Ponad 7000 publikacji medycznych!
Statystyki za 2021 rok:
odsłony: 8 805 378
Artykuły w Czytelni Medycznej o SARS-CoV-2/Covid-19

Poniżej zamieściliśmy fragment artykułu. Informacja nt. dostępu do pełnej treści artykułu
© Borgis - Postępy Nauk Medycznych 11/2011, s. 950-956
*Justyna Janik, Barbara Czarnocka
Oxidative DNA damage and repair in thyroid gland
Oksydacyjne uszkodzenia DNA i ich naprawa w gruczole tarczycy
Department of Biochemistry and Molecular Biology, Medical Centre of Postgraduate Education, Warsaw
Head of Department: prof. dr hab. Barbara Czarnocka
Reaktywne formy tlenu (ROS) powstają endogennie, w wyniku metabolizmu komórkowego, jak również dostają się do komórki ze środowiska zewnętrznego (źródła egzogenne). Nadtlenek wodoru (H2O2), tlen singletowy (1O2) czy rodnik hydroksylowy (?OH) powstają w wielu procesach fizjologicznych, takich jak oddychanie w mitochondriach czy utlenianie w peroksysomach. W tarczycy H2O2 uczestniczy w syntezie hormonów. ROS powodują powstawanie modyfikacji DNA, wśród których 8-oxoG jest najbardziej mutagenną. Uszkodzenia DNA odgrywają istotną rolę w mutagenezie, kancerogenezie i rozwoju innych chorób u ludzi. Główną drogą naprawy utlenionych zasad, w tym 8-oxoG, jest naprawa przez wycinanie zasad (ang. Base Excision Repair – BER). Zaburzenia w naprawie DNA mogą być czynnikiem ryzyka rozwoju wielu chorób, w tym raka tarczycy. Badania nad molekularnymi mechanizmami odpowiedzialnymi za zaburzenia naprawy DNA obejmują polimorfizmy genów naprawy, regulację ich transkrypcji, modyfikacje potranslacyjne oraz inne czynniki. Dane literaturowe wskazują, że stres oksydacyjny, uszkodzenia DNA oraz zwiększona częstotliwość mutacji mogą być czynnikami przyczyniającymi się do rozwoju raka tarczycy. Ponadto, zmiany w systemach naprawy DNA, w tym występowanie polimorfizmów genów naprawczych (OGG1, APE1 i XRCC1) może również wiązać się z ryzykiem transformacji nowotworowej w tarczycy.
Reactive oxygen species (ROS) are formed as a consequence of cell metabolism but can also get into cells from external sources. Hydrogen peroxide (H2O2), singlet oxygen (1O2) and hydroxyl radical (?OH) are produced in many physiological processes such as respiration in the mitochondria and oxidation in the peroxisomes. In thyroid H2O2 participate in hormone synthesis. ROS induce DNA damages that are implied in mutagenesis, tumorigenesis and other human diseases. Among these DNA lesions 8-oxoG is one of the most mutagenic. The main pathway to repair 8-oxoG and other oxidized bases is base excision repair (BER). The efficiency of BER when it comes to eliminating oxidative DNA lesions may be a risk factor for thyroid cancer and other diseases development. Molecular mechanisms responsible for impaired DNA repair have been widely studied and include polymorphisms of repair genes, their transcriptional activation/down-regulation, post-translational modifications and possibly other factors. The data presented here and literature reports demonstrate that increased oxidative stress, DNA damage and somatic mutation rates are contributing factors to the development of thyroid cancers. Moreover, alterations in DNA repair mechanisms, including polymorphisms of repair genes (OGG1, APE1 and XRCC1) may be linked to the risk of thyroid malignant transformation.

Oxidative stress and reactive oxygen species
Most organisms living on Earth are entirely dependent on the presence of oxygen in the atmosphere. However, the by-products of oxygen metabolism are toxic to living organisms. Reactive oxygen species (ROS) in the cell are produced both during normal cellular metabolism or inflammatory reactions and under the influence of external factors like γ, X and UV radiation, biotransformation of dietary chemicals and some diet components, e.g. transient metal ions (1). Normal cellular metabolism seems to be the primary source of endogenous ROS. An imbalance between the formation of ROS and antioxidant defense leads to increased reactive oxygen species generation and oxidative stress development (2). ROS are radical molecules containing oxygen, for example superoxide (O2?–) and hydroxyl radical (?OH), or non-radical molecules, such as hydrogen peroxide (H2O2) and singlet oxygen (1O2), which may be converted into radical forms. The most reactive ROS, hydroxyl radicals, are responsible for oxidation and fragmentation of nucleic acids, proteins and lipids. They are produced in the metal-catalysed Haber-Weiss and Fenton reactions mediated by the transition metal ions such as iron and the copper (3). Iron is a cofactor for many biological reactions and is an important component of metabolism in various tissues and organs, including the thyroid. Iron deficiency may affect thyroid hormone synthesis by decreasing the activity of the heme-dependent thyroid peroxidase (TPO). In addition, low iron levels reduce deiodinase activity, i.e. it slows down the conversion of T4 to T3, and also causes a raise in circulating concentrations of thyroid stimulating hormone (TSH) (4). With higher levels of TSH and low free T4 and T3 levels hypothyroidism occurs. Iron overload, on the other hand, may promote the persistence of harmful labile iron, which can catalyze the generation of potentially carcinogenic DNA adducts in the cell (5).
The role of H2O2 in THE thyroid
H2O2 production was found in vivo in many intracellular structures e.g. mitochondria, endoplasmic reticulum and peroxisomes. A high concentration of hydrogen peroxide was also observed in activated phagocytes, spermatozoids, bacteria and even in exhaled air (6). In the thyroid gland H2O2 is produced by one or two NADPH oxidases (Duox1/2) at the apical membrane of thyrocytes and it participates in hormone biosynthesis. To synthesize T3 and T4 hormones, the thyroid takes up iodine and incorporates it into the precursor of the hormones – thyroglobulin. Iodination of thyrosyl residues on thyroglobulin requires high concentrations of H2O2 as well as oxidized iodine, which is generated by the thyroid peroxidase (TPO) (7). For the TPO function properly H2O2 is necessary. It helps to stabilize the enzyme by autocatalytic covalent heme binding to the TPO molecule, which positively affects TPO activity (8). On the other hand, an excess of H2O2 may inhibit TPO activity and consequently inhibit thyroid hormone synthesis (9). Because H2O2 and iodine are co-substrates in hormone synthesis, changes of iodine concentrations affect the concentration of H2O2. In vitro and in vivo studies demonstrated that iodide inhibits the generation of H2O2 in the thyroid (10, 11). Production of H2O2 is moreover stimulated through the cAMP cascade by the thyrotropin (TSH), which increases the expression of genes important for hormone synthesis (e.g. TPO) (12).
H2O2 has various effects in the cell and it may enhance cell metabolism through diverse mechanisms. Besides that H2O2 acts as an oxidant, and also induces oxidative stress and apoptosis (13) working as an intracellular messenger (14). ROS-derived signals regulate growth, proliferation, differentiation and death of the cell (15-17). It has been demonstrated that in thyroid H2O2-mediated cytotoxicity appears at low H2O2 concentrations and leads to cell apoptosis or less frequently to necrosis (15). Moreover in vivo studies suggest that cytotoxic reaction to oxidative stress may depend on the functional state of the thyroid gland (18).
Despite the fact that hydrogen peroxide does not react directly with components of DNA, it is a precursor to highly reactive hydroxyl radical (?OH), hypochlorite (ClO) and singlet oxygen (1O2). Therefore H2O2 may facilitate a mutagenic process and DNA modification leading to cancer development (19). A thyrocyte which generates a great amount of H2O2 is a long-lived cell and that allows it to accumulate mutations in DNA (20). Consequently, oxidative stress has been suggested to contribute to the pathogenesis of thyroid cancer (21, 22).
Defense against the action and effects of ROS
An antioxidative defense systems, that protect from the formation and effects of reactive oxygen species, function in all living organisms. In the cell the defense against the destructive effects of ROS works on the three levels.
The first level of the system prevents the formation of excessive quantities of ROS. The main component of this level are proteins that bind transition metal ions which thus inhibits Fenton reactions. Iron ions are bound by ferritin, transferrin and lactoferrin, copper ions by ceruloplasmin. Metallothioneins bind a number of different metal ions, as well as albumin, which non-specifically, is capable of binding many metal ions (23).
The second defense level neutralizes ROS. This system includes antioxidant enzymes such as superoxide dismutase (SOD), glutathione and ascorbate peroxidases (GPX, APX1), and glutathione transferase. The other elements of this protection level are small molecule antioxidants that work as direct or indirect free radical scavengers: glutathione, ascorbic acid, cysteine, tocopherols (vitamin E), retinoids (vitamin A analogs), uric acid, carotenoids, bilirubin, ubiquinol, and even glucose and pyruvate (3, 24). The above antioxidative protectors have been found in thyroid gland, e.g. GPX and TPO and are upregulated during the synthesis of thyroid hormones (25). There is also evidence that GPX3 which affects the H2O2 concentration directly interferes with hormone synthesis (26).
The third level of the defense is the elimination of ROS harmful effects on the most important cellular macromolecule – DNA. Oxidative DNA adducts are repaired by enzymes of excision repair systems, which will be described in subsequent chapters.
DNA damage caused by oxygen free radicals attack
ROS reactions with DNA cause the most dangerous consequences for multicellular organisms. The ?OH radical molecule is one of the ROS that is extremely reactive in the oxidation of cellular constituents such as nucleic acids, proteins and lipids. ?OH interactions with DNA may lead to considerable damage, such as oxidized bases, base and sugar lesions, abasic sites, DNA-DNA intrastrand adducts, single or double strand breaks and DNA-protein cross-links (2, 27-29).

Powyżej zamieściliśmy fragment artykułu, do którego możesz uzyskać pełny dostęp.
Mam kod dostępu
  • Aby uzyskać płatny dostęp do pełnej treści powyższego artykułu albo wszystkich artykułów (w zależności od wybranej opcji), należy wprowadzić kod.
  • Wprowadzając kod, akceptują Państwo treść Regulaminu oraz potwierdzają zapoznanie się z nim.
  • Aby kupić kod proszę skorzystać z jednej z poniższych opcji.

Opcja #1


  • dostęp do tego artykułu
  • dostęp na 7 dni

uzyskany kod musi być wprowadzony na stronie artykułu, do którego został wykupiony

Opcja #2


  • dostęp do tego i pozostałych ponad 7000 artykułów
  • dostęp na 30 dni
  • najpopularniejsza opcja

Opcja #3


  • dostęp do tego i pozostałych ponad 7000 artykułów
  • dostęp na 90 dni
  • oszczędzasz 28 zł
1. Migliore L, Copped? F: Genetic and environmental factors in cancer and neurodegenerative diseases. Mutat Res 2002; 512(2-3): 135-53.
2. Halliwell B, Aruoma OI: DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems. FEBS Lett 1991; 281(1-2): 9-19.
3. Sies H: Damage to plasmid DNA by singlet oxygen and its protection. Mutat Res 1993; 299(3-4): 183-91.
4. Beard JL, Borel MJ, Derr J: Impaired thermoregulation and thyroid function in iron-deficiency anemia. Am J Clin Nutr 1990; 52(5): 813-9.
5. Stevens RG, Graubard BI, Micozzi MS et al.: Moderate elevation of body iron level and increased risk of cancer occurrence and death. Int J Cancer 1994; 56(3): 364-369.
6. Halliwell B: Free radicals, reactive oxygen species and human disease: a critical evaluation with special reference to atherosclerosis. Br J Exp Pathol 1989; 70(6) :737-57.
7. De Deken X, Wang D, Dumont JE et al.: Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system. Exp Cell Res 2002; 273(2): 187-96.
8. Fayadat L, Niccoli-Sire P, Lanet J et al.: Role of heme in intracellular trafficking of thyroperoxidase and involvement of H2O2 generated at the apical surface of thyroid cells in autocatalytic covalent heme binding. J Biol Chem 1999; 274(15): 10533-8.
9. Sugawara M, Sugawara Y, Wen K et al.: Generation of oxygen free radicals in thyroid cells and inhibition of thyroid peroxidase. Exp Biol Med (Maywood) 2002; 227(2): 141-6.
10. Ohayon R, Boeynaems JM, Braekman JC et al.: Inhibition of thyroid NADPH-oxidase by 2-iodohexadecanal in a cell-free system. Mol Cell Endocrinol 1994; 99(1): 133-41.
11. Cardoso LC, Martins DC, Figueiredo MD et al.: Ca(2+)/nicotinamide adenine dinucleotide phosphate-dependent H(2)O(2) generation is inhibited by iodide in human thyroids. J Clin Endocrinol Metab 2001; 86(9): 4339-43.
12. Raspé E, Dumont JE: Tonic modulation of dog thyrocyte H2O2 generation and I- uptake by thyrotropin through the cyclic adenosine 3’,5’-monophosphate cascade. Endocrinology 1995; 136(3): 965-73.
13. Riou C, Remy C, Rabilloud R et al.: H2O2 induces apoptosis of pig thyrocytes in culture. J Endocrinol 1998; 156(2): 315-22.
14. Kim H, Lee TH, Hwang YS et al.: Methimazole as an antioxidant and immunomodulator in thyroid cells: mechanisms involving interferon-gamma signaling and H(2)O(2) scavenging. Mol Pharmacol 2001; 60(5): 972-80.
15. Demelash A, Karlsson JO, Nilsson M et al.: Selenium has a protective role in caspase-3-dependent apoptosis induced by H2O2 in primary cultured pig thyrocytes. Eur J Endocrinol 2004; 150(6): 841-9.
16. Burdon RH. Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic Biol Med 1995; 18(4): 775-94.
17. Hansberg W, Aguirre J. Hyperoxidant states cause microbial cell differentiation by cell isolation from dioxygen. J Theor Biol 1990; 142(2): 201-21.
18. Mutaku JF, Poma JF, Many MC et al.: Cell necrosis and apoptosis are differentially regulated during goitre development and iodine-induced involution. J Endocrinol 2002; 172(2): 375-86.
19. Stone JR, Yang S: Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 2006; 8(3-4): 243-70.
20. Corvilain B, Laurent E, Lecomte M et al.: Role of the cyclic adenosine 3’,5’-monophosphate and the phosphatidylinositol-Ca2+ cascades in mediating the effects of thyrotropin and iodide on hormone synthesis and secretion in human thyroid slices. J Clin Endocrinol Metab 1994; 79(1): 152-9.
21. Ha HC, Thiagalingam A, Nelkin BD et al.: Reactive oxygen species are critical for the growth and differentiation of medullary thyroid carcinoma cells. Clin Cancer Res 2000; 6(9): 3783-7.
22. Karbownik M, Lewinski A: The role of oxidative stress in physiological and pathological processes in the thyroid gland; possible involvement in pineal-thyroid interactions. Neuro Endocrinol Lett 2003; 24(5): 293-303.
23. Sato M, Bremner I: Oxygen free radicals and metallothionein. Free Radic Biol Med 1993; 14(3): 325-37.
24. Sies H: Strategies of antioxidant defense. Eur J Biochem 1993; 215(2): 213-9.
25. Howie AF, Arthur JR, Nicol F et al.: Identification of a 57-kilodalton selenoprotein in human thyrocytes as thioredoxin reductase and evidence that its expression is regulated through the calcium-phosphoinositol signaling pathway. J Clin Endocrinol Metab 1998; 83(6): 2052-8.
26. Howie AF, Walker SW, Akesson B et al.: Thyroidal extracellular glutathione peroxidase: a potential regulator of thyroid-hormone synthesis. Biochem J 1995; 308 ( Pt 3): 713-7.
27. Lloyd DR, Phillips DH, Carmichael PL: Generation of putative intrastrand cross-links and strand breaks in DNA by transition metal ion-mediated oxygen radical attack. Chem Res Toxicol 1997; 10(4): 393-400.
28. Cadet J, Berger M, Douki T et al.: Oxidative damage to DNA: formation, measurement, and biological significance. Rev Physiol Biochem Pharmacol 1997; 131: 1-87.
29. Bjelland S, Seeberg E: Mutagenicity, toxicity and repair of DNA base damage induced by oxidation. Mutat Res 2003; 531(1-2): 37-80.
30. Dizdaroglu M: Oxidative damage to DNA in mammalian chromatin. Mutat Res 1992; 275(3-6): 331-42.
31. Jackson AL, Loeb LA: The contribution of endogenous sources of DNA damage to the multiple mutations in cancer. Mutat Res 2001; 477(1-2): 7-21.
32. Dizdaroglu M: Free-radical-induced formation of an 8,5’-cyclo-2’-deoxyguanosine moiety in deoxyribonucleic acid. Biochem J 1986; 238(1): 247-54.
33. Dizdaroglu M: Quantitative determination of oxidative base damage in DNA by stable isotope-dilution mass spectrometry. FEBS Lett 1993; 315(1): 1-6.
34. Tudek B, Winczura A, Janik J et al.: Involvement of oxidatively damaged DNA and repair in cancer development and aging. Am J Transl Res 2010; 2(3): 254-84.
35. Kuchino Y, Mori F, Kasai H et al.: Misreading of DNA templates containing 8-hydroxydeoxyguanosine at the modified base and at adjacent residues. Nature 1987; 327(6117): 77-9.
36. Shibutani S, Takeshita M, Grollman AP: Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 1991; 349(6308): 431-4.
37. Cheng KC, Cahill DS, Kasai H et al.: 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G-T and A-C substitutions. J Biol Chem 1992; 267(1): 166-72.
38. Ret?l J, Hoebee B, Braun JE et al.: Mutational specificity of oxidative DNA damage. Mutat Res 1993; 299(3-4): 165-82.
39. Ribeiro DT, De Oliveira RC, Di Mascio P et al.: Singlet oxygen induces predominantly G to T transversions on a single-stranded shuttle vector replicated in monkey cells. Free Radic Res 1994; 21(2): 75-83.
40. Olinski R, Zastawny T, Budzbon J et al.: DNA base modifications in chromatin of human cancerous tissues. FEBS Lett 1992; 309(2): 193-8.
41. Malins DC: Identification of hydroxyl radical-induced lesions in DNA base structure: biomarkers with a putative link to cancer development. J Toxicol Environ Health 1993; 40(2-3): 247-61.
42. Hollstein M, Sidransky D, Vogelstein B et al.: p53 mutations in human cancers. Science 1991; 253(5015): 49-53.
43. Maier J, van Steeg H, van Oostrom C et al.: Deoxyribonucleic acid damage and spontaneous mutagenesis in the thyroid gland of rats and mice. Endocrinology 2006; 147(7): 3391-7.
44. Cole J, Skopek TR: International Commission for Protection Against Environmental Mutagens and Carcinogens. Working paper no. 3. Somatic mutant frequency, mutation rates and mutational spectra in the human population in vivo. Mutat Res 1994; 304(1): 33-105.
45. Shahedian B, Shi Y, Zou M et al.: Thyroid carcinoma is characterized by genomic instability: evidence from p53 mutations. Mol Genet Metab 2001; 72(2): 155-63.
46. Krohn K, Maier J, Paschke R: Mechanisms of disease: hydrogen peroxide, DNA damage and mutagenesis in the development of thyroid tumors. Nat Clin Pract Endocrinol Metab 2007; 3(10): 713-20.
47. Friedberg EC. DNA damage and repair. Nature 2003; 421(6921): 436-40.
48. Fortini P, Pascucci B, Parlanti E et al.: The base excision repair: mechanisms and its relevance for cancer susceptibility. Biochimie 2003; 85(11): 1053-71.
49. Hill JW, Hazra TK, Izumi T et al.: Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair Nucleic Acids Res 2001; 29(2): 430-8
50. Schreiber V, Amé JC, Dollé P et al.: Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J Biol Chem 2002; 277(25): 23028-36.
51. Goode EL, Ulrich CM, Potter JD: Polymorphisms in DNA repair genes and associations with cancer risk. Cancer Epidemiol Biomarkers Prev 2002; 11(12): 1513-30.
52. Kohno T, Shinmura K, Tosaka M et al.: Genetic polymorphisms and alternative splicing of the hOGG1 gene, that is involved in the repair of 8-hydroxyguanine in damaged DNA. Oncogene 1998; 16(25): 3219-25.
53. Sidorenko VS, Grollman AP, Jaruga P et al.: Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase. FEBS J 2009; 276(18): 5149-62.
54. Dherin C, Radicella JP, Dizdaroglu M et al.: Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations. Nucleic Acids Res 1999; 27(20): 4001-7.
55. Bravard A, Vacher M, Moritz E et al.: Oxidation status of human OGG1-S326C polymorphic variant determines cellular DNA repair capacity. Cancer Res 2009; 69(8): 3642-9.
56. Janik J, Swoboda M, Janowska B et al.: 8-Oxoguanine incision activity is impaired in lung tissues of NSCLC patients with the polymorphism of OGG1 and XRCC1 genes. Mutat Res 2011; 709-710: 21-31.
57. Takezaki T, Gao CM, Wu JZ et al.: hOGG1 Ser(326)Cys polymorphism and modification by environmental factors of stomach cancer risk in Chinese. Int J Cancer 2002; 99(4): 624-7.
58. Chen L, Elahi A, Pow-Sang J et al.: Association between polymorphism of human oxoguanine glycosylase 1 and risk of prostate cancer. J Urol 2003; 170(6 Pt 1): 2471-4.
59. Cho EY, Hildesheim A, Chen CJ et al.: Nasopharyngeal carcinoma and genetic polymorphisms of DNA repair enzymes XRCC1 and hOGG1. Cancer Epidemiol Biomarkers Prev 2003; 12(10): 1100-4.
60. Xing DY, Tan W, Song N et al.: Ser326Cys polymorphism in hOGG1 gene and risk of esophageal cancer in a Chinese population. Int J Cancer 2001; 95(3): 140-3.
61. Niwa Y, Matsuo K, Ito H et al.: Association of XRCC1 Arg399Gln and OGG1 Ser326Cys polymorphisms with the risk of cervical cancer in Japanese subjects. Gynecol Oncol 2005; 99(1): 43-9.
62. Rossner P Jr, Terry MB, Gammon MD et al.: OGG1 polymorphisms and breast cancer risk. Cancer Epidemiol Biomarkers Prev 2006; 15(4): 811-5.
63. Hansen R, Saeb? M, Skjelbred CF et al.: GPX Pro198Leu and OGG1 Ser326Cys polymorphisms and risk of development of colorectal adenomas and colorectal cancer. Cancer Lett 2005; 229(1): 85-91.
64. García-Quispes WA, Pérez-Machado G, Akdi A et al.: Association studies of OGG1, XRCC1, XRCC2 and XRCC3 polymorphisms with differentiated thyroid cancer. Mutat Res 2011; 709-710: 67-72.
65. Janssen K, Schlink K, Götte W et al.: DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326. Mutat Res 2001; 486(3): 207-16.
66. Obtulowicz T, Swoboda M, Speina E et al.: Oxidative stress and 8-oxoguanine repair are enhanced in colon adenoma and carcinoma patients. Mutagenesis 2010; 25(5): 463-71.
67. Chevillard S, Radicella JP, Levalois C et al.: Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours. Oncogene 1998; 16(23): 3083-6
68. Shinmura K, Kohno T, Kasai H et al.: Infrequent mutations of the hOGG1 gene, that is involved in the excision of 8-hydroxyguanine in damaged DNA, in human gastric cancer. Jpn J Cancer Res 1998; 89(8): 825-8.
69. Anderson PC, Daggett V: The R46Q, R131Q and R154H polymorphs of human DNA glycosylase/beta-lyase hOgg1 severely distort the active site and DNA recognition site but do not cause unfolding. J Am Chem Soc 2009; 131(27): 9506-15.
70. Arai K, Morishita K, Shinmura K at al.: Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage. Oncogene 1997; 14(23): 2857-61.
71. Fan CY, Liu KL, Huang HY et al.: Frequent allelic imbalance and loss of protein expression of the DNA repair gene hOGG1 in head and neck squamous cell carcinoma. Lab Invest 2001; 81(10): 1429-38.
72. Park J, Chen L, Tockman MS et al.: The human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) DNA repair enzyme and its association with lung cancer risk. Pharmacogenetics 2004; 14(2): 103-9.
73. Royer MC, Zhang H, Fan CY et al.: Genetic alterations in papillary thyroid carcinoma and hashimoto thyroiditis: An analysis of hOGG1 loss of heterozygosity. Arch Otolaryngol Head Neck Surg 2010; 136(3): 240-2.
74. Zienolddiny S, Campa D, Lind H et al.: Polymorphisms of DNA repair genes and risk of non-small cell lung cancer. Carcinogenesis 2006; 27(3): 560-7.
75. Hu JJ, Smith TR, Miller MS et al.: Amino acid substitution variants of APE1 and XRCC1 genes associated with ionizing radiation sensitivity. Carcinogenesis 2001; 22(6): 917-22.
76. Hung RJ, Hall J, Brennan P, Boffetta P: Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review. Am J Epidemiol 2005; 162(10): 925-42.
77. Shen MR, Zdzienicka MZ, Mohrenweiser H et al.: Mutations in hamster single-strand break repair gene XRCC1 causing defective DNA repair. Nucleic Acids Res 1998; 26(4): 1032-7.
78. Marsin S, Vidal AE, Sossou M et al.: Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1. J Biol Chem 2003; 278(45): 44068-74.
79. Nazarkina ZK, Khodyreva SN, Marsin S et al.: XRCC1 interactions with base excision repair DNA intermediates. DNA Repair (Amst) 2007; 6(2): 254-64.
80. Ho T, Li G, Lu J et al.: Association of XRCC1 polymorphisms and risk of differentiated thyroid carcinoma: a case-control analysis. Thyroid 2009; 19(2): 129-35.
81. Chiang FY, Wu CW, Hsiao PJ et al.: Association between polymorphisms in DNA base excision repair genes XRCC1, APE1, and ADPRT and differentiated thyroid carcinoma. Clin Cancer Res 2008; 14(18): 5919-24.
82. Sigurdson AJ, Land CE, Bhatti P et al.: Thyroid nodules, polymorphic variants in DNA repair and RET-related genes, and interaction with ionizing radiation exposure from nuclear tests in Kazakhstan. Radiat Res 2009; 171(1): 77-88.
83. Akulevich NM, Saenko VA, Rogounovitch TI et al.: Polymorphisms of DNA damage response genes in radiation-related and sporadic papillary thyroid carcinoma. Endocr Relat Cancer 2009; 16(2): 491-503.
84. Hu Z, Ma H, Chen F et al.: XRCC1 polymorphisms and cancer risk: a meta-analysis of 38 case-control studies. Cancer Epidemiol Biomarkers Prev 2005; 14(7): 1810-8.
85. Mertens AC, Mitby PA, Radloff G et al.: XRCC1 and glutathione-S-transferase gene polymorphisms and susceptibility to radiotherapy-related malignancies in survivors of Hodgkin disease. Cancer 2004; 101(6): 1463-72.
otrzymano: 2011-09-12
zaakceptowano do druku: 2011-10-17

Adres do korespondencji:
*Justyna Janik
Zakład Biochemii i Biologii Molekularnej Centrum Medyczne Kształcenia Podyplomowego
ul. Marymoncka 99/103, 01-813 Warszawa
tel.: (22) 569-38-28, fax: (22) 569-37-12
e-mail: janikj@cmkp.edu.pl

Postępy Nauk Medycznych 11/2011
Strona internetowa czasopisma Postępy Nauk Medycznych