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Volumn 53, Issue 10, 2012, Pages 1929-1941

Estrogen receptor potentiates mTORC2 signaling in breast cancer cells by upregulating superoxide anions

Author keywords

Estrogen receptor; Free radicals; mTORC2; Redox signaling; ROS; Superoxide anions

Indexed keywords

ACETYLCYSTEINE; ANION; ESTROGEN RECEPTOR; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MANGANESE DERIVATIVE; MANGANESE TETRAKIS(4 BENZOIC ACID)PORPHYRIN; OXYGEN; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 84867358532     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.08.595     Document Type: Article
Times cited : (17)

References (55)
  • 1
    • 63749101977 scopus 로고    scopus 로고
    • International Agency for Research on Cancer WHO Geneva
    • International Agency for Research on Cancer World Cancer Report 2008 WHO Geneva
    • (2008) World Cancer Report
  • 2
    • 15444368857 scopus 로고    scopus 로고
    • Mechanisms of estrogen receptor signaling: Convergence of genomic and nongenomic actions on target genes
    • L. Bjornstrom, and M. Sjoberg Mechanisms of estrogen receptor signaling: convergence of genomic and nongenomic actions on target genes Mol. Endocrinol. 19 2005 833 842
    • (2005) Mol. Endocrinol. , vol.19 , pp. 833-842
    • Bjornstrom, L.1    Sjoberg, M.2
  • 3
    • 0032569831 scopus 로고    scopus 로고
    • Tamoxifen in the treatment of breast cancer
    • C.K. Osborne Tamoxifen in the treatment of breast cancer N. Engl. J. Med. 339 1998 1609 1618
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1609-1618
    • Osborne, C.K.1
  • 4
    • 71549166007 scopus 로고    scopus 로고
    • MTOR/S6K1 and MAPK/RSK signaling pathways coordinately regulate estrogen receptor alpha serine 167 phosphorylation
    • R.L. Yamnik, and M.K. Holz mTOR/S6K1 and MAPK/RSK signaling pathways coordinately regulate estrogen receptor alpha serine 167 phosphorylation FEBS Lett 584 2010 124 128
    • (2010) FEBS Lett , vol.584 , pp. 124-128
    • Yamnik, R.L.1    Holz, M.K.2
  • 5
    • 0020318808 scopus 로고
    • Antiestrogen treatment of breast cancer: An overview
    • O.H. Pearson, A. Manni, and B.M. Arafah Antiestrogen treatment of breast cancer: an overview Cancer Res. 42 1982 3424s 3429s
    • (1982) Cancer Res. , vol.42
    • Pearson, O.H.1    Manni, A.2    Arafah, B.M.3
  • 6
    • 79960182468 scopus 로고    scopus 로고
    • Novel flavonoids with antiproliferative activities against breast cancer cells
    • N. Yao, C.Y. Chen, C.Y. Wu, K. Motonishi, H.J. Kung, and K.S. Lam Novel flavonoids with antiproliferative activities against breast cancer cells J. Med. Chem. 54 2011 4339 4349
    • (2011) J. Med. Chem. , vol.54 , pp. 4339-4349
    • Yao, N.1    Chen, C.Y.2    Wu, C.Y.3    Motonishi, K.4    Kung, H.J.5    Lam, K.S.6
  • 7
    • 0034035343 scopus 로고    scopus 로고
    • A metabolite of equine estrogens, 4-hydroxyequilenin, induces DNA damage and apoptosis in breast cancer cell lines
    • Y. Chen, X. Liu, E. Pisha, A.I. Constantinou, Y. Hua, and L. Shen A metabolite of equine estrogens, 4-hydroxyequilenin, induces DNA damage and apoptosis in breast cancer cell lines Chem. Res. Toxicol. 13 2000 342 350
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 342-350
    • Chen, Y.1    Liu, X.2    Pisha, E.3    Constantinou, A.I.4    Hua, Y.5    Shen, L.6
  • 8
    • 0035945656 scopus 로고    scopus 로고
    • Estrogen and the risk of breast cancer
    • M. Clemons, and P. Goss Estrogen and the risk of breast cancer N. Engl. J. Med. 344 2001 276 285
    • (2001) N. Engl. J. Med. , vol.344 , pp. 276-285
    • Clemons, M.1    Goss, P.2
  • 9
    • 34447335052 scopus 로고    scopus 로고
    • Estrogen-induced generation of reactive oxygen and nitrogen species, gene damage, and estrogen-dependent cancers
    • D. Roy, Q. Cai, Q. Felty, and S. Narayan Estrogen-induced generation of reactive oxygen and nitrogen species, gene damage, and estrogen-dependent cancers J. Toxicol. Environ. Health B Crit. Rev. 10 2007 235 257
    • (2007) J. Toxicol. Environ. Health B Crit. Rev. , vol.10 , pp. 235-257
    • Roy, D.1    Cai, Q.2    Felty, Q.3    Narayan, S.4
  • 11
    • 18244405569 scopus 로고    scopus 로고
    • Estrogen-induced mitochondrial reactive oxygen species as signal-transducing messengers
    • Q. Felty, W.C. Xiong, D. Sun, S. Sarkar, K.P. Singh, and J. Parkash Estrogen-induced mitochondrial reactive oxygen species as signal-transducing messengers Biochemistry 44 2005 6900 6909
    • (2005) Biochemistry , vol.44 , pp. 6900-6909
    • Felty, Q.1    Xiong, W.C.2    Sun, D.3    Sarkar, S.4    Singh, K.P.5    Parkash, J.6
  • 12
    • 78650555076 scopus 로고
    • Estrogen-induced reactive oxygen species-mediated signalings contribute to breast cancer
    • V. Okoh, A. Deoraj, and D. Roy Estrogen-induced reactive oxygen species-mediated signalings contribute to breast cancer Biochim. Biophys. Acta 115-133 1815 2011
    • (1815) Biochim. Biophys. Acta , vol.115-133 , pp. 2011
    • Okoh, V.1    Deoraj, A.2    Roy, D.3
  • 13
    • 0036402136 scopus 로고    scopus 로고
    • Reactive oxygen species stimulated human hepatoma cell proliferation via cross-talk between PI3-K/PKB and JNK signaling pathways
    • S.L. Liu, X. Lin, D.Y. Shi, J. Cheng, C.Q. Wu, and Y.D. Zhang Reactive oxygen species stimulated human hepatoma cell proliferation via cross-talk between PI3-K/PKB and JNK signaling pathways Arch. Biochem. Biophys. 406 2002 173 182
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 173-182
    • Liu, S.L.1    Lin, X.2    Shi, D.Y.3    Cheng, J.4    Wu, C.Q.5    Zhang, Y.D.6
  • 14
    • 0036044379 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced apoptosis: Oxidative or reductive stress?
    • S. Pervaiz, and M.V. Clement Hydrogen peroxide-induced apoptosis: oxidative or reductive stress? Methods Enzymol. 352 2002 150 159
    • (2002) Methods Enzymol. , vol.352 , pp. 150-159
    • Pervaiz, S.1    Clement, M.V.2
  • 17
    • 0035808388 scopus 로고    scopus 로고
    • Intracellular acidification triggered by mitochondrial-derived hydrogen peroxide is an effector mechanism for drug-induced apoptosis in tumor cells
    • J.L. Hirpara, M.V. Clement, and S. Pervaiz Intracellular acidification triggered by mitochondrial-derived hydrogen peroxide is an effector mechanism for drug-induced apoptosis in tumor cells J. Biol. Chem 276 2001 514 521
    • (2001) J. Biol. Chem , vol.276 , pp. 514-521
    • Hirpara, J.L.1    Clement, M.V.2    Pervaiz, S.3
  • 18
  • 20
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • D.A. Guertin, and D.M. Sabatini Defining the role of mTOR in cancer Cancer Cell 12 2007 9 22
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 21
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • E. Jacinto, R. Loewith, A. Schmidt, S. Lin, M.A. Ruegg, and A. Hall Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive Nat. Cell Biol. 6 2004 1122 1128
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Ruegg, M.A.5    Hall, A.6
  • 22
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • D.D. Sarbassov, S.M. Ali, D.H. Kim, D.A. Guertin, R.R. Latek, and H. Erdjument-Bromage Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton Curr. Biol. 14 2004 1296 1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6
  • 23
    • 77952305228 scopus 로고    scopus 로고
    • Targeting mTORC2 inhibits colon cancer cell proliferation in vitro and tumor formation in vivo
    • D. Roulin, Y. Cerantola, A. Dormond-Meuwly, N. Demartines, and O. Dormond Targeting mTORC2 inhibits colon cancer cell proliferation in vitro and tumor formation in vivo Mol. Cancer 9 2010 57
    • (2010) Mol. Cancer , vol.9 , pp. 57
    • Roulin, D.1    Cerantola, Y.2    Dormond-Meuwly, A.3    Demartines, N.4    Dormond, O.5
  • 26
    • 28144440871 scopus 로고    scopus 로고
    • Changes in cytoskeletal protein composition indicative of an epithelial-mesenchymal transition in human micrometastatic and primary breast carcinoma cells
    • B. Willipinski-Stapelfeldt, S. Riethdorf, V. Assmann, U. Woelfle, T. Rau, and G. Sauter Changes in cytoskeletal protein composition indicative of an epithelial-mesenchymal transition in human micrometastatic and primary breast carcinoma cells Clin. Cancer Res. 11 2005 8006 8014
    • (2005) Clin. Cancer Res. , vol.11 , pp. 8006-8014
    • Willipinski-Stapelfeldt, B.1    Riethdorf, S.2    Assmann, V.3    Woelfle, U.4    Rau, T.5    Sauter, G.6
  • 27
    • 20144362478 scopus 로고    scopus 로고
    • The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability
    • S.A. Dames, J.M. Mulet, K. Rathgeb-Szabo, M.N. Hall, and S. Grzesiek The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability J. Biol. Chem. 280 2005 20558 20564
    • (2005) J. Biol. Chem. , vol.280 , pp. 20558-20564
    • Dames, S.A.1    Mulet, J.M.2    Rathgeb-Szabo, K.3    Hall, M.N.4    Grzesiek, S.5
  • 28
    • 54449091769 scopus 로고    scopus 로고
    • Superoxide anions regulate TORC1 and its ability to bind Fpr1:rapamycin complex
    • T.K. Neklesa, and R.W. Davis Superoxide anions regulate TORC1 and its ability to bind Fpr1:rapamycin complex Proc. Natl. Acad. Sci. USA 105 2008 15166 15171
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15166-15171
    • Neklesa, T.K.1    Davis, R.W.2
  • 29
    • 79957657436 scopus 로고    scopus 로고
    • Bile acid receptor agonist GW4064 regulates PPARgamma coactivator-1alpha expression through estrogen receptor-related receptor alpha
    • S.K. Dwivedi, N. Singh, R. Kumari, J.S. Mishra, S. Tripathi, and P. Banerjee Bile acid receptor agonist GW4064 regulates PPARgamma coactivator-1alpha expression through estrogen receptor-related receptor alpha Mol. Endocrinol. 25 2011 922 932
    • (2011) Mol. Endocrinol. , vol.25 , pp. 922-932
    • Dwivedi, S.K.1    Singh, N.2    Kumari, R.3    Mishra, J.S.4    Tripathi, S.5    Banerjee, P.6
  • 30
    • 0344043305 scopus 로고    scopus 로고
    • Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis
    • F.J. Miller Jr., D.D. Gutterman, C.D. Rios, D.D. Heistad, and B.L. Davidson Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis Circ Res 82 1998 1298 1305
    • (1998) Circ Res , vol.82 , pp. 1298-1305
    • Miller Jr., F.J.1    Gutterman, D.D.2    Rios, C.D.3    Heistad, D.D.4    Davidson, B.L.5
  • 32
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • M.W. Pfaffl A new mathematical model for relative quantification in real-time RT-PCR Nucleic Acids Res 29 e45 2001
    • (2001) Nucleic Acids Res , vol.29 E45
    • Pfaffl, M.W.1
  • 33
    • 77954235821 scopus 로고    scopus 로고
    • Targeting mTOR: Prospects for mTOR complex 2 inhibitors in cancer therapy
    • C.A. Sparks, and D.A. Guertin Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy Oncogene 29 2010 3733 3744
    • (2010) Oncogene , vol.29 , pp. 3733-3744
    • Sparks, C.A.1    Guertin, D.A.2
  • 34
    • 0842291432 scopus 로고    scopus 로고
    • Identification of estrogen-responsive genes by complementary deoxyribonucleic acid microarray and characterization of a novel early estrogen-induced gene: EEIG1
    • D.Y. Wang, R. Fulthorpe, S.N. Liss, and E.A. Edwards Identification of estrogen-responsive genes by complementary deoxyribonucleic acid microarray and characterization of a novel early estrogen-induced gene: EEIG1 Mol. Endocrinol. 18 2004 402 411
    • (2004) Mol. Endocrinol. , vol.18 , pp. 402-411
    • Wang, D.Y.1    Fulthorpe, R.2    Liss, S.N.3    Edwards, E.A.4
  • 35
    • 62449266454 scopus 로고    scopus 로고
    • Specific phosphorylation of mammalian target of rapamycin (mTOR): Phospho-Ser2481 is a marker for intact mTOR signaling complex 2
    • J. Copp, G. Manning, and T.T.O.R.C. Hunter specific phosphorylation of mammalian target of rapamycin (mTOR): phospho-Ser2481 is a marker for intact mTOR signaling complex 2 Cancer Res 69 2009 1821 1827
    • (2009) Cancer Res , vol.69 , pp. 1821-1827
    • Copp, J.1    Manning, G.2    Hunter, T.T.O.R.C.3
  • 36
    • 68049126433 scopus 로고    scopus 로고
    • Signaling events downstream of mammalian target of rapamycin complex 2 are attenuated in cells and tumors deficient for the tuberous sclerosis complex tumor suppressors
    • J. Huang, S. Wu, C.L. Wu, and B.D. Manning Signaling events downstream of mammalian target of rapamycin complex 2 are attenuated in cells and tumors deficient for the tuberous sclerosis complex tumor suppressors Cancer Res 69 2009 6107 6114
    • (2009) Cancer Res , vol.69 , pp. 6107-6114
    • Huang, J.1    Wu, S.2    Wu, C.L.3    Manning, B.D.4
  • 37
    • 47949125486 scopus 로고    scopus 로고
    • The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C
    • V. Facchinetti, W. Ouyang, H. Wei, N. Soto, A. Lazorchak, and C. Gould The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C EMBO J 27 2008 1932 1943
    • (2008) EMBO J , vol.27 , pp. 1932-1943
    • Facchinetti, V.1    Ouyang, W.2    Wei, H.3    Soto, N.4    Lazorchak, A.5    Gould, C.6
  • 38
    • 79953216041 scopus 로고    scopus 로고
    • Evidence for direct activation of mTORC2 kinase activity by phosphatidylinositol 3,4,5-trisphosphate
    • X. Gan, J. Wang, B. Su, and D. Wu Evidence for direct activation of mTORC2 kinase activity by phosphatidylinositol 3,4,5-trisphosphate J. Biol. Chem. 286 2011 10998 11002
    • (2011) J. Biol. Chem. , vol.286 , pp. 10998-11002
    • Gan, X.1    Wang, J.2    Su, B.3    Wu, D.4
  • 39
    • 33748438978 scopus 로고    scopus 로고
    • Redox regulation of endogenous substrate oxidation by cardiac mitochondria
    • P. Korge, and J.N. Weiss Redox regulation of endogenous substrate oxidation by cardiac mitochondria Am. J. Physiol. Heart Circ. Physiol 291 2006 H1436 H1445
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.291
    • Korge, P.1    Weiss, J.N.2
  • 41
    • 0024397410 scopus 로고
    • Catechol estrogen formation in MCF-7 cell culture and effects of bromoestrogen inhibitors
    • R.W. Brueggemeier, N.E. Katlic, C.W. Palmer Jr, and J.M. Stevens Catechol estrogen formation in MCF-7 cell culture and effects of bromoestrogen inhibitors Mol. Cell. Endocrinol. 64 1989 161 167
    • (1989) Mol. Cell. Endocrinol. , vol.64 , pp. 161-167
    • Brueggemeier, R.W.1    Katlic, N.E.2    Palmer Jr., C.W.3    Stevens, J.M.4
  • 44
    • 10044225935 scopus 로고    scopus 로고
    • Strong calcium entry activates mitochondrial superoxide generation, upregulating kinase signaling in hippocampal neurons
    • J. Hongpaisan, C.A. Winters, and S.B. Andrews Strong calcium entry activates mitochondrial superoxide generation, upregulating kinase signaling in hippocampal neurons J. Neurosci. 24 2004 10878 10887
    • (2004) J. Neurosci. , vol.24 , pp. 10878-10887
    • Hongpaisan, J.1    Winters, C.A.2    Andrews, S.B.3
  • 45
    • 50649122731 scopus 로고    scopus 로고
    • Mitochondrial redox signaling by p66Shc is involved in regulating androgenic growth stimulation of human prostate cancer cells
    • S. Veeramani, T.C. Yuan, F.F. Lin, and M.F. Lin Mitochondrial redox signaling by p66Shc is involved in regulating androgenic growth stimulation of human prostate cancer cells Oncogene 27 2008 5057 5068
    • (2008) Oncogene , vol.27 , pp. 5057-5068
    • Veeramani, S.1    Yuan, T.C.2    Lin, F.F.3    Lin, M.F.4
  • 46
    • 0032699638 scopus 로고    scopus 로고
    • Increased mitochondrial superoxide production in rat liver mitochondria, rat hepatocytes, and HepG2 cells following ethinyl estradiol treatment
    • J. Chen, Y. Li, J.A. Lavigne, M.A. Trush, and J.D. Yager Increased mitochondrial superoxide production in rat liver mitochondria, rat hepatocytes, and HepG2 cells following ethinyl estradiol treatment Toxicol. Sci. 51 1999 224 235
    • (1999) Toxicol. Sci. , vol.51 , pp. 224-235
    • Chen, J.1    Li, Y.2    Lavigne, J.A.3    Trush, M.A.4    Yager, J.D.5
  • 47
    • 9644267549 scopus 로고    scopus 로고
    • Binding of MCF-7 cell mitochondrial proteins and recombinant human estrogen receptors alpha and beta to human mitochondrial DNA estrogen response elements
    • J.Q. Chen, M. Eshete, W.L. Alworth, and J.D. Yager Binding of MCF-7 cell mitochondrial proteins and recombinant human estrogen receptors alpha and beta to human mitochondrial DNA estrogen response elements J. Cell. Biochem. 93 2004 358 373
    • (2004) J. Cell. Biochem. , vol.93 , pp. 358-373
    • Chen, J.Q.1    Eshete, M.2    Alworth, W.L.3    Yager, J.D.4
  • 48
  • 49
    • 33744514462 scopus 로고    scopus 로고
    • Functional estrogen receptors in the mitochondria of breast cancer cells
    • A. Pedram, M. Razandi, D.C. Wallace, and E.R. Levin Functional estrogen receptors in the mitochondria of breast cancer cells Mol. Biol. Cell 17 2006 2125 2137
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2125-2137
    • Pedram, A.1    Razandi, M.2    Wallace, D.C.3    Levin, E.R.4
  • 50
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • K.K. Griendling, D. Sorescu, and M. Ushio-Fukai NAD(P)H oxidase: role in cardiovascular biology and disease Circ. Res. 86 2000 494 501
    • (2000) Circ. Res. , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 52
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • A. Salmeen, and D. Barford Functions and mechanisms of redox regulation of cysteine-based phosphatases Antioxid. Redox Signaling 7 2005 560 577
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 560-577
    • Salmeen, A.1    Barford, D.2
  • 53
    • 19944431403 scopus 로고    scopus 로고
    • Efficacy of a rapamycin analog (CCI-779) and IFN-gamma in tuberous sclerosis mouse models
    • L. Lee, P. Sudentas, B. Donohue, K. Asrican, A. Worku, and V. Walker Efficacy of a rapamycin analog (CCI-779) and IFN-gamma in tuberous sclerosis mouse models Genes Chromosomes Cancer 42 2005 213 227
    • (2005) Genes Chromosomes Cancer , vol.42 , pp. 213-227
    • Lee, L.1    Sudentas, P.2    Donohue, B.3    Asrican, K.4    Worku, A.5    Walker, V.6
  • 54
    • 34147097962 scopus 로고    scopus 로고
    • Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling
    • W.A. Schroder, M. Buck, N. Cloonan, J.F. Hancock, A. Suhrbier, and T. Sculley Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling Cell. Signalling 19 2007 1279 1289
    • (2007) Cell. Signalling , vol.19 , pp. 1279-1289
    • Schroder, W.A.1    Buck, M.2    Cloonan, N.3    Hancock, J.F.4    Suhrbier, A.5    Sculley, T.6
  • 55
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • D. Han, F. Antunes, R. Canali, D. Rettori, and E. Cadenas Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol J. Biol. Chem. 278 2003 5557 5563
    • (2003) J. Biol. Chem. , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5


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