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X-ray induced DNA damage and repair in germ cells of PARP1(-/-) male mice.

TitoloX-ray induced DNA damage and repair in germ cells of PARP1(-/-) male mice.
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2013
AutoriVillani, Paola, Fresegna Anna Maria, Ranaldi Roberto, Eleuteri Patrizia, Paris Lorena, Pacchierotti Francesca, and Cordelli Eugenia
RivistaInt J Mol Sci
Volume14
Issue9
Paginazione18078-92
Data di pubblicazione2013 Sep 04
ISSN14220067
Parole chiaveAnimals, Comet Assay, DNA damage, DNA repair, Flow cytometry, Germ Cells, Histones, male, Mice, Mice, Inbred C57BL, Mice, Knockout, Phosphorylation, Poly (ADP-Ribose) Polymerase-1, Poly(ADP-ribose) Polymerases, X-Rays
Abstract

Poly(ADP-ribose)polymerase-1 (PARP1) is a nuclear protein implicated in DNA repair, recombination, replication, and chromatin remodeling. The aim of this study was to evaluate possible differences between PARP1(-/-) and wild-type mice regarding induction and repair of DNA lesions in irradiated male germ cells. Comet assay was applied to detect DNA damage in testicular cells immediately, and two hours after 4 Gy X-ray irradiation. A similar level of spontaneous and radiation-induced DNA damage was observed in PARP1(-/-) and wild-type mice. Conversely, two hours after irradiation, a significant level of residual damage was observed in PARP1(-/-) cells only. This finding was particularly evident in round spermatids. To evaluate if PARP1 had also a role in the dynamics of H2AX phosphorylation in round spermatids, in which γ-H2AX foci had been shown to persist after completion of DNA repair, we carried out a parallel analysis of γ-H2AX foci at 0.5, 2, and 48 h after irradiation in wild-type and PARP1(-/-) mice. No evidence was obtained of an effect of PARP1 depletion on H2AX phosphorylation induction and removal. Our results suggest that, in round spermatids, under the tested experimental conditions, PARP1 has a role in radiation-induced DNA damage repair rather than in long-term chromatin modifications signaled by phosphorylated H2AX.

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cited By 7

URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84884261871&doi=10.3390%2fijms140918078&partnerID=40&md5=dcbc64c58c33ee9b727a8f582adeb84f
DOI10.3390/ijms140918078
Alternate JournalInt J Mol Sci
Citation Key4907
PubMed ID24009020
PubMed Central IDPMC3794770