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Volumn 305, Issue , 2013, Pages 120-129

APE1/Ref-1 prevents oxidative inactivation of ERK for G1-to-S progression following lead acetate exposure

Author keywords

APE1; Cyclin D1; ERK; Heavy metal; Oxidation

Indexed keywords

APURINIC APYRIMIDINIC ENDONUCLEASE 1; CYCLIN D1; CYSTEINE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; E 3330; LEAD ACETATE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; REACTIVE OXYGEN METABOLITE; REDOX EFFECTOR FACTOR 1; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84873962597     PISSN: 0300483X     EISSN: 18793185     Source Type: Journal    
DOI: 10.1016/j.tox.2013.01.010     Document Type: Article
Times cited : (18)

References (47)
  • 1
    • 48349107170 scopus 로고    scopus 로고
    • A new APE1/Ref-1-dependent pathway leading to reduction of NF-κB and AP-1, and activation of their DNA-binding activity
    • Ando K., Hirao S., Kabe Y., Ogura Y., Sato I., Yamaguchi Y., Wada T., Handa H. A new APE1/Ref-1-dependent pathway leading to reduction of NF-κB and AP-1, and activation of their DNA-binding activity. Nucleic Acids Res. 2008, 36:4327-4336.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4327-4336
    • Ando, K.1    Hirao, S.2    Kabe, Y.3    Ogura, Y.4    Sato, I.5    Yamaguchi, Y.6    Wada, T.7    Handa, H.8
  • 2
    • 58849117092 scopus 로고    scopus 로고
    • Transcriptional regulatory functions of mammalian AP-endonuclease (APE1/Ref-1), an essential multifunctional protein
    • Bhakat K.K., Mantha A.K., Mitra S. Transcriptional regulatory functions of mammalian AP-endonuclease (APE1/Ref-1), an essential multifunctional protein. Antioxid. Redox Signal. 2009, 11:621-638.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 621-638
    • Bhakat, K.K.1    Mantha, A.K.2    Mitra, S.3
  • 3
    • 17644373442 scopus 로고    scopus 로고
    • Redox regulation of cell-cycle re-entry: cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species
    • Burch P.M., Heintz N.H. Redox regulation of cell-cycle re-entry: cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species. Antioxid. Redox Signal. 2005, 7:741-751.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 741-751
    • Burch, P.M.1    Heintz, N.H.2
  • 4
    • 0033867513 scopus 로고    scopus 로고
    • Activation of JNK, p38 and ERK mitogen-activated protein kinases by chromium(VI) is mediated through oxidative stress but does not affect cytotoxicity
    • Chuang S.M., Liou G.Y., Yang J.L. Activation of JNK, p38 and ERK mitogen-activated protein kinases by chromium(VI) is mediated through oxidative stress but does not affect cytotoxicity. Carcinogenesis 2000, 21:1491-1500.
    • (2000) Carcinogenesis , vol.21 , pp. 1491-1500
    • Chuang, S.M.1    Liou, G.Y.2    Yang, J.L.3
  • 5
    • 0033923816 scopus 로고    scopus 로고
    • Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium
    • Chuang S.M., Wang I.C., Yang J.L. Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium. Carcinogenesis 2000, 21:1423-1432.
    • (2000) Carcinogenesis , vol.21 , pp. 1423-1432
    • Chuang, S.M.1    Wang, I.C.2    Yang, J.L.3
  • 6
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon A.S., Hagan S., Rath O., Kolch W. MAP kinase signalling pathways in cancer. Oncogene 2007, 26:3279-3290.
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 7
    • 84873957737 scopus 로고    scopus 로고
    • Toxicity of lead: a review with recent updates
    • Flora G., Gupta D., Tiwari A. Toxicity of lead: a review with recent updates. Interdiscip. Toxicol. 2012, 5:47-58.
    • (2012) Interdiscip. Toxicol. , vol.5 , pp. 47-58
    • Flora, G.1    Gupta, D.2    Tiwari, A.3
  • 8
    • 0035834764 scopus 로고    scopus 로고
    • Key role of a downstream specificity protein 1 site in cell cycle-regulated transcription of the AP endonuclease gene APE1/APEX in NIH3T3 cells
    • Fung H., Bennett R.A., Demple B. Key role of a downstream specificity protein 1 site in cell cycle-regulated transcription of the AP endonuclease gene APE1/APEX in NIH3T3 cells. J. Biol. Chem. 2001, 276:42011-42017.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42011-42017
    • Fung, H.1    Bennett, R.A.2    Demple, B.3
  • 9
    • 37549004372 scopus 로고    scopus 로고
    • ATF4-dependent oxidative induction of the DNA repair enzyme Ape1 counteracts arsenite cytotoxicity and suppresses arsenite-mediated mutagenesis
    • Fung H., Liu P., Demple B. ATF4-dependent oxidative induction of the DNA repair enzyme Ape1 counteracts arsenite cytotoxicity and suppresses arsenite-mediated mutagenesis. Mol. Cell. Biol. 2007, 27:8834-8847.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8834-8847
    • Fung, H.1    Liu, P.2    Demple, B.3
  • 11
    • 0032188756 scopus 로고    scopus 로고
    • Apurinic endonuclease (Ref-1) is induced in mammalian cells by oxidative stress and involved in clastogenic adaptation
    • Grosch S., Fritz G., Kaina B. Apurinic endonuclease (Ref-1) is induced in mammalian cells by oxidative stress and involved in clastogenic adaptation. Cancer Res. 1998, 58:4410-4416.
    • (1998) Cancer Res. , vol.58 , pp. 4410-4416
    • Grosch, S.1    Fritz, G.2    Kaina, B.3
  • 13
    • 39049174594 scopus 로고    scopus 로고
    • IARC, Inorganic and organic lead compounds
    • IARC Monographs on the Evaluation of Carcinogenic Risks to Human
    • IARC, 2006. Inorganic and organic lead compounds. IARC Monographs on the Evaluation of Carcinogenic Risks to Human 87, pp. 1-471.
    • (2006) , vol.87 , pp. 1-471
  • 16
    • 79952070504 scopus 로고    scopus 로고
    • Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia/reperfusion injury with resin-assisted capture
    • Kohr M.J., Sun J., Aponte A., Wang G., Gucek M., Murphy E., Steenbergen C. Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia/reperfusion injury with resin-assisted capture. Circ. Res. 2011, 108:418-426.
    • (2011) Circ. Res. , vol.108 , pp. 418-426
    • Kohr, M.J.1    Sun, J.2    Aponte, A.3    Wang, G.4    Gucek, M.5    Murphy, E.6    Steenbergen, C.7
  • 17
    • 84860165740 scopus 로고    scopus 로고
    • Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update
    • Kyriakis J.M., Avruch J. Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update. Physiol. Rev. 2012, 92:689-737.
    • (2012) Physiol. Rev. , vol.92 , pp. 689-737
    • Kyriakis, J.M.1    Avruch, J.2
  • 19
    • 34347385439 scopus 로고    scopus 로고
    • 2 checkpoint elicited by arsenite
    • 2 checkpoint elicited by arsenite. J. Cell. Physiol. 2007, 212:481-488.
    • (2007) J. Cell. Physiol. , vol.212 , pp. 481-488
    • Li, J.P.1    Yang, J.L.2
  • 20
    • 84860230332 scopus 로고    scopus 로고
    • Human apurinic/apyrimidinic endonuclease 1 translocalizes to mitochondria after photodynamic therapy and protects cells from apoptosis
    • Li M.X., Shan J.L., Wang D., He Y., Zhou Q., Xia L., Zeng L.L., Li Z.P., Wang G., Yang Z.Z. Human apurinic/apyrimidinic endonuclease 1 translocalizes to mitochondria after photodynamic therapy and protects cells from apoptosis. Cancer Sci. 2012, 103:882-888.
    • (2012) Cancer Sci. , vol.103 , pp. 882-888
    • Li, M.X.1    Shan, J.L.2    Wang, D.3    He, Y.4    Zhou, Q.5    Xia, L.6    Zeng, L.L.7    Li, Z.P.8    Wang, G.9    Yang, Z.Z.10
  • 21
    • 0038498118 scopus 로고    scopus 로고
    • ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway
    • Lin Y.W., Chuang S.M., Yang J.L. ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway. J. Biol. Chem. 2003, 278:21534-21541.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21534-21541
    • Lin, Y.W.1    Chuang, S.M.2    Yang, J.L.3
  • 22
    • 0037276697 scopus 로고    scopus 로고
    • Persistent activation of ERK1/2 by lead acetate increases nucleotide excision repair synthesis and confers anti-cytotoxicity and anti-mutagenicity
    • Lin Y.W., Chuang S.M., Yang J.L. Persistent activation of ERK1/2 by lead acetate increases nucleotide excision repair synthesis and confers anti-cytotoxicity and anti-mutagenicity. Carcinogenesis 2003, 24:53-61.
    • (2003) Carcinogenesis , vol.24 , pp. 53-61
    • Lin, Y.W.1    Chuang, S.M.2    Yang, J.L.3
  • 23
    • 33644863486 scopus 로고    scopus 로고
    • Skp2 for MKP-1 destruction provides a positive feedback regulation of proliferating signaling
    • Skp2 for MKP-1 destruction provides a positive feedback regulation of proliferating signaling. J. Biol. Chem. 2006, 281:915-926.
    • (2006) J. Biol. Chem. , vol.281 , pp. 915-926
    • Lin, Y.W.1    Yang, J.L.2
  • 24
    • 33847117649 scopus 로고    scopus 로고
    • Lead promotes abasic site accumulation and co-mutagenesis in mammalian cells by inhibiting the major abasic endonuclease Ape1
    • McNeill D.R., Wong H.K., Narayana A., Wilson D.M. Lead promotes abasic site accumulation and co-mutagenesis in mammalian cells by inhibiting the major abasic endonuclease Ape1. Mol. Carcinog. 2007, 46:91-99.
    • (2007) Mol. Carcinog. , vol.46 , pp. 91-99
    • McNeill, D.R.1    Wong, H.K.2    Narayana, A.3    Wilson, D.M.4
  • 25
    • 0036618347 scopus 로고    scopus 로고
    • Redox factor-1/APE suppresses oxidative stress by inhibiting the rac1 GTPase
    • Ozaki M., Suzuki S., Irani K. Redox factor-1/APE suppresses oxidative stress by inhibiting the rac1 GTPase. FASEB J. 2002, 16:889-890.
    • (2002) FASEB J. , vol.16 , pp. 889-890
    • Ozaki, M.1    Suzuki, S.2    Irani, K.3
  • 26
    • 33745903081 scopus 로고    scopus 로고
    • Lead toxicity part II: the role of free radical damage and the use of antioxidants in the pathology and treatment of lead toxicity
    • Patrick L. Lead toxicity part II: the role of free radical damage and the use of antioxidants in the pathology and treatment of lead toxicity. Altern. Med. Rev. 2006, 11:114-127.
    • (2006) Altern. Med. Rev. , vol.11 , pp. 114-127
    • Patrick, L.1
  • 28
    • 0032574770 scopus 로고    scopus 로고
    • Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals
    • Ramana C.V., Boldogh I., Izumi T., Mitra S. Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:5061-5066.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5061-5066
    • Ramana, C.V.1    Boldogh, I.2    Izumi, T.3    Mitra, S.4
  • 29
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray P.D., Huang B.W., Tsuji Y. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 2012, 24:981-990.
    • (2012) Cell. Signal. , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 30
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., Bae Y.S., Lee S.R., Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000, 2000:pe1.
    • (2000) Sci. STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 31
    • 0033900168 scopus 로고    scopus 로고
    • Increased AP-1 DNA-binding activity and nuclear REF-1 accumulation in lead-exposed primary cultures of astrocytes
    • Scortegagna M., Hanbauer I. Increased AP-1 DNA-binding activity and nuclear REF-1 accumulation in lead-exposed primary cultures of astrocytes. Neurochem. Res. 2000, 25:861-866.
    • (2000) Neurochem. Res. , vol.25 , pp. 861-866
    • Scortegagna, M.1    Hanbauer, I.2
  • 33
    • 0344845177 scopus 로고    scopus 로고
    • Facilitative mechanisms of lead as a carcinogen
    • Silbergeld E.K. Facilitative mechanisms of lead as a carcinogen. Mutat. Res. 2003, 533:121-133.
    • (2003) Mutat. Res. , vol.533 , pp. 121-133
    • Silbergeld, E.K.1
  • 34
    • 14044269479 scopus 로고    scopus 로고
    • The intracellular localization of APE1/Ref-1: more than a passive phenomenon?
    • Tell G., Damante G., Caldwell D., Kelley M.R. The intracellular localization of APE1/Ref-1: more than a passive phenomenon?. Antioxid. Redox Signal. 2005, 7:367-384.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 367-384
    • Tell, G.1    Damante, G.2    Caldwell, D.3    Kelley, M.R.4
  • 35
    • 78149471195 scopus 로고    scopus 로고
    • Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment
    • Tell G., Fantini D., Quadrifoglio F. Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment. Cell. Mol. Life Sci. 2010, 67:3589-3608.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3589-3608
    • Tell, G.1    Fantini, D.2    Quadrifoglio, F.3
  • 36
    • 65349157681 scopus 로고    scopus 로고
    • Compartmentalization of redox signaling through NADPH oxidase-derived ROS
    • Ushio-Fukai M. Compartmentalization of redox signaling through NADPH oxidase-derived ROS. Antioxid. Redox Signal. 2009, 11:1289-1299.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1289-1299
    • Ushio-Fukai, M.1
  • 37
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Veal E.A., Day A.M., Morgan B.A. Hydrogen peroxide sensing and signaling. Mol. Cell 2007, 26:1-14.
    • (2007) Mol. Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 38
    • 47849098786 scopus 로고    scopus 로고
    • Activation of protein kinase Cα signaling prevents cytotoxicity and mutagenicity following lead acetate in CL3 human lung cancer cells
    • Wang C.Y., Lin Y.W., Yang J.L. Activation of protein kinase Cα signaling prevents cytotoxicity and mutagenicity following lead acetate in CL3 human lung cancer cells. Toxicology 2008, 250:55-61.
    • (2008) Toxicology , vol.250 , pp. 55-61
    • Wang, C.Y.1    Lin, Y.W.2    Yang, J.L.3
  • 39
    • 60349127816 scopus 로고    scopus 로고
    • Lead acetate induces EGFR activation upstream of SFK and PKCα linkage to the Ras/Raf-1/ERK signaling
    • Wang C.Y., Wang Y.T., Tzeng D.W., Yang J.L. Lead acetate induces EGFR activation upstream of SFK and PKCα linkage to the Ras/Raf-1/ERK signaling. Toxicol. Appl. Pharmacol. 2009, 235:244-252.
    • (2009) Toxicol. Appl. Pharmacol. , vol.235 , pp. 244-252
    • Wang, C.Y.1    Wang, Y.T.2    Tzeng, D.W.3    Yang, J.L.4
  • 40
    • 80055081332 scopus 로고    scopus 로고
    • Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3
    • Wentworth C.C., Alam A., Jones R.M., Nusrat A., Neish A.S. Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3. J. Biol. Chem. 2011, 286:38448-38455.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38448-38455
    • Wentworth, C.C.1    Alam, A.2    Jones, R.M.3    Nusrat, A.4    Neish, A.S.5
  • 41
    • 79960039308 scopus 로고    scopus 로고
    • The ERK cascade: distinct functions within various subcellular organelles
    • Wortzel I., Seger R. The ERK cascade: distinct functions within various subcellular organelles. Genes Cancer 2011, 2:195-209.
    • (2011) Genes Cancer , vol.2 , pp. 195-209
    • Wortzel, I.1    Seger, R.2
  • 42
    • 77955174568 scopus 로고    scopus 로고
    • Subcellular localization of apurinic endonuclease 1 promotes lung tumor aggressiveness via NF-κB activation
    • Wu H.H., Cheng Y.W., Chang J.T., Wu T.C., Liu W.S., Chen C.Y., Lee H. Subcellular localization of apurinic endonuclease 1 promotes lung tumor aggressiveness via NF-κB activation. Oncogene 2010, 29:4330-4340.
    • (2010) Oncogene , vol.29 , pp. 4330-4340
    • Wu, H.H.1    Cheng, Y.W.2    Chang, J.T.3    Wu, T.C.4    Liu, W.S.5    Chen, C.Y.6    Lee, H.7
  • 43
    • 0032938885 scopus 로고    scopus 로고
    • Singlet oxygen is the major species participating in the induction of DNA strand breakage and 8-hydroxydeoxyguanosine adduct by lead acetate
    • Yang J.L., Wang L.C., Chang C.Y., Liu T.Y. Singlet oxygen is the major species participating in the induction of DNA strand breakage and 8-hydroxydeoxyguanosine adduct by lead acetate. Environ. Mol. Mutagen. 1999, 33:194-201.
    • (1999) Environ. Mol. Mutagen. , vol.33 , pp. 194-201
    • Yang, J.L.1    Wang, L.C.2    Chang, C.Y.3    Liu, T.Y.4
  • 44
    • 0030476790 scopus 로고    scopus 로고
    • Lead acetate mutagenicity and mutational spectrum in the hypoxanthine guanine phosphoribosyltransferase gene of Chinese hamster ovary K1 cells
    • Yang J.L., Yeh S.C., Chang C.Y. Lead acetate mutagenicity and mutational spectrum in the hypoxanthine guanine phosphoribosyltransferase gene of Chinese hamster ovary K1 cells. Mol. Carcinog. 1996, 17:181-191.
    • (1996) Mol. Carcinog. , vol.17 , pp. 181-191
    • Yang, J.L.1    Yeh, S.C.2    Chang, C.Y.3
  • 45
    • 77950800323 scopus 로고    scopus 로고
    • Cdc20 proteolysis requires p38 MAPK signaling and Cdh1-independent APC/C ubiquitination during spindle assembly checkpoint activation by cadmium
    • Yen A.H., Yang J.L. Cdc20 proteolysis requires p38 MAPK signaling and Cdh1-independent APC/C ubiquitination during spindle assembly checkpoint activation by cadmium. J. Cell. Physiol. 2010, 223:327-334.
    • (2010) J. Cell. Physiol. , vol.223 , pp. 327-334
    • Yen, A.H.1    Yang, J.L.2
  • 46
    • 43049102429 scopus 로고    scopus 로고
    • Alteration of APE1/ref-1 expression in non-small cell lung cancer: the implications of impaired extracellular superoxide dismutase and catalase antioxidant systems
    • Yoo D.G., Song Y.J., Cho E.J., Lee S.K., Park J.B., Yu J.H., Lim S.P., Kim J.M., Jeon B.H. Alteration of APE1/ref-1 expression in non-small cell lung cancer: the implications of impaired extracellular superoxide dismutase and catalase antioxidant systems. Lung Cancer 2008, 60:277-284.
    • (2008) Lung Cancer , vol.60 , pp. 277-284
    • Yoo, D.G.1    Song, Y.J.2    Cho, E.J.3    Lee, S.K.4    Park, J.B.5    Yu, J.H.6    Lim, S.P.7    Kim, J.M.8    Jeon, B.H.9
  • 47
    • 51049091691 scopus 로고    scopus 로고
    • Small-molecule inhibitor of the AP endonuclease 1/REF-1 E3330 inhibits pancreatic cancer cell growth and migration
    • Zou G.M., Maitra A. Small-molecule inhibitor of the AP endonuclease 1/REF-1 E3330 inhibits pancreatic cancer cell growth and migration. Mol. Cancer Ther. 2008, 7:2012-2021.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2012-2021
    • Zou, G.M.1    Maitra, A.2


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