Depletion of poly(ADP-ribose) polymerase-1 reduces host cell reactivation of a UV-damaged adenovirus-encoded reporter gene in human dermal fibroblasts

Ghodgaonkar, Medini; Zacal, Natalie; Kassam, Shaqil; Rainbow, Andrew J.; Shah, Girish M.

doi:10.1016/j.dnarep.2008.01.001

Cited by 26 publications

(30 citation statements)

References 83 publications

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“…Our results strongly indicate that PARP-1 is the principle player in the above responses, because cells specifically depleted of PARP-1 do not form detectable amounts of PARylated proteins in response to UV and are also inefficient at repair of UVdamaged genomic DNA. Our results are consistent with earlier reports that impaired PARP-1 function increases UV-induced skin cancer in mice (19), decreases cellular capacity to repair UV-induced DNA damage from viral reporter gene (20) or genomic DNA of CHO or triple negative breast cancer cells (11,12), and decreases the clonogenicity in response to UV (20).…”

Section: Discussionsupporting

confidence: 83%

Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair

Robu

Shah

Petitclerc

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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158

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Among the earliest responses of mammalian cells to DNA damage is catalytic activation of a nuclear enzyme poly(ADP-ribose) polymerase-1 (PARP-1). Activated PARP-1 forms the polymers of ADPribose (pADPr or PAR) that posttranslationally modify its target proteins, such as PARP-1 and DNA repair-related proteins. Although this metabolism is known to be implicated in other repair pathways, here we show its role in the versatile nucleotide excision repair pathway (NER) that removes a variety of DNA damages including those induced by UV. We show that PARP inhibition or specific depletion of PARP-1 decreases the efficiency of removal of UV-induced DNA damage from human skin fibroblasts or mouse epidermis. Using NER-proficient and -deficient cells and in vitro PARP-1 assays, we show that damaged DNA-binding protein 2 (DDB2), a key lesion recognition protein of the global genomic subpathway of NER (GG-NER), associates with PARP-1 in the vicinity of UV-damaged chromatin, stimulates its catalytic activity, and is modified by pADPr. PARP inhibition abolishes UV-induced interaction of DDB2 with PARP-1 or xeroderma pigmentosum group C (XPC) and also decreases localization of XPC to UV-damaged DNA, which is a key step that leads to downstream events in GG-NER. Thus, PARP-1 collaborates with DDB2 to increase the efficiency of the lesion recognition step of GG-NER.M ammalian cells respond very rapidly to different types of DNA damage by activation of an abundant and ubiquitous nuclear enzyme poly(ADP-ribose) polymerase-1 (PARP-1). The activated PARP-1 uses NAD + to form polymers of ADP-ribose (pADPr or PAR) that modify PARP-1 itself and selected target proteins, such as histones and DNA repair proteins (1). This posttranslational modification, i.e., PARylation, has been implicated in cellular responses ranging from DNA repair to cell death. Among mammalian DNA repair pathways, PARP-1 has been implicated in base excision repair, homologous recombination, and nonhomologous end-joining pathways (2, 3), but we do not know its role in the most versatile nucleotide excision repair (NER) pathway that removes a wide variety of DNA lesions, including UV-induced thymine dimers (T-T) and other cyclobutane pyrimidine dimers (CPD), as well as 6-4 photoproducts (6-4PP) (4).The core mammalian NER pathway uses more than 30 proteins to recognize the damaged site on DNA, remove 24-to 32-nucleotide-long single-stranded DNA containing the lesion, fill the gap using the nondamaged strand as a template, and finally ligate the nick (4). There are two subpathways of NER: the transcription-coupled NER (TC-NER) removes lesions from the actively transcribed strands of the genes and the global genomic NER (GG-NER) repairs lesions from the entire genome. These two pathways differ in the initial step of lesion recognition: TC-NER is initiated when elongating RNA polymerase II stalls at the lesion, whereas GG-NER is initiated when the lesion is recognized in the chromatin context by DDB2 (XPE), which through its participation in the UV-DDB-E3 ligase complex ub...

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Section: Discussionsupporting

confidence: 83%

Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair

Robu

Shah

Petitclerc

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

158

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“…1) following disruption of PARP activity by expression of the PARP-1 DNA-binding domain, chemical inhibitors, or RNAi. Current literature places a role for PARP-1 in the transcriptional coupled repair arm of NER with studies supporting a cooperative interplay between PARP-1 and Cockane syndrome B protein (7,8). Our studies provide a novel alternative mechanism, which demonstrates an association between XPA and PARP-1.…”

Section: Discussionmentioning

confidence: 77%

“…Although the involvement of PARP-1 in base excision repair is well characterized, there is limited knowledge regarding the contributions of PARP-1 to NER. Evidence to support a role for PARP-1 in NER includes retention of UVR-induced photoproducts previously described (7,8) and our data in keratinocytes (Fig. 1) following disruption of PARP activity by expression of the PARP-1 DNA-binding domain, chemical inhibitors, or RNAi.…”

Section: Discussionmentioning

confidence: 99%

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Poly(ADP-ribose) Contributes to an Association between Poly(ADP-ribose) Polymerase-1 and Xeroderma Pigmentosum Complementation Group A in Nucleotide Excision Repair

King

Cooper

Liu

et al. 2012

Journal of Biological Chemistry

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Background: Little is known regarding the role of PARP-1 in UVR-induced photolesion repair. Results: PARP inhibitors decrease PARP-1-XPA associations and reduce chromatin binding of XPA. Conclusion: PARP activation promotes XPA association with PARP-1 and chromatin. Significance: These data provide a mechanistic basis for the contribution of PARP-1 to nucleotide excision repair and expands the role of poly(ADP-ribose) in DNA repair pathways.

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“…Our positive control for potentiation of UV-mediated cytotoxicity was ABT-888, an inhibitor of the PARP-1 polymerase. Cells were irradiated and then cultured in the presence of ABT-888 at a concentration of 50µM [13,14].…”

Section: To the Editormentioning

confidence: 99%

oriconazole does not Potentiate Photo Damage from UVB Exposure

Angeles¹,

Cleaver

Feeney³

et al. 2013

J Clin Exp Dermatol Res

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Voriconazole is an effective anti-fungal triazole commonly used in bone marrow and solid organ transplant recipients. However, reports of accelerated development of aggressive squamous cell carcinomas in immunocompromised patients are documented following voriconazole use. It is hypothesized that voriconazole or its primary N-oxide metabolite, voricinazole-N-oxide increases keratinocyte susceptibility via UV-mediated cell damage. We aimed to investigate whether voriconazole or voriconazole-N-oxide potentiate cell death after UVB irradiation in vitro.Both compounds absorb UVB but voriconazole exhibited weak emission while voriconazole-N-oxide showed no detectable emission in UVA. Exposure of different skin cell lines to these compounds did not show significant reduction in cell survival and regardless whether the cells were exposed to the drugs before or after UVB irradiation. However, in primary human keratinocytes, both drugs caused a small increase in cell survival following drug incubation and UVB irradiation. This is the first report documenting the effect of voriconazole and voriconazole-N-oxide in relation to UVBassociated cell death in vitro.

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Depletion of poly(ADP-ribose) polymerase-1 reduces host cell reactivation of a UV-damaged adenovirus-encoded reporter gene in human dermal fibroblasts

Cited by 26 publications

References 83 publications

Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair

Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair

Poly(ADP-ribose) Contributes to an Association between Poly(ADP-ribose) Polymerase-1 and Xeroderma Pigmentosum Complementation Group A in Nucleotide Excision Repair

oriconazole does not Potentiate Photo Damage from UVB Exposure

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