolism.

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“…The enzyme is totally dependent on DNA [5] and is markedly stimulated by fragmentation of the DNA [6][7][8][9]. Evidence has accumulated over the last 5 years that (ADP-ribose)n participates in the cellular recovery from DNA damage [10,11 ]. Both radiation and alkylating agents lower the cellular NAD content [6,[12][13][14] and thereby interfere with glycolysis.…”

Section: Introductionmentioning

confidence: 99%

“…Both radiation and alkylating agents lower the cellular NAD content [6,[12][13][14] and thereby interfere with glycolysis. This drop in cellular NAD is mediated by nuclear ADP-ribosyl transferase [10,12]. Poly~ADP-ribose) in intact cells is increased after DNA damage [15].…”

Section: Introductionmentioning

confidence: 99%

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

Gray¹,

Durkacz²,

Shall³

1981

FEBS Letters

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(ADP-ribose)n participates in DNA excision repair

Cited by 1,059 publications

References 25 publications

Inhibition of poly(ADP‐ribosyl)ation does not prevent lymphocyte entry into the cell cycle

Inhibition of poly(ADP‐ribosyl)ation does not prevent lymphocyte entry into the cell cycle

Proteome analysis of proliferative response of bystander cells adjacent to cells exposed to ionizing radiation

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

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