Distinct Repair Activities of Human 7,8-Dihydro-8-oxoguanine DNA Glycosylase and Formamidopyrimidine DNA Glycosylase for Formamidopyrimidine and 7,8-Dihydro-8-oxoguanine

Asagoshi, Kenjiro; Yamada, Takao; Terato, Hiroaki; Ohyama, Yoshihiko; Monden, Yoshiaki; Arai, T.; Nishimura, Susumu; Aburatani, Hiroyuki; Lindahl, Tomas; Ide, Hiroshi

doi:10.1074/jbc.275.7.4956

Cited by 109 publications

(121 citation statements)

References 41 publications

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“…The former is generated by reaction of guanine with ROS [40]. The latter is generated by bind 2'-deoxyribose to 8-oxo-guanie [41]. Among the formed aldehydes, 4-HNE is the major product of lipid peroxidation, and it has been suggested to play a major role in tissue toxicity associated with lipid peroxidation [42].…”

Section: Discussionmentioning

confidence: 99%

Enhanced intrarenal oxidative stress and angiotensinogen in IgA nephropathy patients

Kobori

Katsurada

Ozawa

et al. 2007

Biochemical and Biophysical Research Communications

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This study was performed to determine whether immunoreactivity of intrarenal hemeoxygenase-1 and angiotensinogen are increased in IgA nephropathy (IgAN) patients. Hemeoxygenase-1 and angiotensinogen immunoreactivity were determined by immunohistochemistry robot system in renal specimens from 39 patients with IgAN. Normal portions of surgically resected kidney served as controls. IgAN patients showed moderate proteinuria (1.1+/−0.2 g/day); however, the control group did not show any proteinuria. Immunoreactivity of intrarenal hemeoxygenase-1 and angiotensinogen in IgAN were significantly increased compared to normal kidneys (2.42+/−0.42 vs 1.00+/−0.26 for hemeoxygenase-1 and 4.05+/−0.40 vs 1.00+/−0.21 for angiotensinogen, arbitrary unit). Even though these IgAN patients did not show massive renal damage, hemeoxygenase-1 and angiotensinogen immunoreactivity were increased in these patients at this time point. These data suggest that activated intrarenal reactive oxygen species-angiotensinogen axis plays some roles in development of IgAN at the early stage and will provide supportive foundation of effectiveness of the renin-angiotensin system blockade in IgAN.

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Section: Discussionmentioning

confidence: 99%

Enhanced intrarenal oxidative stress and angiotensinogen in IgA nephropathy patients

Kobori

Katsurada

Ozawa

et al. 2007

Biochemical and Biophysical Research Communications

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“…For example, OGG1 compares unfavorably in both its affinity for 8-oxoG in DNA [7], and its turn-over rate (K cat ) at 8-oxoG-containing substrates [8]. This has led several investigators to suggest that human OGG1 remains bound to the AP site formed as an intermediate in the excision repair process and that other BER proteins may be necessary for dislodging OGG1 to produce a more vigorous turnover rate.…”

Section: Introductionmentioning

confidence: 99%

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

2007

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Besides its role in translation and ribosome maturation, human ribosomal protein S3 (hS3) is implicated in DNA damage recognition as reflected by its affinity for abasic sites and 7, 8-dihydro-8-oxoguanine (8-oxoG) residues in DNA in vitro. Here, we demonstrate that hS3 is capable of carrying out both roles by its ex vivo translocation from the cytoplasm to the nucleus as a consequence of genotoxic stress. The translocation of hS3 is dependent on ERK1/2-mediated phosphorylation of a threonine residue (T42) of hS3. Two different ectopically expressed site-directed mutants of T42 failed to respond to conditions of genotoxic stress, thus providing a link between DNA damage and ERK1/2 dependent phosphorylation of hS3. Lastly, hS3 was traced in exposed cells to its colocalization with 8-oxoG foci, raising the possibility that hS3 is a member of a cellular DNA damage response pathway that results in its interaction with sites of DNA damage.

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“…10 The ability to excise FapyA is thus a major substrate difference between the 2 enzymes. Further, in a direct comparison of kinetics parameters, Asagoshi et al 7 observed that FPG releases 8-oxoG and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (me-Fapy) 80-fold faster than hOGG1. FPG thus exhibits higher velocity and wider substrate specificity than hOGG1.…”

mentioning

confidence: 99%

“…6 In vitro studies have described the poor catalytic properties of hOGG1, the major DNA glycosylase for 8-oxoG in human cells. 7,8 The threat to genome integrity represented by oxidized purines could be reduced in human cells by expression of efficient repair activities obtained from heterologous sources. 9 The E. coli formamidopyrimidine DNA glycosylase (FPG) protein differs from hOGG1 under several aspects.…”

mentioning

confidence: 99%

Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein

Ropolo¹,

Geroldi²,

Degan³

et al. 2005

Intl Journal of Cancer

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Repair of some oxidized purines such as 8-oxo-7,8-dihydroguanine (8-oxoG) is inefficient in human cells in comparison to repair of other major endogenous lesions (e.g. uracil, abasic sites or oxidized pyrimidines). This is due to the poor catalytic properties of hOGG1, the major DNA glycosylase involved in 8-oxoG removal. The formamidopyrimidine DNA glycosylase (FPG) protein from E. coli is endowed with a potent 8-oxoG glycolytic activity coupled with a b,d-AP lyase. In this study, we have expressed FPG fused to the enhanced green fluorescent protein (EGFP) in human bladder cells to accelerate the repair of oxidative DNA damage. Cells expressing the fusion protein EGFP-FPG repaired 8-oxoG and AP sites at accelerated rates, in particular via the single-nucleotide insertion base excision repair (BER) pathway and were resistant to mutagenicity of the oxidizing carcinogen potassium bromate. FPG may stably protect human cells from some harmful effects of oxidative DNA damage. ' 2005 Wiley-Liss, Inc.Key words: DNA base excision repair; oxidative DNA damage; overexpression; antimutagenesis; FPG protein Reactive oxygen species (ROS) are formed continuously as a consequence of normal cellular metabolism and are further increased during inflammation and exposure to external agents such as UV or ionizing radiations. They have been implicated in a number of tumours and links have been also suggested with neurological, endocrine and cardiovascular disorders. 1 Among ROS, the highly reactive hydroxyl radical (AEOH) adds to the C8 positions of purines generating C8-OH adduct radicals. Oxidation of these intermediates yields 8-oxo-7,8-dihydroguanine (8-oxoG) and 8-oxo-7,8-dihydroadenine (8-oxoA), 2 lesions that form at detectable rates under physiological conditions 1,2 and mispair frequently during DNA replication. 1,3 The one-electron reduction of the C8-OH adduct radicals yields instead 2 imidazole ring-opened purines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino-5-formamidopyrimidine (Fapy A) that also have miscoding properties. The hazard to genome integrity represented by some of these lesions (notably 8-oxoG) is further increased by the poor efficiency of their repair in human cells as compared to repair of other frequent endogenous lesions such as deaminated cytosine (U), base loss (AP) sites or a number of oxidized pyrimidines. [4][5][6] The slowness of 8-oxoG repair has been confirmed in living human cells where 8-oxodG was the second most persistent lesion among eleven oxidized bases. 6 In vitro studies have described the poor catalytic properties of hOGG1, the major DNA glycosylase for 8-oxoG in human cells. 7,8 The threat to genome integrity represented by oxidized purines could be reduced in human cells by expression of efficient repair activities obtained from heterologous sources. 9 The E. coli formamidopyrimidine DNA glycosylase (FPG) protein differs from hOGG1 under several aspects. hOGG1 only excises from DNA 8-oxoG and FapyG, while FPG fastly releases 8-oxoG, FapyG and FapyA with s...

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Distinct Repair Activities of Human 7,8-Dihydro-8-oxoguanine DNA Glycosylase and Formamidopyrimidine DNA Glycosylase for Formamidopyrimidine and 7,8-Dihydro-8-oxoguanine

Cited by 109 publications

References 41 publications

Enhanced intrarenal oxidative stress and angiotensinogen in IgA nephropathy patients

Enhanced intrarenal oxidative stress and angiotensinogen in IgA nephropathy patients

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein

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