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1.

001-es BibID:BIBFORM065564
Első szerző:Aguilera-Aguirre, Leopoldo
Cím:Whole transcriptome analysis reveals a role for OGG1-initiated DNA repair signaling in airway remodeling / Leopoldo Aguilera-Aguirre, Koa Hosoki, Attila Bacsi, Zsolt Radák, Sanjiv Sur, Muralidhar L. Hegde, Bing Tian, Alfredo Saavedra-Molina, Allan R. Brasier, Xueqing Ba, Istvan Boldogh
Dátum:2015
ISSN:0891-5849
Megjegyzések:Reactive oxygen species (ROS) generated by environmental exposures, and endogenously as by-products of respiration, oxidatively modify biomolecules including DNA. Accumulation of ROS-induced DNA damage has been implicated in various diseases that involve inflammatory processes, and efficient DNA repair is considered critical in preventing such diseases. One of the most abundant DNA base lesions is 7,8-dihydro-8-oxoguanine (8-oxoG), which is repaired by the 8-oxoguanine DNA glycosylase 1 (OGG1)-initiated base-excision repair (OGG1-BER) pathway. Recent studies have shown that the OGG1-BER by-product 8-oxoG base forms a complex with cytosolic OGG1, activating small GTPases and downstream cell signaling in cultured cells and lungs. This implies that persistent OGG1-BER could result in signaling leading to histological changes in airways. To test this, we mimicked OGG1-BER by repeatedly challenging airways with its repair product 8-oxoG base. Gene expression was analyzed by RNA sequencing (RNA-Seq) and qRT-PCR, and datasets were evaluated by gene ontology and statistical tools. RNA-Seq analysis identified 3252 differentially expressed transcripts (2435 up- and 817 downregulated, ? 3-fold change). Among the upregulated transcripts, 2080 mRNAs were identified whose encoded protein products were involved in modulation of the actin family cytoskeleton, extracellular matrix, cell adhesion, cadherin, and cell junctions, affecting biological processes such as tissue development, cell-to-cell adhesion, cell communication, and the immune system. These data are supported by histological observations showing epithelial alterations, subepithelial fibrosis, and collagen deposits in the lungs. These data imply that continuous challenge by the environment and consequent OGG1-BER-driven signaling trigger gene expression consistent with airway remodeling.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
8-Oxoguanine
Airway remodeling
OGG1-BER
Megjelenés:Free Radical Biology And Medicine 89 (2015), p. 20-33. -
További szerzők:Hosoki, Koa Bácsi Attila (1967-) (immunológus) Radák Zsolt Sur, Sanjiv Hegde, Muralidhar L. Tian, Bing Saavedra-Molina, Alfredo Brasier, Allan R. Ba, Xueqing Boldogh István
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2.

001-es BibID:BIBFORM055556
035-os BibID:(scopus)84907867357 (wos)000343109700119
Első szerző:Ba, Xueqing
Cím:The Role of 8-Oxoguanine DNA Glycosylase-1 in Inflammation / Xueqing Ba, Leopoldo Aguilera-Aguirre, Qura Tul Ain Nmi Rashid, Attila Bacsi, Zsolt Radak, Sanjiv Sur, Koa Hosoki, Muralidhar L. Hegde, Istvan Boldogh
Dátum:2014
ISSN:1661-6596 1422-0067
Megjegyzések:Many, if not all, environmental pollutants/chemicals and infectious agents increase intracellular levels of reactive oxygen species (ROS) at the site of exposure. ROS not only function as intracellular signaling entities, but also induce damage to cellular molecules including DNA. Among the several dozen ROS-induced DNA base lesions generated in the genome, 8-oxo-7,8-dihydroguanine (8-oxoG) is one of the most abundant because of guanine's lowest redox potential among DNA bases. In mammalian cells, 8-oxoG is repaired by the 8-oxoguanine DNA glycosylase-1 (OGG1)-initiated DNA base excision repair pathway (OGG1-BER). Accumulation of 8-oxoG in DNA has traditionally been associated with mutagenesis, as well as various human diseases and aging processes, while the free 8-oxoG base in body fluids is one of the best biomarkers of ongoing pathophysiological processes. In this review, we discuss the biological significance of the 8-oxoG base and particularly the role of OGG1-BER in the activation of small GTPases and changes in gene expression, including those that regulate pro-inflammatory chemokines/cytokines and cause inflammation.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:International Journal of Molecular Sciences. - 15 : 9 (2014), p. 16975-16997. -
További szerzők:Aguilera-Aguirre, Leopoldo Rashid, Qura Tul Ain Nmi Bácsi Attila (1967-) (immunológus) Radák Zsolt Sur, Sanjiv Hosoki, Koa Hegde, Muralidhar L. Boldogh István
Pályázati támogatás:TAMOP 4.2.2.A-11/1/KONV-2012-2023
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3.

001-es BibID:BIBFORM091749
Első szerző:Boldogh István
Cím:OGG1 at the Crossroads of Inflammation and DNA Base Excision Repair / I. Boldogh, L. Pan, S. Vlahopoulos, X. Zheng, K. Wang, T. K. Hazra, M. L. Hegde, A. Bacsi, Z. Radak, A. R. Brasier, X. Ba
Dátum:2020
Megjegyzések:Oxidative modification(s) to nucleic acid bases are an unavoidable consequence of reactions by reactive oxygen species. Arguably, the most abundant ROS-generated lesion in nuclear and mitochondrial DNA is 7, 8-dihydro-8-oxoguanine (8-oxoGua), which is repaired primarily by 8-oxoguanine DNA glycosylase 1, in the OGG1-initiated base excision repair pathway. Deficiency in OGG1 repair is believed to have role(s) in development and progression of various disease processes, including neurodegenerative, cardiovascular, metabolic diseases, and aging-associated pathologies. The common link among these diseases is acute/chronic inflammatory processes. Emerging data support the idea that OGG1-induced adjustments in DNA structure at genomic 8-oxoGua with or without excision, serve as a nucleation site for transcription factor binding allowing prompt expression of genes, essential for reestablishment of a homeostatic state via innate and adaptive immune responses after exposure to biological and/or cytotoxic agents. As part of the immune defenses, OGG1 in complex with a free 8-oxoGua base also exerts transcriptional control via small GTPase signaling pathways. These data are consistent with the limited immune responses of Ogg1 knockout mice. Thus, evolution integrated genome maintenance by OGG1-BER and control host homeostatic state via inflammation, which, if not controlled, can be one of the mechanistic explanations for OGG1's previously proposed link to diseases and aging processes.
ISBN:978-1-83916-251-0; 978-1-83916-254-1; 978-1-83916-256-5
Tárgyszavak:Természettudományok Biológiai tudományok könyvfejezet
könyvrészlet
OGG1
Megjelenés:DNA Damage, DNA Repair and Disease: Volume 2 / Eds. Miral Dizdaroglu, R. Stephen Lloyd. - p. 75-103. -
További szerzők:Pan, Lang Vlahopoulos, Spiros A. Zheng, Xiaoxiang Wang, K. Hazra, Tapas K. Hegde, Muralidhar L. Bácsi Attila (1967-) (immunológus) Radák Zsolt Brasier, Allan R. Ba, Xueqing
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4.

001-es BibID:BIBFORM041839
Első szerző:Boldogh István
Cím:Activation of ras signaling pathway by 8-oxoguanine DNA glycosylase bound to its excision product, 8-oxoguanine / Istvan Boldogh, Gyorgy Hajas, Leopoldo Aguilera-Aguirre, Muralidhar L. Hegde, Zsolt Radak, Attila Bacsi, Sanjiv Sur, Tapas K. Hazra, Sankar Mitra
Dátum:2012
ISSN:0021-9258
Megjegyzések:8-Oxo-7,8-dihydroguanine (8-oxoG), arguably the most abundant base lesion induced in mammalian genomes by reactive oxygen species, is repaired via the base excision repair pathway that is initiated with the excision of 8-oxoG by OGG1. Here we show that OGG1 binds the 8-oxoG base with high affinity and that the complex then interacts with canonical Ras family GTPases to catalyze replacement of GDP with GTP, thus serving as a guanine nuclear exchange factor. OGG1-mediated activation of Ras leads to phosphorylation of the mitogen-activated kinases MEK1,2/ERK1,2 and increasing downstream gene expression. These studies document for the first time that in addition to its role in repairing oxidized purines, OGG1 has an independent guanine nuclear exchange factor activity when bound to 8-oxoG.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry 287 : 25 (2012), p. 20769-20773. -
További szerzők:Hajas György (1970-) (biológus) Aguilera-Aguirre, Leopoldo Hegde, Muralidhar L. Radák Zsolt Bácsi Attila (1967-) (immunológus) Sur, Sanjiv Hazra, Tapas K. Mitra, Sankar
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5.

001-es BibID:BIBFORM065562
Első szerző:Germán Péter (gyermekgyógyász)
Cím:8-Oxoguanine DNA glycosylase1-driven DNA repair : a paradoxical role in lung aging / Peter German, David Saenz, Peter Szaniszlo, Leopoldo Aguilera-Aguirre, Lang Pan, Muralidhar L. Hegde, Attila Bacsi, Gyorgy Hajas, Zsolt Radak, Xueqing Ba, Sankar Mitra, John Papaconstantinou, Istvan Boldogh
Dátum:2017
ISSN:0047-6374
Megjegyzések:Age-associated changes in lung structure and function are some of the most important predictors of overall health, cognitive activities and longevity. Common to all aging cells is an increase in oxidatively modified DNA bases, primarily 8-oxo-7,8-dihydroguanine (8-oxoG). It is repaired via DNA base excision repair pathway driven by 8-oxoguanine DNA glycosylase-1 (OGG1-BER), whose role in aging has been the focus of many studies. This study hypothesizes that signaling and consequent gene expression during cellular response to OGG1-BER "wires" senescence/aging processes. To test OGG1-BER was mimicked by repeatedly exposing diploid lung fibroblasts cells and airways of mice to 8-oxoG base. Results showed that repeated exposures led to G1 cell cycle arrest and pre-matured senescence of cultured cells in which over 1000 genes were differentially expressed -86% of them been identical to those in naturally senesced cells. Gene ontology analysis of gene expression displayed biological processes driven by small GTPases, phosphoinositide 3-kinase and mitogen activated kinase cascades both in cultured cells and lungs. These results together, points to a new paradigm about the role of DNA damage and repair by OGG1 in aging and age-associated disease processes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
OGG1
8-oxoguanine
Senescence
Aging
Megjelenés:Mechanisms Of Ageing And Development 161 : Pt A (2017), p. 51-65. -
További szerzők:Saenz, David N. Szaniszló Péter Aguilera-Aguirre, Leopoldo Pan, Lang Hegde, Muralidhar L. Bácsi Attila (1967-) (immunológus) Hajas György (1970-) (biológus) Radák Zsolt Ba, Xueqing Mitra, Sankar Papaconstantinou, John Boldogh István
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6.

001-es BibID:BIBFORM047640
Első szerző:Germán Péter (gyermekgyógyász)
Cím:Activation of cellular signaling by 8-oxoguanine DNA glycosylase-1-initiated DNA base excision repair / Peter German, Peter Szaniszlo, Gyorgy Hajas, Zsolt Radak, Attila Bacsi, Tapas K. Hazra, Muralidhar L. Hegde, Xueqing Ba, Istvan Boldogh
Dátum:2013
ISSN:1568-7864
Megjegyzések:Accumulation of 8-oxo-7,8-dihydroguanine (8-oxoG) in the DNA results in genetic instability and mutagenesis, and is believed to contribute to carcinogenesis, aging processes and various aging-related diseases. 8-OxoG is removed from the DNA via DNA base excision repair (BER), initiated by 8-oxoguanine DNA glycosylase-1 (OGG1). Our recent studies have shown that OGG1 binds its repair product 8-oxoG base with high affinity at a site independent from its DNA lesion-recognizing catalytic site and the OGG1?8-oxoG complex physically interacts with canonical Ras family members. Furthermore, exogenously added 8-oxoG base enters the cells and activates Ras GTPases; however, a link has not yet been established between cell signaling and DNA BER, which is the endogenous source of the 8-oxoG base. In this study, we utilized KG-1 cells expressing a temperature-sensitive mutant OGG1, siRNA ablation of gene expression, and a variety of molecular biological assays to define a link between OGG1-BER and cellular signaling. The results show that due to activation of OGG1-BER, 8-oxoG base is released from the genome in sufficient quantities for activation of Ras GTPase and resulting in phosphorylation of the downstream Ras targets Raf1, MEK1,2 and ERK1,2. These results demonstrate a previously unrecognized mechanism for cellular responses to OGG1-initiated DNA BER.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Ogg1
Base excision repair
Cell signaling
Megjelenés:Dna Repair. - 12 : 10 (2013), p. 856-863. -
További szerzők:Szaniszló Péter Hajas György (1970-) (biológus) Radák Zsolt Bácsi Attila (1967-) (immunológus) Hazra, Tapas K. Hegde, Muralidhar L. Ba, Xueqing Boldogh István
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7.

001-es BibID:BIBFORM047651
Első szerző:Hajas György (biológus)
Cím:8-Oxoguanine DNA glycosylase-1 links DNA repair to cellular signaling via the activation of the small GTPase Rac1 / Gyorgy Hajas, Attila Bacsi, Leopoldo Aguilera-Aguirre, Muralidhar L. Hegde, K. Hazra Tapas, Sanjiv Sur, Zsolt Radak, Xueqing Ba, Istvan Boldogh
Dátum:2013
ISSN:0891-5849
Megjegyzések:8-Oxo-7,8-dihydroguanine (8-oxoG) is one of the most abundant DNA base lesions induced by reactive oxygen species (ROS). Accumulation of 8-oxoG in the mammalian genome is considered a marker of oxidative stress, to be causally linked to inflammation, and is thought to contribute to aging processes and various aging-related diseases. Unexpectedly, mice that lack 8-oxoguanine DNA glycosylase-1 (OGG1) activity and accumulate 8-oxoG in their genome have a normal phenotype and longevity; in fact, they show increased resistance to both inflammation and oxidative stress. OGG1 excises and generates free 8-oxoG base during DNA base-excision repair (BER) processes. In the present study, we report that in the presence of the 8-oxoG base, OGG1 physically interacts with guanine nucleotide-free and GDP-bound Rac1 protein. This interaction results in rapid GDP?GTP, but not GTP?GDP, exchange in vitro. Importantly, a rise in the intracellular 8-oxoG base levels increases the proportion of GTP-bound Rac1. In turn Rac1-GTP mediates an increase in ROS levels via nuclear membrane-associated NADPH oxidase type 4. These results show a novel mechanism by which OGG1 in complex with 8-oxoG is linked to redox signaling and cellular responses.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
8-Oxoguanine DNA glycosylase-1
8-Oxoguanine
Rac1 GTPase
Megjelenés:Free Radical Biology And Medicine. - 61C (2013), p. 384-394. -
További szerzők:Bácsi Attila (1967-) (immunológus) Aguilera-Aguirre, Leopoldo Hegde, Muralidhar L. Tapas, K. Hazra Sur, Sanjiv Radák Zsolt Ba, Xueqing Boldogh István
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8.

001-es BibID:BIBFORM055557
Első szerző:Luo, Jixian
Cím:8-Oxoguanine DNA glycosylase-1-mediated DNA repair is associated with Rho GTPase activation and α-smooth muscle actin polymerization / Jixian Luo, Koa Hosoki, Attila Bacsi, Zsolt Radak, Muralidhar L. Hegde, Sanjiv Sur, Tapas K. Hazra, Allan R. Brasier, Xueqing Ba, Istvan Boldogh
Dátum:2014
ISSN:0891-5849
Megjegyzések:Reactive oxygen species (ROS) are activators of cell signaling and modify cellular molecules, including DNA. 8-Oxo-7,8-dihydroguanine (8-oxoG) is one of the prominent lesions in oxidatively damaged DNA, whose accumulation is causally linked to various diseases and aging processes, whereas its etiological relevance is unclear. 8-OxoG is repaired by the 8-oxoguanine DNA glycosylase-1 (OGG1)-initiated DNA base excision repair (BER) pathway. OGG1 binds free 8-oxoG and this complex functions as an activator of Ras family GTPases. Here we examined whether OGG1-initiated BER is associated with the activation of Rho GTPase and mediates changes in the cytoskeleton. To test this possibility, we induced OGG1-initiated BER in cultured cells and mouse lungs and used molecular approaches such as active Rho pull-down assays, siRNA ablation of gene expression, immune blotting, and microscopic imaging. We found that OGG1 physically interacts with Rho GTPase and, in the presence of 8-oxoG base, increases Rho-GTP levels in cultured cells and lungs, which mediates ?-smooth muscle actin (?-SMA) polymerization into stress fibers and increases the level of ?-SMA in insoluble cellular/tissue fractions. These changes were absent in cells lacking OGG1. These unexpected data and those showing that 8-oxoG repair is a lifetime process suggest that, via Rho GTPase, OGG1 could be involved in the cytoskeletal changes and organ remodeling observed in various chronic diseases.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Free Radical Biology and Medicine. - 73 (2014), p. 430-438. -
További szerzők:Hosoki, Koa Bácsi Attila (1967-) (immunológus) Radák Zsolt Hegde, Muralidhar L. Sur, Sanjiv Hazra, Tapas K. Brasier, Allan R. Ba, Xueqing Boldogh István
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9.

001-es BibID:BIBFORM069722
Első szerző:Pan, Lang
Cím:Oxidized Guanine Base Lesions Function in 8-Oxoguanine DNA Glycosylase-1-mediated Epigenetic Regulation of Nuclear Factor ?B-driven Gene Expression / Lang Pan, Bing Zhu, Wenjing Hao, Xianlu Zeng, Spiros A. Vlahopoulos, Tapas K. Hazra, Muralidhar L. Hegde, Zsolt Radak, Attila Bacsi, Allan R. Brasier, Xueqing Ba, Istvan Boldogh
Dátum:2016
ISSN:0021-9258 1083-351X
Megjegyzések:A large percentage of redox-responsive gene promoters containevolutionarily conserved guanine-rich clusters; guaninesare the bases most susceptible to oxidative modification(s). Consequently,7,8-dihydro-8-oxoguanine (8-oxoG) is one of themost abundant base lesions in promoters and is primarilyrepaired via the 8-oxoguanine DNA glycosylase-1 (OOG1)-initiatedbase excision repair pathway. In view of a prompt cellularresponse to oxidative challenge, we hypothesized that the8-oxoG lesion and the cognate repair protein OGG1 are utilizedin transcriptional gene activation. Here, we document TNF -induced enrichment of both 8-oxoG and OGG1 in promoters ofpro-inflammatory genes, which precedes interaction of NF- Bwith its DNA-binding motif. OGG1 bound to 8-oxoG upstreamfrom the NF- B motif increased its DNA occupancy by promotingan on-rate of both homodimeric and heterodimeric forms ofNF- B. OGG1 depletion decreased both NF- B binding andgene expression, whereas Nei-like glycosylase-1 and -2 had amarginal effect. These results are the first to document a novelparadigm wherein the DNA repair protein OGG1 bound to itssubstrate is coupled to DNA occupancy of NF- B and functionsin epigenetic regulation of gene expression.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
8-oxoguanine DNA glycosylase1
8-oxoguanine
NF-kappaB
gene expression
inflammation
Megjelenés:Journal Of Biological Chemistry 291 : 49 (2016), p. 25553-25566. -
További szerzők:Zhu, Bing Hao, Wenjing Zeng, Xianlu Vlahopoulos, Spiros A. Hazra, Tapas K. Hegde, Muralidhar L. Radák Zsolt Bácsi Attila (1967-) (immunológus) Brasier, Allan R. Ba, Xueqing Boldogh István
Pályázati támogatás:United States National Institute of Environmental Health and Sciences (grant number: RO1 ES018948 to IB)
Egyéb
United States National Institute of Allergic and Infectious Diseases (grant number: PO1-AI062885, to ARB and IB)
Egyéb
United States National Institute of Environmental Health and Sciences Center Grant (grant number: P30 ES006676 to ARB, IB)
Egyéb
National Science Foundation of China (grant number: 31571339 to XB)
Egyéb
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