Salvage of oxidized guanine derivatives in the (2'-deoxy)ribonucleotide pool as source of mutations in DNA

Mutation Research - Genetic Toxicology and Environmental Mutagenesis

Volumn 703, Issue 1, 2010, Pages 11-17

  Henderson, Paul T ^a   Evans, Mark D ^b   Cooke, Marcus S ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

8 oxodG; Accelerator mass Spectrometry; DNA repair; Nucleotide pool oxidation; Salvage

Indexed keywords

8 HYDROXYDEOXYGUANOSINE; 8 HYDROXYGUANINE; GUANINE DERIVATIVE;

ANIMAL EXPERIMENT; DNA REPAIR; GENE MUTATION; IMMUNOASSAY; MOUSE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM; REVIEW;

ANIMALS; DEOXYGUANOSINE; DNA DAMAGE; DNA REPAIR; GUANINE; HUMANS; MUTATION; OXIDATIVE STRESS;

EID: 78549267773     PISSN: 13835718     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrgentox.2010.08.021     Document Type: Review

References (112)

1. Dizdaroglu M. Determination of free radical-induced damage to DNA. Free Radic. Biol. Med. 1991, 10:225-242.
2. Evans M.D., Dizdaroglu M., Cooke M.S. Oxidative DNA damage and disease: induction, repair and significance. Mutat. Res. 2004, 567:1-61.
3. Alam Z.I, Jenner A., Daniel S.E., Lees A.J., Cairns N., Marsden C.D., Jenner P., Halliwell B. Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J. Neurochem. 1997, 69:1196-1203.
4. Hollstein M., Sidransky D., Vogelstein B., Harris C.C. p53 mutations in human cancers. Science 1991, 253:49-53.
5. Beal M.F. Mitochondria, oxidative damage, and inflammation in Parkinson's disease. Ann. N. Y. Acad. Sci. 2003, 991:120-131.
6. Halliwell B Biochemistry of oxidative stress. Biochem. Soc. Trans. 2007, 35:1147-1150.
7. Halliwell B. Oxidative stress and cancer: have we moved forward?. Biochem. J. 2007, 401:1-11.
8. Gruber J., Schaffer S., Halliwell B. The mitochondrial free radical theory of ageing-where do we stand?. Front Biosci. 2008, 13:6554-6579.
9. Cooke M.S., Olinski R., Loft S. Measurement and meaning of oxidatively modified DNA lesions in urine. Cancer Epidemiol. Biomarkers Prev. 2008, 17:3-14.
10. Cooke M.S., Henderson P.T., Evans M.D. Sources of extracellular, oxidatively-modified DNA lesions: implications for their measurement in urine. J. Clin. Biochem. Nutr. 2009, 45:255-270.
11. Loft S, Moller P., Cooke M.S., Rozalski R., Olinski R. Antioxidant vitamins and cancer risk: is oxidative damage to DNA a relevant biomarker?. Eur. J. Nutr. 2008, 47(Suppl. 2):19-28.
12. Gedik C.M., Collins A. Establishing the background level of base oxidation in human lymphocyte DNA: results of an interlaboratory validation study. FASEB J. 2005, 19:82-84.
13. Guetens G., De Boeck G., Highley M., van Oosterom A.T., De Bruijn E.A. Oxidative DNA damage: biological significance and methods of analysis. Crit Rev. Clin. Lab Sci. 2002, 39:331-457.
14. Mangal D., Vudathala D., Park J.H., Lee S.H., Penning T.M., Blair I.A. Analysis of 7,8-dihydro-8-oxo-2'-deoxyguanosine in cellular DNA during oxidative stress. Chem. Res. Toxicol. 2009, 22:788-797.
15. Boysen G., Collins L.B., Liao S., Luke A.M., Pachkowski B.F., Watters J.L., Swenberg J.A. Analysis of 8-oxo-7,8-dihydro-2'-deoxyguanosine by ultra high pressure liquid chromatography-heat assisted electrospray ionization-tandem mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2010, 878:375-380.
16. Hayakawa H., Taketomi A., Sakumi K., Kuwano M., Sekiguchi M. Generation and elimination of 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate, a mutagenic substrate for DNA synthesis, in human cells. Biochemistry 1995, 34:89-95.
17. Hah S.S., Kim H.M., Sumbad R.A., Henderson P.T. Hydantoin derivative formation from oxidation of 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-oxodG) and incorporation of C-14-labeled 8-oxodG into the DNA of human breast cancer cells. Bioorg. Med. Chem. Lett. 2005, 15:3627-3631.
18. Hah S.S., Mundt J.M., Kim H.M., Sumbad R.A., Turteltaub K.W., Henderson P.T. Measurement of 7,8-dihydro-8-oxo-2'-deoxyguanosine metabolism in MCF-7 cells at low concentrations using accelerator mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:11203-11208.
19. Mundt J.M., Hah S.S., Sumbad R.A., Schramm V., Henderson P.T. Incorporation of extracellular 8-oxodG into DNA and RNA requires purine nucleoside phosphorylase in MCF-7 cells. Nucleic Acids Res. 2008, 36:228-236.
20. Werner A. Reversed-phase and ion-pair separations of nucleotides, nucleosides and nucleobases: analysis of biological samples in health and disease. J. Chromatogr. 1993, 618:3-14.
21. Huang D, Zhang Y., Chen X. Analysis of intracellular nucleoside triphosphate levels in normal and tumor cell lines by high-performance liquid chromatography. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2003, 784:101-109.
22. Floyd R.A., Watson J.J., Wong P.K., Altmiller D.H., Rickard R.C. Hydroxyl free radical adduct of deoxyguanosine: sensitive detection and mechanisms of formation. Free Radic. Res. Commun. 1986, 1:163-172.
23. Kasai H., Crain P.F., Kuchino Y., Nishimura S., Ootsuyama A., Tanooka H. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis 1986, 7:1849-1851.
24. Turk P.W., Weitzman S.A. Free radical DNA adduct 8-OH-deoxyguanosine affects activity of Hpa II and Msp I restriction endonucleases. Free Radic. Res. 1995, 23:255-258.
25. Halliwell B., Dizdaroglu M. The measurement of oxidative damage to DNA by HPLC and GC/MS techniques. Free Radic. Res. Commun. 1992, 16:75-87.
26. Weimann A., Belling D., Poulsen H.E. Quantification of 8-oxo-guanine and guanine as the nucleobase, nucleoside and deoxynucleoside forms in human urine by high-performance liquid chromatography-electrospray tandem mass spectrometry. Nucleic Acids Res. 2002, 30:E7.
27. Rozalski R, Siomek A., Gackowski D., Foksinski M., Gran C., Klungland A., Olinski R. Diet is not responsible for the presence of several oxidatively damaged DNA lesions in mouse urine. Free Radic. Res. 2004, 38:1201-1205.
28. Cooke M.S., Evans M.D., Dove R., Rozalski R., Gackowski D., Siomek A., Lunec J., Olinski R. DNA repair is responsible for the presence of oxidatively damaged DNA lesions in urine. Mutat. Res. Fundam. Mol. Mech. Mutagen. 2005, 574:58-66.
29. Lin H.S., Jenner A.M., Ong C.N., Huang S.H., Whiteman M., Halliwell B. A high-throughput and sensitive methodology for the quantification of urinary 8-hydroxy-2'-deoxyguanosine: measurement with gas chromatography-mass spectrometry after single solid-phase extraction. Biochem. J. 2004, 380:541-548.
30. Cooke M.S., Singh R., Hall G.K., Mistry V., Duarte T.L., Farmer P.B., Evans M.D. Evaluation of enzyme-linked immunosorbent assay and liquid chromatography-tandem mass spectrometry methodology for the analysis of 8-oxo-7,8-dihydro-2'-deoxyguanosine in saliva and urine. Free Radic. Biol. Med. 2006, 41:1829-1836.
31. Weimann A., Belling D., Poulsen H.E. Measurement of 8-oxo-2'-deoxyguanosine and 8-oxo-2'-deoxyadenosine in DNA and human urine by high performance liquid chromatography-electrospray tandem mass spectrometry. Free Radic. Biol. Med. 2001, 30:757-764.
32. Evans M.D., Singh R., Mistry V., Sandhu K., Farmer P.B., Cooke M.S. Analysis of urinary 8-oxo-7,8-dihydro-purine-2'-deoxyribonucleosides by LC-MS/MS and improved ELISA. Free Radic. Res. 2008, 42:831-840.
33. Turteltaub K.W., Felton J.S., Gledhill B.L., Vogel J.S., Southon J.R., Caffee M.W., Finkel R.C., Nelson D.E., Proctor I.D., Davis J.C. Accelerator mass spectrometry in biomedical dosimetry: relationship between low-level exposure and covalent binding of heterocyclic amine carcinogens to DNA. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:5288-5292.
34. Dingley K.H., Roberts M.L., Velsko C.A., Turteltaub K.W. Attomole detection of 3H in biological samples using accelerator mass spectrometry: application in low-dose, dual-isotope tracer studies in conjunction with 14C accelerator mass spectrometry. Chem. Res. Toxicol. 1998, 11:1217-1222.
35. 41Ca and accelerator mass spectrometry to monitor calcium metabolism in end stage renal disease patients. Clin. Chem. 2005, 51:2095-2102.
36. 41Ca to assess changes in bone calcium metabolism. Anal. Bioanal. Chem. 2006, 386:1587-1602.
37. Denk E., Hillegonds D., Hurrell R.F., Vogel J., Fattinger K., Hauselmann H.J., Kraenzlin M., Walczyk T. Evaluation of 41calcium as a new approach to assess changes in bone metabolism: effect of a bisphosphonate intervention in postmenopausal women with low bone mass. J. Bone Miner. Res. 2007, 22:1518-1525.
38. Turteltaub K.W., Knize M.G., Buonarati M.H., McManus M.E., Veronese M.E., Mazrimas J.A., Felton J.S. Metabolism of 2-amino-1-methyl-6-phenylimidazo[4,5-b] pyridine (PhIP) by liver microsomes and isolated rabbit cytochrome P450 isozymes. Carcinogenesis 1990, 11:941-946.
39. Turteltaub K.W., Watkins B.E., Vanderlaan M., Felton J.S. Role of metabolism on the DNA binding of MeIQx in mice and bacteria. Carcinogenesis 1990, 11:43-49.
40. 32P-postlabeling. Prog. Clin. Biol. Res. 1991, 372:243-253.
41. Felton J.S., Knize M.K., Turteltaub K.W., Buonarati M.H., Taylor R.T., Vanderlaan M., Watkins B.E., Tucker J.D., Thompson L.H. Mutagens and carcinogens in cooked foods: concentration, potency, and risk. Adv. Exp. Med. Biol. 1991, 289:133.
42. 32P-postlabeling assay. Carcinogenesis 1993, 14:545-550.
43. Snyderwine E.G., Buonarati M.H., Felton J.S., Turteltaub K.W. Metabolism of the food-derived mutagen/carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in nonhuman primates. Carcinogenesis 1993, 14:2517-2522.
44. Felton J.S., Turteltaub K.W. Accelerator mass spectrometry for measuring low-dose carcinogen binding to DNA. Environ. Health Perspect. 1994, 102:450-452.
45. Malfatti M.A., Buonarati M.H., Turteltaub K.W., Shen N.H., Felton J.S. The role of sulfation and/or acetylation in the metabolism of the cooked-food mutagen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine in Salmonella typhimurium and isolated rat hepatocytes. Chem. Res. Toxicol. 1994, 7:139-147.
46. Franz C.E., Bangerter C., Fultz E., Mayer K.M., Vogel J.S., Turteltaub K.W. Dose-response studies of MeIQx in rat liver and liver DNA at low doses. Carcinogenesis 1995, 16:367-373.
47. Malfatti M.A., Shen N.H., Wu R.W., Turteltaub K.W., Felton J.S. A correlation of Salmonella mutagenicity with DNA adducts induced by the cooked-food mutagen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine. Mutagenesis 1995, 10:425-431.
48. Turteltaub K.W., Vogel J.S., Frantz C., Felton J.S., McManus M. Assessment of the DNA adduction and pharmacokinetics of PhIP and MeIOx in rodents at doses approximating human exposure using the technique of accelerator mass spectrometry (AMS) and 32P-postlabeling. Princess Takamatsu Symp. 1995, 23:93-102.
49. 14C]-benzene in B6C3F1 mice. Carcinogenesis 1997, 18:2421-2427.
50. Turteltaub K.W., Dingley K.H., Curtis K.D., Malfatti M.A., Turesky R.J., Garner R.C., Felton J.S., Lang N.P. Macromolecular adduct formation and metabolism of heterocyclic amines in humans and rodents at low doses. Cancer Lett. 1999, 143:149-155.
51. Lang N.P., Nowell S., Malfatti M.A., Kulp K.S., Knize M.G., Davis C., Massengill J., Williams S., MacLeod S., Dingley K.H., Felton J.S., Turteltaub K.W. In vivo human metabolism of [2-14C]2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP). Cancer Lett. 1999, 143:135-138.
52. Dingley K.H., Curtis K.D., Nowell S., Felton J.S., Lang N.P., Turteltaub K.W. DNA and protein adduct formation in the colon and blood of humans after exposure to a dietary-relevant dose of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine. Cancer Epidemiol. Biomarkers Prev. 1999, 8:507-512.
53. Malfatti M.A., Kulp K.S., Knize M.G., Davis C., Massengill J.P., Williams S., Nowell S., MacLeod S., Dingley K.H., Turteltaub K.W., Lang N.P., Felton J.S. The identification of [2-(14)C]2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine metabolites in humans. Carcinogenesis 1999, 20:705-713.
54. Goldman R., Day B.W., Carver T.A., Mauthe R.J., Turteltaub K.W., Shields P.G. Quantitation of benzo[a]pyrene-DNA adducts by postlabeling with 14C-acetic anhydride and accelerator mass spectrometry. Chem. Biol. Interact. 2000, 126:171-183.
55. Hah S.S., Mundt J.M., Ubick E.A., Turteltaub K.W., Gregg J.P., Henderson P.T. A sample preparation protocol for quantification of radiolabeled nucleoside incorporation into DNA by accelerator mass spectrometry. Nucl. Instrum. Methods Phys. Res. Sect. B: Beam Interact. Mater. Atoms 2007, 259:763-766.
56. Sporty J.L., Kabir M.M., Turteltaub K.W., Ognibene T., Lin S.J., Bench G. Single sample extraction protocol for the quantification of NAD and NADH redox states in Saccharomyces cerevisiae. J. Sep. Sci. 2008, 18:3202-3211.
57. Hah S.S., Henderson P.T., Turteltaub K.W. Recent advances in biomedical applications of accelerator mass spectrometry. J. Biomed. Sci. 2009, 16:54.
58. Hah S.S., Henderson P.T., Turteltaub K.W. Towards biomarker-dependent individualized chemotherapy: exploring cell-specific differences in oxaliplatin-DNA adduct distribution using accelerator mass spectrometry. Bioorg. Med. Chem. Lett. 2010, 20(8):2448-2451.
59. Lemke S.L., Dueker S.R., Follett J.R., Lin Y., Carkeet C., Buchholz B.A., Vogel J.S., Clifford A.J. Absorption and retinol equivalence of beta-carotene in humans is influenced by dietary vitamin A intake. J. Lipid Res. 2003, 44:1591-1600.
60. Lin Y., Dueker S.R., Follett J.R., Fadel J.G., Arjomand A., Schneider P.D., Miller J.W., Green R., Buchholz B.A., Vogel J.S., Phair R.D., Clifford A.J. Quantitation of in vivo human folate metabolism. Am. J. Clin. Nutr. 2004, 80:680-691.
61. Lappin G., Kuhnz W., Jochemsen R., Kneer J., Chaudhary A., Oosterhuis B., Drijfhout W.J., Rowland M., Garner R.C. Use of microdosing to predict pharmacokinetics at the therapeutic dose: experience with 5 drugs. Clin. Pharmacol. Ther. 2006, 80:203-215.
62. Knutson C.G., Skipper P.L., Liberman R.G., Tannenbaum S.R., Marnett L.J. Monitoring in vivo metabolism and elimination of the endogenous DNA adduct, M1dG {3-(2-deoxy-beta-d-erythro-pentofuranosyl)pyrimido[1,2-alpha]purin-10(3H)-one}, by accelerator mass spectrometry. Chem. Res. Toxicol. 2008, 21:1290-1294.
63. Liberman R.G., Skipper P.L., Tannenbaum S.R. BEAMS Lab at MIT: status report. Nucl. Instrum. Methods Phys. Res. B 2010, 263:887-890.
64. Tompkins E.M., Farmer P.B., Lamb J.H., Jukes R., Dingley K., Ubick E., Turteltaub K.W., Martin E.A., Brown K. A novel 14C-postlabeling assay using accelerator mass spectrometry for the detection of O6-methyldeoxy-guanosine adducts. Rapid Commun. Mass Spectrom. 2006, 20:883-891.
65. Zhou X., Liberman R.G., Skipper P.L., Margolin Y., Tannenbaum S.R., Dedon P.C. Quantification of DNA strand breaks and abasic sites by oxime derivatization and accelerator mass spectrometry: application to gamma-radiation and peroxynitrite. Anal. Biochem. 2005, 343:84-92.
66. Degan P., Shigenaga M.K., Park E.M., Alperin P.E., Ames B.N. Immunoaffinity isolation of urinary 8-hydroxy-2'-deoxyguanosine and 8-hydroxyguanine and quantitation of 8-hydroxy-2'-deoxyguanosine in DNA by polyclonal antibodies. Carcinogenesis 1991, 12:865-871.
67. Toyokuni S., Tanaka T., Hattori Y., Nishiyama Y., Yoshida A., Uchida K., Hiai H., Ochi H., Osawa T. Quantitative immunohistochemical determination of 8-hydroxy-2'-deoxyguanosine by a monoclonal antibody N45.1: its application to ferric nitrilotriacetate-induced renal carcinogenesis model. Lab. Invest. 1997, 76:365-374.
68. Yin B., Whyatt R.M., Perera F.P., Randall M.C., Cooper T.B., Santella R.M. Determination of 8-hydroxydeoxyguanosine by an immunoaffinity chromatography-monoclonal antibody-based ELISA. Free Radic. Biol. Med. 1995, 18:1023-1032.
69. Kikuchi H., Furuta A., Nishioka K., Suzuki S.O., Nakabeppu Y., Iwaki T. Impairment of mitochondrial DNA repair enzymes against accumulation of 8-oxo-guanine in the spinal motor neurons of amyotrophic lateral sclerosis. Acta Neuropathol. 2002, 103:408-414.
70. Chiou C.C., Chang P.Y., Chan E.C., Wu T.L., Tsao K.C., Wu J.T. Urinary 8-hydroxydeoxyguanosine and its analogs as DNA marker of oxidative stress: development of an ELISA and measurement in both bladder and prostate cancers. Clin. Chim. Acta 2003, 334:87-94.
71. Sawamoto Y., Sugano N., Tanaka H., Ito K. Detection of periodontopathic bacteria and an oxidative stress marker in saliva from periodontitis patients. Oral Microbiol. Immunol. 2005, 20:216-220.
72. Sugano N., Yokoyama K., Oshikawa M., Kumagai K., Takane M., Tanaka H., Ito K. Detection of Streptococcus anginosus and 8-hydroxydeoxyguanosine in saliva. J. Oral Sci. 2003, 45:181-184.
73. Yoshida R., Ogawa Y., Kasai H. Urinary 8-oxo-7,8-dihydro-2'-deoxyguanosine values measured by an ELISA correlated well with measurements by high-performance liquid chromatography with electrochemical detection. Cancer Epidemiol. Biomarkers Prev. 2002, 11:1076-1081.
74. Ihara Y., Takata H., Tanabe Y., Nobukuni K., Hayabara T. Influence of repetitive transcranial magnetic stimulation on disease severity and oxidative stress markers in the cerebrospinal fluid of patients with spinocerebellar degeneration. Neurol. Res. 2005, 27:310-313.
75. Kikuchi A., Takeda A., Onodera H., Kimpara T., Hisanaga K., Sato N., Nunomura A., Castellani R.J., Perry G., Smith M.A., Itoyama Y. Systemic increase of oxidative nucleic acid damage in Parkinson's disease and multiple system atrophy. Neurobiol. Dis. 2002, 9:244-248.
76. Cooke M.S., Patel K., Ahmad J., Holloway K., Evans M.D., Lunec J. Monoclonal antibody to single-stranded DNA: a potential tool for DNA repair studies. Biochem. Biophys. Res. Commun. 2001, 284:232-238.
77. Haghdoost S., Czene S., Naslund I., Skog S., Harms-Ringdahl M. Extracellular 8-oxo-dG as a sensitive parameter for oxidative stress in vivo and in vitro. Free Radic. Res. 2005, 39:153-162.
78. Kantha S.S., Wada S., Tanaka H., Takeuchi M., Watabe S., Ochi H. Carnosine sustains the retention of cell morphology in continuous fibroblast culture subjected to nutritional insult. Biochem. Biophys. Res. Commun. 1996, 223:278-282.
79. David S.S., Wiliams S.D. Chemistry of glycosylases and endonucleases involved in base-excision repair. Chem. Rev. 1998, 98:1221-1261.
80. Arai K., Morishita K., Shinmura K., Kohno T., Kim S.R., Nohmi T., Taniwaki M., Ohwada S., Yokota J. Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage. Oncogene 1997, 14:2857-2861.
81. Rosenquist T.A., Zharkov D.O., Grollman A.P. Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:7429-7434.
82. Bruner S.D., Nash H.M., Lane W.S., Verdine G.L. Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway. Curr. Biol. 1998, 8:393-403.
83. Parsons J.L., Zharkov D.O., Dianov G.L. NEIL1 excises 3' end proximal oxidative DNA lesions resistant to cleavage by NTH1 and OGG1. Nucleic Acids Res. 2005, 33:4849-4856.
84. Dou H., Mitra S., Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 2003, 278:49679-49684.
85. Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F., Miller J.H. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 1996, 178:3885-3892.
86. Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T., Takao M., Yasui A., Yamamoto K., Asano M. Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue. Cancer Res. 1997, 57:2151-2156.
87. Rozalski R., Siomek A., Gackowski D., Foksinski M., Gran C., Klungland A., Olinski R. Substantial decrease of urinary 8-oxo-7,8-dihydroguanine, a product of the base excision repair pathway, in DNA glycosylase defective mice. Int. J. Biochem. Cell Biol. 2005, 37:1331-1336.
88. Morland I., Rolseth V., Luna L., Rognes T., Bjoras M., Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 2002, 30:4926-4936.
89. Mundt J.M., Hah S.S., Sumbad R.A., Schramm V., Henderson P.T. Incorporation of extracellular 8-oxodG into DNA and RNA requires purine nucleoside phosphorylase in MCF-7 cells. Nucleic Acids Res. 2007, 20(12):1745-1751.
90. Reardon J.T., Bessho T., Kung H.C., Bolton P.H., Sancar A. In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:9463-9468.
91. Jaiswal M., Lipinski L.J., Bohr V.A., Mazur S.J. Efficient in vitro repair of 7-hydro-8-oxodeoxyguanosine by human cell extracts: involvement of multiple pathways. Nucleic Acids Res. 1998, 26:2184-2191.
92. Lipinski L.J., Hoehr N., Mazur S.J., Dianov G.L., Senturker S., Dizdaroglu M., Bohr V.A. Repair of oxidative DNA base lesions induced by fluorescent light is defective in xeroderma pigmentosum group A cells. Nucleic Acids Res. 1999, 27:3153-3158.
93. McGoldrick J.P., Yeh Y.C., Solomon M., Essigmann J.M., Lu A.L. Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. Mol. Cell Biol. 1995, 15:989-996.
94. Russo M.T., De Luca G., Degan P., Parlanti E., Dogliotti E., Barnes D.E., Lindahl T., Yang H.J., Miller J.H., Bignami M. Accumulation of the oxidative base lesion 8-hydroxyguanine in DNA of tumor-prone mice defective in both the Myh and Ogg1 DNA glycosylases. Cancer Res. 2004, 64:4411-4414.
95. Macpherson P., Barone F., Maga G., Mazzei F., Karran P., Bignami M. 8-Oxoguanine incorporation into DNA repeats in vitro and mismatch recognition by MutSalpha. Nucleic Acids Res. 2005, 33:5094-5105.
96. Kornberg A., Baker T.A. DNA Replication 1992, W.H. Freeman, New York.
97. Dandona P., Thusu K., Cook S., Snyder B., Makowski J., Armstrong D., Nicotera T. Oxidative damage to DNA in diabetes mellitus. Lancet 1996, 347:444-445.
98. Mo J.Y., Maki H., Sekiguchi M. Hydrolytic elimination of a mutagenic nucleotide, 8-oxodGTP, by human 18-kilodalton protein: sanitization of nucleotide pool. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:11021-11025.
99. Cai J.P., Ishibashi T., Takagi Y., Hayakawa H., Sekiguchi M. Mouse MTH2 protein which prevents mutations caused by 8-oxoguanine nucleotides. Biochem. Biophys. Res. Commun. 2003, 305:1073-1077.
100. Ishibashi T., Hayakawa H., Sekiguchi M. A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides. EMBO Rep. 2003, 4:479-483.
101. Hori M., Satou K., Harashima H., Kamiya H. Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate) by human MTH1, MTH2, and NUDT5. Free Radic. Biol. Med. 2010, 48:1197-1201.
102. Arner E.S.J., Eriksson S. Mammalian deoxyribonucleoside kinases. Pharmacol. Ther. 1995, 67:155-186.
103. Van Rompay A.R., Johansson M., Karlsson A. Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases. Pharmacol. Ther. 2000, 87:189-198.
104. Mathews C.K. DNA precursor metabolism and genomic stability. FASEB J. 2006, 20:1300-1314.
105. Park E.M., Shigenaga M.K., Degan P., Korn T.S., Kitzler J.W., Wehr C.M., Kolachana P., Ames B.N. Assay of excised oxidative DNA lesions: isolation of 8-oxoguanine and its nucleoside derivatives from biological fluids with a monoclonal antibody column. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:3375-3379.
106. Hayakawa H., Hofer A., Thelander L., Kitajima S., Cai Y., Oshiro S., Yakushiji H., Nakabeppu Y., Kuwano M., Sekiguchi M. Metabolic fate of oxidized guanine ribonucleotides in mammalian cells. Biochemistry 1999, 38:3610-3614.
107. Tanaka H., Arakawa H., Yamaguchi T., Shiraishi K., Fukuda S., Matsui K., Takei Y., Nakamura Y. A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature 2000, 404:42-49.
108. Nakano K., Balint E., Ashcroft M., Vousden K.H. A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene 2000, 19:4283-4289.
109. Zeng H.H., Choi J.Y., Chung M.H. 8-Hydroxyguanine, a product from damaged DNA can be used in the DNA salvage pathway. Chin. Chem. Lett. 2003, 14:529-532.
110. Hyun J.W, Choi J.Y., Zeng H.H., Lee Y.S., Kim H.S., Yoon S.H., Chung M.H. Leukemic cell line, KG-1 has a functional loss of hOGG1 enzyme due to a point mutation and 8-hydroxydeoxyguanosine can kill KG-1. Oncogene 2000, 19:4476-4479.
111. Hyun J.W., Jung Y.C., Kim H.S., Choi E.Y., Kim J.E., Yoon B.H., Yoon S.H., Lee Y.S., Choi J., You H.J., Chung M.H. 8-Hydroxydeoxyguanosine causes death of human leukemia cells deficient in 8-oxoguanine glycosylase 1 activity by inducing apoptosis. Mol. Cancer Res. 2003, 1:290-299.
112. Kim J.E., Chung M.H. 8-Oxo-7,8-dihydro-2'-deoxyguanosine is not salvaged for DNA synthesis in human leukemic U937 cells. Free Radic. Res. 2006, 40:461-466.