A review of adaptive mechanisms in cell responses towards oxidative stress caused by dental resin monomers

Biomaterials

Volumn 34, Issue 19, 2013, Pages 4555-4563

  Krifka, Stephanie ^a   Spagnuolo, Gianrico ^b   Schmalz, Gottfried ^a   Schweikl, Helmut ^a  

^a UNIVERSITY HOSPITAL REGENSBURG   (Germany)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Adaptive cell response; Dental composite; Oxidative stress; Resin monomer

Indexed keywords

ATAXIA-TELANGIECTASIA MUTATED; CELL RESPONSE; DENTAL RESTORATIVE MATERIALS; MITOGEN ACTIVATED PROTEIN KINASE; NON-ENZYMATIC ANTIOXIDANTS; RESIN MONOMER; SIGNAL TRANSDUCTION PATHWAYS; TRIETHYLENE GLYCOL DIMETHACRYLATE;

ACRYLIC MONOMERS; CELL CULTURE; CELL DEATH; DENTAL COMPOSITES; DENTAL MATERIALS; INTERFACES (MATERIALS); LIVING POLYMERIZATION; OXIDATIVE STRESS; OXYGEN; PEPTIDES; PLANTS (BOTANY); RESINS; RESTORATION; SIGNAL TRANSDUCTION; STEM CELLS; TISSUE; TRANSCRIPTION FACTORS;

MONOMERS;

ACTIVATING TRANSCRIPTION FACTOR 2; ACTIVATING TRANSCRIPTION FACTOR 3; ANTIOXIDANT; CATALASE; CHECKPOINT KINASE 2; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HEME OXYGENASE 1; HISTONE H2AX; MITOGEN ACTIVATED PROTEIN KINASE; MONOMER; PROTEIN C JUN; PROTEIN P53; REACTIVE OXYGEN METABOLITE; RESIN; TRIETHYLENE GLYCOL DIMETHACRYLATE;

ADAPTIVE IMMUNITY; ANTIOXIDANT ACTIVITY; APOPTOSIS; CELL CULTURE; CELL DEATH; CELL FUNCTION; CELL SURVIVAL; CYTOTOXICITY; DNA DAMAGE; MOUTH CAVITY; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVIEW; SIGNAL TRANSDUCTION;

ACRYLIC RESINS; ANIMALS; APOPTOSIS; COMPOSITE RESINS; DNA DAMAGE; ENZYME ACTIVATION; GLUTATHIONE; HUMANS; MAP KINASE SIGNALING SYSTEM; MUTAGENS; OXIDATIVE STRESS; POLYURETHANES; REACTIVE OXYGEN SPECIES; TRANSCRIPTION FACTORS;

ATAXIA TELANGIECTASIA;

EID: 84875823839     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2013.03.019     Document Type: Review

References (138)

1. Cramer N.B., Stansbury J.W., Bowman C.N. Recent advances and developments in composite dental restorative materials. JDent Res 2011, 90:402-416.
2. Ferracane J.L. Resin composite-state of the art. Dent Mater 2011, 27:29-38.
3. Sadowsky S.J. An overview of treatment considerations for esthetic restorations: a review of the literature. JProsthet Dent 2006, 96:433-442.
4. Demarco F.F., Corrêa M.B., Cenci M.S., Moraes R.R., Opdam N.J. Longevity of posterior composite restorations: not only a matter of materials. Dent Mater 2012, 28:87-101.
5. Williams D.F. On the nature of biomaterials. Biomaterials 2009, 30:5897-5909.
6. Chen M.H. Update on dental nanocomposites. JDent Res 2010, 89:549-560.
7. Peutzfeldt A. Resin composites in dentistry: the monomer systems. Eur J Oral Sci 1997, 105:97-116.
8. Van Landuyt K.L., Snauwaert J., De Munck J., Peumans M., Yoshida Y., Poitevin A., et al. Systematic review of the chemical composition of contemporary dental adhesives. Biomaterials 2007, 28:3757-3785.
9. Durner J., Spahl W., Zaspel J., Schweikl H., Hickel R., Reichl F.X. Eluted substances from unpolymerized and polymerized dental restorative materials and their Nernst partition coefficient. Dent Mater 2010, 26:91-99.
10. Drummond J.L. Degradation, fatigue, and failure of resin dental composite materials. JDent Res 2008, 87:710-719.
11. Ferracane J.L. Elution of leachable components from composites. JOral Rehabil 1994, 21:441-452.
12. Ferracane J.L. Resin-based composite performance: are there some things we can't predict?. Dent Mater 2013, 29:51-58.
13. Santerre J.P., Shajii L., Leung B.W. Relation of dental composite formulations to their degradation and the release of hydrolyzed polymeric-resin-derived products. Crit Rev Oral Biol Med 2001, 12:136-151.
14. Van Landuyt K.L., Nawrot T., Geebelen B., De Munck J., Snauwaert J., Yoshihara K., et al. How much do resin-based dental materials release? A meta-analytical approach. Dent Mater 2011, 27:723-747.
15. Seiss M., Langer C., Hickel R., Reichl F.X. Quantitative determination of TEGDMA, BHT, and DMABEE in eluates from polymerized resin-based dental restorative materials by use of GC/MS. Arch Toxicol 2009, 83:1109-1115.
16. Costa C.A., Hebling J., Hanks C.T. Current status of pulp capping with dentin adhesive systems: a review. Dent Mater 2000, 16:188-197.
17. Murray P.E., Hafez A.A., Windsor L.J., Smith A.J., Cox C.F. Comparison of pulp responses following restoration of exposed and non-exposed cavities. JDent 2002, 30:213-222.
18. Modena K.C., Casas-Apayco L.C., Atta M.T., Costa C.A., Hebling J., Sipert C.R., et al. Cytotoxicity and biocompatibility of direct and indirect pulp capping materials. JAppl Oral Sci 2009, 17:544-554.
19. Hanks C.T., Strawn S.E., Wataha J.C., Craig R.G. Cytotoxic effects of resin components on cultured mammalian fibroblasts. JDent Res 1991, 70:1450-1455.
20. Geurtsen W. Biocompatibility of resin-modified filling materials. Crit Rev Oral Biol Med 2000, 11:333-355.
21. Nocca G., Ragno R., Carbone V., Martorana G.E., Rossetti D.V., Gambarini G., et al. Identification of glutathione-methacrylates adducts in gingival fibroblasts and erythrocytes by HPLC-MS and capillary electrophoresis. Dent Mater 2011, 27:e87-98.
22. Schweikl H., Spagnuolo G., Schmalz G. Genetic and cellular toxicology of dental resin monomers. JDent Res 2006, 85:870-877.
23. Chang H.H., Guo M.K., Kasten F.H., Chang M.C., Huang G.F., Wang Y.L., et al. Stimulation of glutathione depletion, ROS production and cell cycle arrest of dental pulp cells and gingival epithelial cells by HEMA. Biomaterials 2005, 26:745-753.
24. Schweikl H., Hartmann A., Hiller K.A., Spagnuolo G., Bolay C., Brockhoff G., et al. Inhibition of TEGDMA and HEMA-induced genotoxicity and cell cycle arrest by N-acetylcysteine. Dent Mater 2007, 23:688-695.
25. Eckhardt A., Harorli T., Limtanyakul J., Hiller K.A., Bosl C., Bolay C., et al. Inhibition of cytokine and surface antigen expression in LPS-stimulated murine macrophages by triethylene glycol dimethacrylate. Biomaterials 2009, 30:1665-1674.
26. Schmalz G., Krifka S., Schweikl H. Toll-like receptors, LPS, and dental monomers. Adv Dent Res 2011, 23:302-306.
27. Bølling A.K., Samuelsen J.T., Morisbak E., Ansteinsson V., Becher R., Dahl J.E., et al. Dental monomers inhibit LPS-induced cytokine release from the macrophage cell line RAW264.7. Toxicol Lett 2013, 216:130-138.
28. Tsukimura N., Yamada M., Aita H., Hori N., Yoshino F., Chang-II Lee M., et al. Biomaterials 2009, 30:3378-3389.
29. Galler K., Schweikl H., Hiller K.A., Cavender A., Bolay C., D'Souza R., et al. TEGDMA reduces the expression of genes involved in biomineralization. JDent Res 2011, 90:257-262.
30. About I. Dentin regeneration invitro: the pivotal role of supportive cells. Adv Dent Res 2011, 23:320-324.
31. About I., Camps J., Mitsiadis T.A., Bottero M.J., Butler W., Franquin J.C. Influence of resinous monomers on the differentiation invitro of human pulp cells into odontoblasts. Biomed Mater Res 2002, 63:418-423.
32. Bakopoulou A., Leyhausen G., Volk J., Tsiftsoglou A., Garefis P., Koidis P., et al. Effects of HEMA and TEDGMA on the invitro odontogenic differentiation potential of human pulp stem/progenitor cells derived from deciduous teeth. Dent Mater 2011, 27:608-617.
33. Bakopoulou A., Leyhausen G., Volk J., Koidis P., Geurtsen W. Effects of resinous monomers on the odontogenic differentiation and mineralization potential of highly proliferative and clonogenic cultured apical papilla stem cells. Dent Mater 2012, 28:327-339.
34. Dröge W. Free radicals in the physiological control of cell function. Physiol Rev 2002, 82:47-95.
35. Kohen R., Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification. Toxicol Pathol 2002, 30:620-650.
36. Genestra M. Oxyl radicals, redox-sensitive signalling cascades and antioxidants. Cell Signal 2007, 19:1807-1819.
37. Forman H.J., Torres M. Redox signaling in macrophages. Mol Aspects Med 2001, 22:189-216.
38. Valko M., Izakovic M., Mazur M., Rhodes C.J., Telser J. Role of oxygen radicals in DNA damage and cancer incidence. Mol Cell Biochem 2004, 266:37-56.
39. Pervaiz S., Taneja R., Ghaffari S. Oxidative stress regulation of stem and progenitor cells. Antioxid Redox Signal 2009, 11:2777-2789.
40. D'Autréaux B., Toledano M.B. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007, 8:813-824.
41. Halliwell B. Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radic Res 1999, 31:261-272.
42. Trachootham D., Lu W., Ogasawara M.A., Nilsa R.D., Huang P. Redox regulation of cell survival. Antioxid Redox Signal 2008, 10:1343-1374.
43. Circu M.L., Aw T.Y. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 2010, 48:749-762.
44. Forman H.J., Zhang H., Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med 2009, 30:1-12.
45. Lu S.C. Regulation of glutathione synthesis. Mol Aspects Med 2009, 30:42-59.
46. Brigelius-Flohé R. Tissue-specific functions of individual glutathione peroxidases. Free Radic Biol Med 1999, 27:951-965.
47. Han D., Hanawa N., Saberi B., Kaplowitz N. Mechanisms of liver injury. III. Role of glutathione redox status in liver injury. Am J Physiol Gastrointest Liver Physiol 2006, 291:G1-G7.
48. Schäfer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001, 30:1191-1212.
49. Jones D.P. Redefining oxidative stress. Antioxid Redox Signal 2006, 8:1865-1879.
50. Stanislawski L., Lefeuvre M., Bourd K., Soheili-Majd E., Goldberg M., Périanin A. TEGDMA-induced toxicity in human fibroblasts is associated with early and drastic glutathione depletion with subsequent production of oxygen reactive species. JBiomed Mater Res A 2003, 66:476-482.
51. Walther U.I., Siagian, Walther S.C., Reichl F.X., Hickel R. Antioxidative vitamins decrease cytotoxicity of HEMA and TEGDMA in cultured cell lines. Arch Oral Biol 2004, 49:125-131.
52. Samuelsen J.T., Kopperud H.M., Holme J.A., Dragland I.S., Christensen T., Dahl J.E. Role of thiol-complex formation in 2-hydroxyethyl- methacrylate-induced toxicity invitro. JBiomed Mater Res A 2011, 96:395-401.
53. Schweikl H., Schmalz G. Triethylene glycol dimethacrylate induces large deletions in the hprt gene of V79 cells. Mutat Res 1999, 438:71-78.
54. Geurtsen W., Leyhausen G. Chemical-biological interactions of the resin monomer triethyleneglycol-dimethacrylate (TEGDMA). JDent Res 2001, 80:2046-2050.
55. Yamada M., Kojima N., Paranjpe A., Att W., Aita H., Jewett A., et al. N-acetyl cysteine (NAC)-assisted detoxification of PMMA resin. JDent Res 2008, 87:372-377.
56. Yamada M., Ogawa T. Chemodynamics underlying N-acetyl cysteine-mediated bone cement monomer detoxification. Acta Biomater 2009, 5:2963-2973.
57. Nocca G., D'Antò V., Desiderio C., Rossetti D.V., Valletta R., Baquala A.M., et al. N-acetyl cysteine directed detoxification of 2-hydroxyethyl methacrylate by adduct formation. Biomaterials 2010, 31:2508-2516.
58. Zafarullah M., Li W.Q., Sylvester J., Ahmad M. Molecular mechanisms of N-acetylcysteine actions. Cell Mol Life Sci 2003, 60:6e20.
59. Paranjpe A., Cacalano N.A., Hume W.R., Jewett A. N-acetylcysteine protects dental pulp stromal cells from HEMA-induced apoptosis by inducing differentiation of the cells. Free Radic Biol Med 2007, 43:1394-1408.
60. Paranjpe A., Cacalano N.A., Hume W.R., Jewett A. N-acetyl cysteine mediates protection from 2-hydroxyethyl methacrylate induced apoptosis via nuclear factor kappa B-dependent and independent pathways: potential involvement of JNK. Toxicol Sci 2009, 108:356-366.
61. Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem 1995, 64:97-112.
62. Miller A.F. Superoxide dismutases: ancient enzymes and new insights. FEBS Lett 2012, 586:585-595.
63. Rhee S.G., Chae H.Z., Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 2005, 38:11-17.
64. Zamocky M., Furtmüller P.G., Obinger C. Evolution of catalases from bacteria to humans. Antioxid Redox Signal 2008, 10:1527-1548.
65. Griffith O.W., Meister A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). JBiol Chem 1979, 254:7558-7560.
66. Williamson J.M., Meister A. Stimulation of hepatic glutathione formation by administration of L-2-oxothiazolidine-4-carboxylate, a 5-oxo-L-prolinase substrate. Proc Natl Acad Sci U S A 1981, 78:936-939.
67. Krifka S., Hiller K.A., Spagnuolo G., Jewett A., Schmalz G., Schweikl H. The influence of glutathione on redox regulation by antioxidant proteins and apoptosis in macrophages exposed to 2-hydroxyethyl methacrylate (HEMA). Biomaterials 2012, 33:5177-5186.
68. Lei X.G., Cheng W.H., McClung J.P. Metabolic regulation and function of glutathione peroxidase-1. Annu Rev Nutr 2007, 27:41-61.
69. 2 permeation through cytoplasmic and peroxisomal membranes: comparison with experimental data. Biochim Biophys Acta 2004, 1673:149-159.
70. Gozzelino R., Jeney V., Soares M.P. Mechanisms of cell protection by heme oxygenase-1. Annu Rev Pharmacol Toxicol 2010, 50:323-354.
71. Durante W. Protective role of heme oxygenase-1 against inflammation in atherosclerosis. Front Biosci 2011, 16:2372-2388.
72. Schweikl H., Hiller K.A., Eckhardt A., Bolay C., Spagnuolo G., Stempfl T., et al. Differential gene expression involved in oxidative stress response caused by triethylene glycol dimethacrylate. Biomaterials 2008, 29:1377-1387.
73. Spagnuolo G., D'Antò V., Cosentino C., Schmalz G., Schweikl H., Rengo S. Effect of N-acetyl-L-cysteine on ROS production and cell death caused by HEMA in human primary gingival fibroblasts. Biomaterials 2006, 27:1803-1809.
74. De Vries N., De Flora S. N-acetyl-l-cysteine. JCell Biochem Suppl 1993, 17F:270-277.
75. Spagnuolo G., Mauro C., Leonardi A., Santillo M., Paternò R., Schweikl H., et al. NF-kappaB protection against apoptosis induced by HEMA. JDent Res 2004, 83:837-842.
76. Huang C.S., Moore W.R., Meister A. On the active site thiol of gamma-glutamylcysteine synthetase: relationships to catalysis, inhibition, and regulation. Proc Natl Acad Sci U S A 1988, 85:2464-2468.
77. Runchel C., Matsuzawa A., Ichijo H. Mitogen-activated protein kinases in mammalian oxidative stress responses. Antioxid Redox Signal 2011, 15:205-218.
78. Gaestel M. Specificity of signaling from MAPKs to MAPKAPKs: kinases' tango nuevo. Front Biosci 2008, 13:6050-6059.
79. Keshet Y., Seger R. The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions. Methods Mol Biol 2010, 661:3-38.
80. Chambard J.C., Lefloch R., Pouyssegur J., Lenormand P. ERK implication in cell cycle regulation. Biochim Biophys Acta 2007, 1773:1299-1310.
81. Shaul Y.D., Seger R. The MEK/ERK cascade: from signaling specificity to diverse functions. Biochim Biophys Acta 2007, 1773:1213-1226.
82. Pearson G., Robinson F., Beers Gibson T., Xu B.E., Karandikar M., Berman K., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr Rev 2001, 22:153-183.
83. Dong C., Davis R.J., Flavell R.A. MAP kinases in the immune response. Annu Rev Immunol 2002, 20:55-72.
84. Duch A., de Nadal E., Posas F. The p38 and Hog1 SAPKs control cell cycle progression in response to environmental stresses. FEBS Lett 2012, 586:2925-2931.
85. Whitmarsh A.J. Regulation of gene transcription by mitogen-activated protein kinase signaling pathways. Biochim Biophys Acta 2007, 1773:1285-1298.
86. Turjanski A.G., Vaqué J.P., Gutkind J.S. MAP kinases and the control of nuclear events. Oncogene 2007, 26:3240-3253.
87. Yang S.H., Whitmarsh A.J., Davis R.J., Sharrocks A.D. Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1. EMBO J 1998, 17:740-749.
88. Rubinfeld H., Seger R. The ERK cascade: a prototype of MAPK signaling. Mol Biotechnol 2005, 31:151-174.
89. Besnard A., Galan-Rodriguez B., Vanhoutte P., Caboche J. Elk-1 a transcription factor with multiple facets in the brain. Front Neurosci 2011, 5:35.
90. Dérijard B., Hibi M., Wu I.H., Barrett T., Su B., Deng T., et al. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994, 76:1025-1037.
91. Cuenda A., Rousseau S. p38 MAP-kinases pathway regulation, function and role in human diseases. Biochim Biophys Acta 2007, 1773:1358-1375.
92. Brenner D.A., O'Hara M., Angel P., Chojkier M., Karin M. Prolonged activation of jun and collagenase genes by tumour necrosis factor-alpha. Nature 1989, 337:661-663.
93. Devary Y., Gottlieb R.A., Lau L.F., Karin M. Rapid and preferential activation of the c-jun gene during the mammalian UV response. Mol Cell Biol 1991, 11:2804-2811.
94. Wagner E.F., Nebreda A.R. Signal integration by JNK and p38 MAPK pathways in cancer development. Nat Rev Cancer 2009, 9:537-549.
95. Bhoumik A., Lopez-Bergami P., Ronai Z. ATF2 on the double - activating transcription factor and DNA damage response protein. Pigment Cell Res 2007, 20:498-506.
96. Maekawa T., Shinagawa T., Sano Y., Sakuma T., Nomura S., Nagasaki K., et al. Reduced levels of ATF-2 predispose mice to mammary tumors. Mol Cell Biol 2007, 27:1730-1744.
97. Bhoumik A., Ronai Z. ATF2: a transcription factor that elicits oncogenic or tumor suppressor activities. Cell Cycle 2008, 7:2341-2345.
98. Yan C., Lu D., Hai T., Boyd D.D. Activating transcription factor 3, a stress sensor, activates p53 by blocking its ubiquitination. EMBO J 2005, 24:2425-2435.
99. Lu D., Chen J., Hai T. The regulation of ATF3 gene expression by mitogen-activated protein kinases. Biochem J 2007, 401:559-567.
100. Samuelsen J.T., Dahl J.E., Karlsson S., Morisbak E., Becher R. Apoptosis induced by the monomers HEMA and TEGDMA involves formation of ROS and differential activation of the MAP-kinases p38, JNK and ERK. Dent Mater 2007, 23:34-39.
101. Spagnuolo G., D'Antò V., Valletta R., Strisciuglio C., Schmalz G., Schweikl H., et al. Effect of HEMA on human pulp cells survival pathways ERK and Akt. JEndod 2008, 34:684-688.
102. Eckhardt A., Gerstmayr N., Hiller K.A., Bolay C., Waha C., Spagnuolo G., et al. TEGDMA-induced oxidative DNA damage and activation of ATM and MAP Kinases. Biomaterials 2009, 30:2006-2014.
103. Krifka S., Petzel C., Hiller K.A., Frank E.M., Bosl C., Spagnuolo G., et al. Resin monomer-induced differential activation of MAP kinases and apoptosis in mouse macrophages and human pulp cells. Biomaterials 2010, 31:2964-2975.
104. Krifka S., Hiller K.A., Bolay C., Petzel C., Spagnuolo G., Reichl F.X., et al. Function of MAPK and downstream transcription factors in monomer-induced apoptosis. Biomaterials 2012, 33:740-750.
105. Fox G.C., Shafiq M., Briggs D.C., Knowles P.P., Collister M., Didmon M.J., et al. Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases. Nature 2007, 447:487-492.
106. Owens D.M., Keyse S.M. Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases. Oncogene 2007, 26:3203-3213.
107. Hegedus Z., Czibula A., Kiss-Toth E. Tribbles: novel regulators of cell function; evolutionary aspects. Cell Mol Life Sci 2006, 63:1632-1641.
108. Krifka S., Petzel C., Bolay C., Hiller K.A., Spagnuolo G., Schmalz G., et al. Activation of stress-regulated transcription factors by triethylene glycol dimethacrylate monomer. Biomaterials 2011, 32:1787-1795.
109. Hirose N., Maekawa T., Shinagawa T., Ishii S. ATF-2 regulates lipopolysaccharide-induced transcription in macrophage cells. Biochem Biophys Res Commun 2009, 385:72-77.
110. Thompson M.R., Xu D., Williams B.R. ATF3 transcription factor and its emerging roles in immunity and cancer. JMol Med (Berl) 2009, 87:1053-1060.
111. Lum H., Roebuck K.A. Oxidant stress and endothelial cell dysfunction. Am J Physiol Cell Physiol 2001, 280:C719-C741.
112. Kehrer J.P. The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 2000, 149:43-50.
113. Imlay J.A. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 2008, 77:755-776.
114. Memisoglu A., Samson L. Base excision repair in yeast and mammals. Mutat Res 2000, 451:39-51.
115. Wilson D.M., Sofinowski T.M., McNeill D.R. Repair mechanisms for oxidative DNA damage. Front Biosci 2003, 8:d963-981.
116. Tsunoda M., Sakaue T., Naito S., Sunami T., Abe N., Ueno Y., et al. Insights into the structures of DNA damaged by hydroxyl radical: crystal structures of DNA duplexes containing 5-formyluracil. JNucleic Acids 2010, 2010:107289.
117. Berquist B.R., Wilson D.M. Pathways for repairing and tolerating the spectrum of oxidative DNA lesions. Cancer Lett 2012, 327:61-72.
118. Blasiak J., Synowiec E., Tarnawska J., Czarny P., Poplawski T., Reiter R.J. Dental methacrylates may exert genotoxic effects via the oxidative induction of DNA double strand breaks and the inhibition of their repair. Mol Biol Rep 2012, 39:7487-7496.
119. Yoshida T., Mett I., Bhunia A.K., Bowman J., Perez M., Zhang L., et al. Rtp801, a suppressor of mTOR signaling, is an essential mediator of cigarette smoke-induced pulmonary injury and emphysema. Nat Med 2010, 16:767-773.
120. Kleinsasser N.H., Schmid K., Sassen A.W., Harréus U.A., Staudenmaier R., Folwaczny M., et al. Cytotoxic and genotoxic effects of resin monomers in human salivary gland tissue and lymphocytes as assessed by the single cell microgel electrophoresis (Comet) assay. Biomaterials 2006, 27:1762-1770.
121. Sancar A., Lindsey-Boltz L.A., Unsal-Kaçmaz K., Linn S. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu Rev Biochem 2004, 73:39-85.
122. Jones R.M., Petermann E. Replication fork dynamics and the DNA damage response. Biochem J 2012, 443:13-26.
123. Samuelsen J.T., Holme J.A., Becher R., Karlsson S., Morisbak E., Dahl J.E. HEMA reduces cell proliferation and induces apoptosis invitro. Dent Mater 2008, 24:134-140.
124. Shiloh Y. ATM and related protein kinases: safeguarding genome integrity. Nat Rev Cancer 2003, 3:155-168.
125. Tanaka T., Huang X., Halicka H.D., Zhao H., Traganos F., Albino A.P., et al. Cytometry of ATM activation and histone H2AX phosphorylation to estimate extent of DNA damage induced by exogenous agents. Cytometry A 2007, 71:648-661.
126. Urcan E., Scherthan H., Styllou M., Haertel U., Hickel R., Reichl F.X. Induction of DNA double-strand breaks in primary gingival fibroblasts by exposure to dental resin composites. Biomaterials 2010, 31:2010-2014.
127. Ansteinsson V., Solhaug A., Samuelsen J.T., Holme J.A., Dahl J.E. DNA-damage, cell-cycle arrest and apoptosis induced in BEAS-2B cells by 2-hydroxyethyl methacrylate (HEMA). Mutat Res 2011, 723:158-164.
128. Szczepanska J., Poplawski T., Synowiec E., Pawlowska E., Chojnacki C.J., Chojnacki J., et al. 2-hydroxylethyl methacrylate (HEMA), a tooth restoration component, exerts its genotoxic effects in human gingival fibroblasts trough methacrylic acid, an immediate product of its degradation. Mol Biol Rep 2012, 39:1561-1574.
129. Durner J., Debiak M., Bürkle A., Hickel R., Reichl F.X. Induction of DNA strand breaks by dental composite components compared to X-ray exposure in human gingival fibroblasts. Arch Toxicol 2011, 85:143-148.
130. Lavin M.F., Gueven N. The complexity of p53 stabilization and activation. Cell Death Differ 2006, 13:941-950.
131. Toledo F., Wahl G.M. Regulating the p53 pathway: invitro hypotheses, invivo veritas. Nat Rev Cancer 2006, 6:909-923.
132. Kruse J.P., Gu W. Modes of p53 regulation. Cell 2009, 137:609-622.
133. Yu J., Zhang L.P.U.M.A. Apotent killer with or without p53. Oncogene 2009, 27:S71-S83.
134. Gartel A.L. p21(WAF1/CIP1) and cancer: a shifting paradigm?. Biofactors 2009, 35:161-164.
135. Asada M., Yamada T., Ichijo H., Delia D., Miyazono K., Fukumuro K., et al. Apoptosis inhibitory activity of cytoplasmic p21(Cip1/WAF1) in monocytic differentiation. EMBO J 1999, 18:1223-1234.
136. Zhan J., Easton J.B., Huang S., Mishra A., Xiao L., Lacy E.R., et al. Negative regulation of ASK1 by p21Cip1 involves a small domain that includes Serine 98 that is phosphorylated by ASK1 invivo. Mol Cell Biol 2007, 27:3530-3541.
137. Schweikl H., Altmannberger I., Hanser N., Hiller K.A., Bolay C., Brockhoff G., et al. The effect of triethylene glycol dimethacrylate on the cell cycle of mammalian cells. Biomaterials 2005, 26:4111-4118.
138. Pawlowska E., Poplawski T., Ksiazek D., Szczepanska J., Blasiak J. Genotoxicity and cytotoxicity of 2-hydroxyethyl methacrylate. Mutat Res 2010, 696:122-129.