8 results on '"Catizone, Angela"'
Search Results
2. MOESM2 of Levetiracetam enhances the temozolomide effect on glioblastoma stem cell proliferation and apoptosis
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Scicchitano, Bianca, Sorrentino, Silvia, Proietti, Gabriella, Lama, Gina, Dobrowolny, Gabriella, Catizone, Angela, Binda, Elena, Larocca, Luigi, and Sica, Gigliola
- Abstract
Additional file 2: Figure S1. Effects of different chemotherapeutic drugs on Jurkat cell proliferation. (A) BrdU cell proliferation assay of Jurkat cells treated for 48 h with TMZ (250 µM), ETO (10 µM), IRI (10 µg/ml) and CARB (10 µg/ml). (B) Western blot analysis of total lysates from Jurkat cells, treated as described above was performed to detect PCNA expression levels; β-actin was used as a loading control. (C) Densitometric analysis of three independent experiments on PCNA expression levels. ** p
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- 2018
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3. ADP-ribose polymer depletion leads to nuclear Ctcf re-localization and chromatin rearrangement(1)
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Guastafierro, Tiziana, Catizone, Angela, Calabrese, Roberta, Zampieri, Michele, Martella, Oliviano, Bacalini, Maria Giulia, Reale, Anna, Di Girolamo, Maria, Miccheli, Margherita, Farrar, Dawn, Klenova, Elena, Ciccarone, Fabio, Caiafa, Paola, Department of Cellular Biotechnologies and Haematology, Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome]-Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Department of Anatomy, Histology, Forensic Medicine and Orthopedics, Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Consorzio Mario Negri Sud, Chieti - Italy, Department of Biological Sciences (DBS), Central Campus, University of Essex, and This work was supported by the International Fondo per gli Investimenti della Ricercadi Base 2006 [grant number RBIN06E9Z8_003] and by the Ministero dell’Istruzione,dell’Universita e della Ricerca (Progetti di Ricerca di Interesse Nazionale 2008, P.C.), Italy.
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MESH: Cell Nucleus ,CCCTC-Binding Factor ,Glycoside Hydrolases ,Recombinant Fusion Proteins ,Active Transport, Cell Nucleus ,Poly (ADP-Ribose) Polymerase-1 ,MESH: Active Transport, Cell Nucleus ,Poly(ADP-ribose) Polymerase Inhibitors ,Cell Line ,MESH: Mutant Proteins ,Mice ,MESH: DNA Methylation ,MESH: Glycoside Hydrolases ,MESH: Recombinant Fusion Proteins ,Animals ,MESH: Animals ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,MESH: Mice ,MESH: Adenosine Diphosphate Ribose ,Cell Nucleus ,Adenosine Diphosphate Ribose ,MESH: Poly(ADP-ribose) Polymerases ,MESH: Chromatin Assembly and Disassembly ,MESH: Lamins ,DNA Methylation ,Chromatin Assembly and Disassembly ,MESH: Gene Knockdown Techniques ,MESH: Amino Acid Substitution ,Lamins ,MESH: Cell Line ,Repressor Proteins ,MESH: Mutagenesis, Site-Directed ,Amino Acid Substitution ,MESH: Repressor Proteins ,Gene Knockdown Techniques ,Mutagenesis, Site-Directed ,Mutant Proteins ,Poly(ADP-ribose) Polymerases - Abstract
International audience; Ctcf (CCCTC-binding factor) directly induces Parp [poly(ADP-ribose) polymerase] 1 activity and its PARylation [poly(ADPribosyl)ation] in the absence of DNA damage. Ctcf, in turn, is a substrate for this post-synthetic modification and as such it is covalently and non-covalently modified by PARs (ADP-ribose polymers). Moreover, PARylation is able to protect certain DNA regions bound by Ctcf from DNA methylation. We recently reported that de novo methylation of Ctcf target sequences due to overexpression of Parg [poly(ADP-ribose)glycohydrolase] induces loss of Ctcf binding. Considering this, we investigate to what extent PARP activity is able to affect nuclear distribution of Ctcf in the present study. Notably, Ctcf lost its diffuse nuclear localization following PAR (ADP-ribose polymer) depletion and accumulated at the periphery of the nucleus where it was linked with nuclear pore complex proteins remaining external to the perinuclear Lamin B1 ring. We demonstrated that PAR depletion-dependent perinuclear localization of Ctcf was due to its blockage from entering the nucleus. Besides Ctcf nuclear delocalization, the outcome of PAR depletion led to changes in chromatin architecture. Immunofluorescence analyses indicated DNA redistribution, a generalized genomic hypermethylation and an increase of inactive compared with active chromatin marks in Parg-overexpressing or Ctcf-silenced cells. Together these results underline the importance of the cross-talk between Parp1 and Ctcf in the maintenance of nuclear organization.
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- 2012
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4. c-MET receptor as potential biomarker and target molecule for malignant testicular germ cell tumors
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Corano Scheri, K, Leonetti, E, Laino, L, Gigantino, V, Gesualdi, L, Grammatico, P, Bizzari, M, Franco, R, Oosterhuis, Jw, Stoop, H, Looijenga, Lhj, Ricci, G, Catizone, A., Corano Scheri, Katia, Leonetti, Erica, Laino, Luigi, Gigantino, Vincenzo, Gesualdi, Luisa, Grammatico, Paola, Bizzari, Mariano, Franco, Renato, Wolter Oosterhuis, J, Stoop, Han, Looijenga, Leendert, Ricci, Giulia, Catizone., Angela, and Pathology
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c-MET inhibitors ,0301 basic medicine ,endocrine system ,Cancer therapy ,TGCTs ,C-MET inhibitor ,HGF ,c-MET ,cancer therapy ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,Oncology ,TGCT ,030220 oncology & carcinogenesis ,C-MET - Abstract
Type II testicular germ cell tumors (TGCTs) represent the most frequent malignancy in Caucasian males (20-40 years). Even if diagnosed with disseminated disease, > 80% of patients are cured; however, a small percentage of cases progress and result in death. It is commonly accepted that these cancers arise from a disturbed testicular embryonic niche that leads to the block of gonocyte differentiation. The subsequent development of the invasive seminomas and nonseminomas is due to a combination of genetic, epigenetic and microenvironmentbased alterations (genvironment). Hepatocyte growth factor (HGF) is present in the testicular microenvironment, together with its receptor c-MET, from early embryonic development to an adult stage. In addition, c-MET is a well-known proto-oncogene involved in the onset and progression of various human cancers. Herein, we have investigated the expression and availability of HGF and c-MET in TCam-2, NCCIT and NT2D1 cells, which are type II (T)GCT representative cell lines, and the effect of c-MET activation/repression on the regulation of cancerous biological processes. We found that NT2D1 cells increase their proliferation, polarized migration, and invasion in response to HGF administration. NCCIT cells respond to HGF stimulation only partially, whereas TCam-2 cells do not respond to HGF, at least according to the investigated parameters. Interestingly, the immunohistochemical study of c-MET distribution in TGCTs confirm its presence in both seminoma and non-seminoma lesions with different patterns. Notably, we found the highest c-MET immunoreactivity in the epithelial elements of the various components of TGCTs: teratoma, yolk sac tumor and choriocarcinoma. Type II testicular germ cell tumors (TGCTs) represent the most frequent malignancy in Caucasian males (20-40 years). Even if diagnosed with disseminated disease, > 80% of patients are cured; however, a small percentage of cases progress and result in death. It is commonly accepted that these cancers arise from a disturbed testicular embryonic niche that leads to the block of gonocyte differentiation. The subsequent development of the invasive seminomas and nonseminomas is due to a combination of genetic, epigenetic and microenvironmentbased alterations (genvironment). Hepatocyte growth factor (HGF) is present in the testicular microenvironment, together with its receptor c-MET, from early embryonic development to an adult stage. In addition, c-MET is a well-known proto-oncogene involved in the onset and progression of various human cancers. Herein, we have investigated the expression and availability of HGF and c-MET in TCam-2, NCCIT and NT2D1 cells, which are type II (T)GCT representative cell lines, and the effect of c-MET activation/repression on the regulation of cancerous biological processes. We found that NT2D1 cells increase their proliferation, polarized migration, and invasion in response to HGF administration. NCCIT cells respond to HGF stimulation only partially, whereas TCam-2 cells do not respond to HGF, at least according to the investigated parameters. Interestingly, the immunohistochemical study of c-MET distribution in TGCTs confirm its presence in both seminoma and non-seminoma lesions with different patterns. Notably, we found the highest c-MET immunoreactivity in the epithelial elements of the various components of TGCTs: teratoma, yolk sac tumor and choriocarcinoma.
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- 2018
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5. Inositol induces mesenchymal-epithelial reversion in breast cancer cells through cytoskeleton rearrangement
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Alessandro Palombo, Simona Dinicola, Mirko Minini, Saleh Alwasel, Alessandra Cucina, Mariano Bizzarri, Sara Proietti, Giulia Ricci, Angela Catizone, Abdel Halim Harrath, Maria Grazia Masiello, Gianmarco Fabrizi, Dinicola, Simona, Fabrizi, Gianmarco, Masiello, Maria Grazia, Proietti, Sara, Palombo, Alessandro, Minini, Mirko, Harrath, Abdel Halim, Alwasel, Saleh H., Ricci, Giulia, Catizone, Angela, Cucina, Alessandra, and Bizzarri, Mariano
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0301 basic medicine ,Mesoderm ,Cell membrane ,Phosphatidylinositol 3-Kinases ,chemistry.chemical_compound ,0302 clinical medicine ,Invasion ,Cell Movement ,Inositol ,Cytoskeleton ,emt ,met ,invasion ,motility ,Phosphorylation ,beta Catenin ,rho-Associated Kinases ,Medicine (all) ,Microfilament Proteins ,EMT ,NF-kappa B ,Motility ,Cell migration ,Cadherins ,Cell biology ,medicine.anatomical_structure ,030220 oncology & carcinogenesis ,MET ,Female ,Filopodia ,Immunoblotting ,Down-Regulation ,Breast Neoplasms ,macromolecular substances ,Biology ,03 medical and health sciences ,Cell Line, Tumor ,Presenilin-1 ,medicine ,Humans ,Vimentin ,Neoplasm Invasiveness ,Protein kinase B ,PI3K/AKT/mTOR pathway ,Fascin ,Wound Healing ,Epithelial Cells ,Cell Biology ,Enzyme Activation ,030104 developmental biology ,chemistry ,Cancer cell ,biology.protein ,Amyloid Precursor Protein Secretases ,Carrier Proteins ,Proto-Oncogene Proteins c-akt - Abstract
Inositol displays multi-targeted effects on many biochemical pathways involved in epithelial-mesenchymal transition (EMT). As Akt activation is inhibited by inositol, we investigated if such effect could hamper EMT in MDA-MB-231 breast cancer cells. In cancer cells treated with pharmacological doses of inositol E-cadherin was increased, β-catenin was redistributed behind cell membrane, and metalloproteinase-9 was significantly reduced, while motility and invading capacity were severely inhibited. Those changes were associated with a significant down-regulation of PI3K/Akt activity, leading to a decrease in downstream signaling effectors: NF-kB, COX-2, and SNAI1. Inositol-mediated inhibition of PS1 leads to lowered Notch 1 release, thus contributing in decreasing SNAI1 levels. Overall, these data indicated that inositol inhibits the principal molecular pathway supporting EMT. Similar results were obtained in ZR-75, a highly metastatic breast cancer line. These findings are coupled with significant changes on cytoskeleton. Inositol slowed-down vimentin expression in cells placed behind the wound-healing edge and stabilized cortical F-actin. Moreover, lamellipodia and filopodia, two specific membrane extensions enabling cell migration and invasiveness, were no longer detectable after inositol addiction. Additionally, fascin and cofilin, two mandatory required components for F-actin assembling within cell protrusions, were highly reduced. These data suggest that inositol may induce an EMT reversion in breast cancer cells, suppressing motility and invasiveness through cytoskeleton modifications.
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- 2016
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6. Nicotine increases colon cancer cell migration and invasion through epithelial to mesenchymal transition (EMT): COX-2 involvement
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Giulia Ricci, Angela Catizone, Gianmarco Fabrizi, Alessandra Cucina, Maria Grazia Masiello, Pierpaolo Coluccia, Mariano Bizzarri, Sara Proietti, Simona Dinicola, Giorgio De Toma, Dinicola, Simona, Masiello, Maria Grazia, Proietti, Sara, Coluccia, Pierpaolo, Fabrizi, Gianmarco, Catizone, Angela, Ricci, Giulia, De Toma, Giorgio, Bizzarri, Mariano, and Cucina, Alessandra
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0301 basic medicine ,Nicotine ,Epithelial-Mesenchymal Transition ,Physiology ,Colorectal cancer ,Clinical Biochemistry ,Antineoplastic Agents ,Biology ,migration ,Dinoprostone ,03 medical and health sciences ,0302 clinical medicine ,Cigarette smoking ,Antigens, CD ,Cell Movement ,medicine ,Humans ,Neoplasm Invasiveness ,Epithelial–mesenchymal transition ,Nitrobenzenes ,beta Catenin ,chemistry.chemical_classification ,Sulfonamides ,Cyclooxygenase 2 Inhibitors ,Mesenchymal stem cell ,EMT ,Colon cancer cell ,Cell Biology ,COX-2 ,invasion ,medicine.disease ,Cadherins ,Colon cancer ,nicotine ,physiology ,clinical biochemistry ,cell biology ,030104 developmental biology ,Enzyme ,chemistry ,Matrix Metalloproteinase 9 ,Cell culture ,Cyclooxygenase 2 ,030220 oncology & carcinogenesis ,Colonic Neoplasms ,Cancer research ,Carcinogens ,Matrix Metalloproteinase 2 ,Caco-2 Cells ,medicine.drug ,Signal Transduction - Abstract
Cigarette smoking is a recognized risk factor for colon cancer and nicotine, the principal active component of tobacco, plays a pivotal role in increasing colon cancer cell growth and survival. The aim of this study was to determine the effect of nicotine on cellular Caco-2 and HCT-8 migration and invasion, focusing on epithelial to mesenchymal transition (EMT) induction and COX-2 pathway involvement. In both these cell lines, treatment with nicotine increased COX-2 expression and the release of its enzymatic product PGE2 . Moreover, nicotine-stimulated cells showed increased migratory and invasive behavior, mesenchymal markers up-regulation and epithelial markers down-regulation, nuclear translocation of the β-catenin, increase of MMP-2 and MMP-9 activity and enhanced NF-κB expression. Noticeably, all these effects are largely mediated by COX-2 activity, since simultaneous treatment of both cell lines with nicotine and NS-398, a selective COX-2 inhibitor, greatly reduced the number of migrating and invading cells and reverted nicotine-induced EMT. These findings emphasize that nicotine triggers EMT, leading hence to increased migration and invasiveness of colon cancer cells. Thereby, the use of COX-2 inhibitor drugs might likely counteract nicotine-mediated EMT effects on colon cancer development and progression. This article is protected by copyright. All rights reserved.
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- 2017
7. ADP-ribose polymer depletion leads to nuclear Ctcf re-localization and chromatin rearrangement
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Tiziana Guastafierro, Anna Reale, Oliviano Martella, Angela Catizone, Margherita Miccheli, Dawn Farrar, Fabio Ciccarone, Maria Di Girolamo, Michele Zampieri, Roberta Calabrese, Maria Giulia Bacalini, Paola Caiafa, Elena Klenova, Guastafierro, Tiziana, Catizone, Angela, Calabrese, Roberta, Zampieri, Michele, Martella, Oliviano, Bacalini, Maria Giulia, Reale, Anna, Di Girolamo, Maria, Miccheli, Margherita, Farrar, Dawn, Klenova, Elena, Ciccarone, Fabio, and Caiafa, Paola
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CCCTC-Binding Factor ,Glycoside Hydrolase ,Poly (ADP-Ribose) Polymerase-1 ,CCCTC-binding factor (Ctcf) ,chromatin structure ,poly(ADP-ribose) glycohydrolase (Parg) ,poly(ADP-ribose) polymerase 1 (Parp1) ,poly(ADP-ribosyl) ation (PARylation) ,active transport ,cell nucleus ,adenosine diphosphate ribose ,amino acid substitution ,animals ,CCCTC-binding factor ,cell line ,chromatin assembly and disassembly ,DNA methylation ,gene knockdown techniques ,glycoside hydrolases ,lamins ,mice ,mutagenesis ,site-directed ,mutant proteins ,poly (ADP-ribose) polymerase-1 ,Poly(ADP-ribose) polymerase Inhibitors ,poly(ADP-ribose) polymerases ,recombinant fusion proteins ,repressor proteins ,Biochemistry ,Poly(ADP-ribose) Polymerase Inhibitor ,Mice ,0302 clinical medicine ,PARP1 ,Mutant Protein ,Cell Nucleu ,Poly(ADP-ribose) Polymerase ,0303 health sciences ,PARG ,Poly(ADP-ribose) glycohydrolase (Parg) ,Active Transport, Cell Nucleu ,Cell biology ,Chromatin ,medicine.anatomical_structure ,030220 oncology & carcinogenesis ,Poly ADP ribose polymerase ,Biology ,Chromatin structure ,Cell Line ,03 medical and health sciences ,Poly(ADP-ribose) polymerase 1 (Parp1) ,medicine ,Settore BIO/10 ,Molecular Biology ,030304 developmental biology ,Adenosine Diphosphate Ribose ,Animal ,Poly(ADP-ribosyl) ation (PARylation) ,Cell Biology ,DNA Methylation ,Repressor Protein ,Chromatin Assembly and Disassembly ,Molecular biology ,Cell nucleus ,Amino Acid Substitution ,CTCF ,Gene Knockdown Technique ,Mutagenesis, Site-Directed ,Lamin ,Recombinant Fusion Protein - Abstract
Ctcf (CCCTC-binding factor) directly induces Parp [poly(ADPribose) polymerase] 1 activity and its PARylation [poly(ADPribosyl) ation] in the absence of DNA damage. Ctcf, in turn, is a substrate for this post-synthetic modification and as such it is covalently and non-covalently modified by PARs (ADP-ribose polymers). Moreover, PARylation is able to protect certain DNA regions bound by Ctcf from DNA methylation. We recently reported that de novo methylation of Ctcf target sequences due to overexpression of Parg [poly(ADP-ribose)glycohydrolase] induces loss of Ctcf binding. Considering this, we investigate to what extent PARP activity is able to affect nuclear distribution of Ctcf in the present study. Notably, Ctcf lost its diffuse nuclear localization following PAR (ADP-ribose polymer) depletion and accumulated at the periphery of the nucleus where it was linked with nuclear pore complex proteins remaining external to the perinuclear Lamin B1 ring. We demonstrated that PAR depletion-dependent perinuclear localization of Ctcf was due to its blockage from entering the nucleus. Besides Ctcf nuclear delocalization, the outcome of PAR depletion led to changes in chromatin architecture. Immunofluorescence analyses indicated DNA redistribution, a generalized genomic hypermethylation and an increase of inactive compared with active chromatin marks in Parg-overexpressing or Ctcf-silenced cells. Together these results underline the importance of the cross-talk between Parp1 and Ctcf in the maintenance of nuclear organization. © The Authors Journal compilation © 2013 Biochemical Society.
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- 2013
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8. Poly(ADP-ribosyl)ation Acts in the DNA Demethylation of Mouse Primordial Germ Cells Also with DNA Damage-Independent Roles
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Angela Catizone, Massimo De Felici, Paola Caiafa, Maria Giulia Bacalini, Francesca Gioia Klinger, Fabio Ciccarone, Michele Zampieri, Roberta Calabrese, Ciccarone, Fabio, Klinger, Francesca Gioia, Catizone, Angela, Calabrese, Roberta, Zampieri, Michele, Bacalini, Maria Giulia, de Felici, Massimo, Caiafa, Paola, Department of Cellular Biotechnologies and Haematology, Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome]-Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Department of Public Health and Cell Biology, Università degli Studi di Roma Tor Vergata [Roma], Department of Anatomy, Histology, Forensic Medicine and Orthopedics, Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP), and Grants from Ministero della Salute (PC), from International FIRB 2006 (RBIN06E9Z8_003) and from Ministero dell'Istruzione, dell'Universita e della Ricerca (PRIN 2008, PC, MDF), Italy.
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Male ,Poly Adenosine Diphosphate Ribose ,Time Factors ,Mouse ,Poly (ADP-Ribose) Polymerase-1 ,lcsh:Medicine ,Mice ,MESH: DNA Methylation ,0302 clinical medicine ,PARP1 ,MESH: Reverse Transcriptase Polymerase Chain Reaction ,MESH: Gene Expression Regulation, Developmental ,Molecular Cell Biology ,MESH: Animals ,DNA (Cytosine-5-)-Methyltransferases ,lcsh:Science ,Poly(ADP-ribose) Polymerase ,Proto-Oncogene Protein ,0303 health sciences ,Settore BIO/17 ,Multidisciplinary ,Chromosome Biology ,Reverse Transcriptase Polymerase Chain Reaction ,Medicine (all) ,parp1 ,epigenetics ,dnmt1 ,tet1 ,5-hydroxymethylcytosine ,Gene Expression Regulation, Developmental ,Genomics ,Animal Models ,Chromatin ,MESH: DNA (Cytosine-5-)-Methyltransferase ,DNA-Binding Proteins ,MESH: Poly Adenosine Diphosphate Ribose ,DNA methylation ,Female ,Cellular Types ,Poly(ADP-ribose) Polymerases ,DNA modification ,Reprogramming ,Research Article ,DNA (Cytosine-5-)-Methyltransferase 1 ,Time Factor ,DNA damage ,DNA-Binding Protein ,Poly ADP ribose polymerase ,Blotting, Western ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,Biology ,Germ Cell ,03 medical and health sciences ,Model Organisms ,MESH: Analysis of Variance ,Proto-Oncogene Proteins ,Genetics ,MESH: Blotting, Western ,Animals ,Epigenetics ,MESH: Mice ,030304 developmental biology ,MESH: DNA Damage ,Analysis of Variance ,Biochemistry, Genetics and Molecular Biology (all) ,Animal ,MESH: Poly(ADP-ribose) Polymerases ,MESH: Time Factors ,lcsh:R ,MESH: Embryo, Mammalian ,[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology ,DNA Methylation ,Embryo, Mammalian ,Molecular biology ,MESH: Male ,MESH: Proto-Oncogene Proteins ,MESH: Germ Cells ,Germ Cells ,DNA demethylation ,Agricultural and Biological Sciences (all) ,DNA (Cytosine-5-)-Methyltransferase ,lcsh:Q ,Gene expression ,MESH: Female ,MESH: DNA-Binding Proteins ,030217 neurology & neurosurgery ,Developmental Biology ,DNA Damage - Abstract
Poly(ADP-ribosyl)ation regulates chromatin structure and transcription driving epigenetic events. In particular, Parp1 is able to directly influence DNA methylation patterns controlling transcription and activity of Dnmt1. Here, we show that ADP-ribose polymer levels and Parp1 expression are noticeably high in mouse primordial germ cells (PGCs) when the bulk of DNA demethylation occurs during germline epigenetic reprogramming in the embryo. Notably, Parp1 activity is stimulated in PGCs even before its participation in the DNA damage response associated with active DNA demethylation. We demonstrate that PARP inhibition impairs both genome-wide and locus-specific DNA methylation erasure in PGCs. Moreover, we evidence that impairment of PARP activity causes a significant reduction of expression of the gene coding for Tet1 hydroxylases involved in active DNA demethylation. Taken together these results demonstrate new and adjuvant roles of poly(ADP-ribosyl)ation during germline DNA demethylation and suggest its possible more general involvement in genome reprogramming. © 2012 Ciccarone et al.
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- 2012
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