메뉴 건너뛰기




Volumn 72, Issue 18, 2012, Pages 4696-4706

Ectopic ATP synthase blockade suppresses lung adenocarcinoma growth by activating the unfolded protein response

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; ADENOSINE TRIPHOSPHATASE INHIBITOR; CITREOVIRIDIN; INITIATION FACTOR 2ALPHA; PHOSPHOTRANSFERASE; PKR LIKE ENDOPLASMIC RETICULUM KINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84866355221     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-12-0567     Document Type: Article
Times cited : (66)

References (50)
  • 1
    • 0031588861 scopus 로고    scopus 로고
    • Catalytic mechanism of F1-ATPase. BBA
    • Weber J, Senior AE. Catalytic mechanism of F1-ATPase. BBA. Bioenergetics 1997;1319:19-58.
    • (1997) Bioenergetics , vol.1319 , pp. 19-58
    • Weber, J.1    Senior, A.E.2
  • 3
    • 33846012211 scopus 로고    scopus 로고
    • Proteomic analysis of isolated membrane fractions from super invasive cancer cells
    • Dowling P, Meleady P, Dowd A, Henry M, Glynn S, Clynes M. Proteomic analysis of isolated membrane fractions from super invasive cancer cells. Biochim Biophys Acta 2007;1774:93-101.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 93-101
    • Dowling, P.1    Meleady, P.2    Dowd, A.3    Henry, M.4    Glynn, S.5    Clynes, M.6
  • 4
    • 8744293655 scopus 로고    scopus 로고
    • Lipid raft proteome reveals ATP synthase complex in the cell surface
    • Bae TJ, Kim MS, Kim JW, Kim BW, Choo HJ, Lee JW, et al. Lipid raft proteome reveals ATP synthase complex in the cell surface. Proteomics 2004;4:3536-48.
    • (2004) Proteomics , vol.4 , pp. 3536-3548
    • Bae, T.J.1    Kim, M.S.2    Kim, J.W.3    Kim, B.W.4    Choo, H.J.5    Lee, J.W.6
  • 5
    • 0037413638 scopus 로고    scopus 로고
    • Ectopic β-chain of ATP synthase is an apolipoprotein AI receptor in hepatic HDL endocytosis
    • Martinez LO, Jacquet S, Esteve JP, Rolland C, Cabezon E, Champagne E, et al. Ectopic β-chain of ATP synthase is an apolipoprotein AI receptor in hepatic HDL endocytosis. Nature 2003;421:75-9.
    • (2003) Nature , vol.421 , pp. 75-79
    • Martinez, L.O.1    Jacquet, S.2    Esteve, J.P.3    Rolland, C.4    Cabezon, E.5    Champagne, E.6
  • 6
    • 0028270662 scopus 로고
    • A novel ligand in lymphocyte-mediated cytotoxicity: Expression of the beta subunit of H +transporting ATP synthase on the surface of tumor cell lines
    • Das B, Mondragon M, Sadeghian M, Hatcher VB, Norin AJ. A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H +transporting ATP synthase on the surface of tumor cell lines. J Exp Med 1994;180:273-81.
    • (1994) J Exp Med , vol.180 , pp. 273-281
    • Das, B.1    Mondragon, M.2    Sadeghian, M.3    Hatcher, V.B.4    Norin, A.J.5
  • 7
    • 9344233830 scopus 로고    scopus 로고
    • Extracellular ATP is generated by ATP synthase complex in adipocyte lipid rafts
    • Kim BW, Choo HJ, Lee JW, Kim JH, Ko YG. Extracellular ATP is generated by ATP synthase complex in adipocyte lipid rafts. Exp Mol Med 2004;36:476-85.
    • (2004) Exp Mol Med , vol.36 , pp. 476-485
    • Kim, B.W.1    Choo, H.J.2    Lee, J.W.3    Kim, J.H.4    Ko, Y.G.5
  • 8
    • 23844499087 scopus 로고    scopus 로고
    • Human keratinocytes release ATP and utilize three mechanisms for nucleotide interconversion at the cell surface
    • Burrell HE, Wlodarski B, Foster BJ, Buckley KA, Sharpe GR, Quayle JM, et al. Human keratinocytes release ATP and utilize three mechanisms for nucleotide interconversion at the cell surface. J Biol Chem 2005;280:29667-76.
    • (2005) J Biol Chem , vol.280 , pp. 29667-29676
    • Burrell, H.E.1    Wlodarski, B.2    Foster, B.J.3    Buckley, K.A.4    Sharpe, G.R.5    Quayle, J.M.6
  • 9
    • 19944432463 scopus 로고    scopus 로고
    • Tumor recognition following Vγ9Vδ2 T cell receptor interactions with a surface F1-ATPase-related structure and apolipoprotein AI
    • Scotet E, Martinez LO, Grant E, Barbaras R, Jeno P, Guiraud M, et al. Tumor recognition following Vγ9Vδ2 T cell receptor interactions with a surface F1-ATPase-related structure and apolipoprotein AI. Immunity 2005;22:71-80.
    • (2005) Immunity , vol.22 , pp. 71-80
    • Scotet, E.1    Martinez, L.O.2    Grant, E.3    Barbaras, R.4    Jeno, P.5    Guiraud, M.6
  • 10
    • 0344011492 scopus 로고    scopus 로고
    • Possible role of cell surface H+-ATP synthase in the extracellular ATP synthesis and proliferation of human umbilical vein endothelial cells
    • Arakaki N, Nagao T, Niki R, Toyofuku A, Tanaka H, Kuramoto Y, et al. Possible role of cell surface H+-ATP synthase in the extracellular ATP synthesis and proliferation of human umbilical vein endothelial cells. Mol Cancer Res 2003;1:931-9.
    • (2003) Mol Cancer Res , vol.1 , pp. 931-939
    • Arakaki, N.1    Nagao, T.2    Niki, R.3    Toyofuku, A.4    Tanaka, H.5    Kuramoto, Y.6
  • 11
    • 12544257800 scopus 로고    scopus 로고
    • An inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface
    • Burwick NR, Wahl ML, Fang J, Zhong Z, Moser TL, Li B, et al. An inhibitor of the F1 subunit of ATP synthase (IF1) modulates the activity of angiostatin on the endothelial cell surface. J Biol Chem 2005;280:1740-5.
    • (2005) J Biol Chem , vol.280 , pp. 1740-1745
    • Burwick, N.R.1    Wahl, M.L.2    Fang, J.3    Zhong, Z.4    Moser, T.L.5    Li, B.6
  • 12
    • 51949099008 scopus 로고    scopus 로고
    • Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells
    • Schmidt C, Lepsverdize E, Chi S, Das A, Pizzo S, Dityatev A, et al. Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells. Mol Psychiatry 2007;13:953-69.
    • (2007) Mol Psychiatry , vol.13 , pp. 953-969
    • Schmidt, C.1    Lepsverdize, E.2    Chi, S.3    Das, A.4    Pizzo, S.5    Dityatev, A.6
  • 13
    • 34447283107 scopus 로고    scopus 로고
    • +-ATP synthase as a potential molecular target for anti-obesity drugs
    • +-ATP synthase as a potential molecular target for anti-obesity drugs. FEBS Lett 2007;581:3405-9.
    • (2007) FEBS Lett , vol.581 , pp. 3405-3409
    • Arakaki, N.1    Kita, T.2    Shibata, H.3    Higuti, T.4
  • 14
    • 31544443514 scopus 로고    scopus 로고
    • Angiostatin is directly cytotoxic to tumor cells at low extracellular pH: A mechanism dependent on cell surface-associated ATP synthase
    • Chi SL, Pizzo SV. Angiostatin is directly cytotoxic to tumor cells at low extracellular pH: a mechanism dependent on cell surface-associated ATP synthase. Cancer Res 2006;66:875-82.
    • (2006) Cancer Res , vol.66 , pp. 875-882
    • Chi, S.L.1    Pizzo, S.V.2
  • 17
    • 85027910458 scopus 로고    scopus 로고
    • A monoclonal antibody (Mc178-Ab) targeted to the ecto-ATP synthase β-subunit-induced cell apoptosis via a mechanism involving the MAKase and Akt pathways
    • Wang W, Ma Z, Liu Y, He Y, Wang Y, Yang C, et al. A monoclonal antibody (Mc178-Ab) targeted to the ecto-ATP synthase β-subunit-induced cell apoptosis via a mechanism involving the MAKase and Akt pathways. Clin Exp Med 2011:1-10.
    • (2011) Clin Exp Med , pp. 1-10
    • Wang, W.1    Ma, Z.2    Liu, Y.3    He, Y.4    Wang, Y.5    Yang, C.6
  • 19
    • 0019511129 scopus 로고
    • Binding of citreoviridin to the beta subunit of the yeast F1-ATPase
    • Gause EM, Buck MA, Douglas MG. Binding of citreoviridin to the beta subunit of the yeast F1-ATPase. J Biol Chem 1981;256:557-9.
    • (1981) J Biol Chem , vol.256 , pp. 557-559
    • Gause, E.M.1    Buck, M.A.2    Douglas, M.G.3
  • 20
    • 0031226737 scopus 로고    scopus 로고
    • Selection of invasive and metastatic subpopulations from a human lung adenocarcinoma cell line
    • Chu YW, Yang PC, Yang SC, Shyu YC, Hendrix M, Wu R, et al. Selection of invasive and metastatic subpopulations from a human lung adenocarcinoma cell line. Am J Respir Cell Mol Biol 1997;17:353-60.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 353-360
    • Chu, Y.W.1    Yang, P.C.2    Yang, S.C.3    Shyu, Y.C.4    Hendrix, M.5    Wu, R.6
  • 22
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, Calfon M, et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 2003;11:619-33.
    • (2003) Mol Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6
  • 23
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • Haynes CM, Titus EA, Cooper AA. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell 2004;15:767-76.
    • (2004) Mol Cell , vol.15 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 24
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000;101:249-58.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 25
    • 33749579383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers autophagy
    • Yorimitsu T, NairU, Yang Z, Klionsky DJ. Endoplasmic reticulum stress triggers autophagy. J Biol Chem 2006;281:30299-304.
    • (2006) J Biol Chem , vol.281 , pp. 30299-30304
    • Yorimitsu, T.1    Nair, U.2    Yang, Z.3    Klionsky, D.J.4
  • 26
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 2003;11:381-9.
    • (2003) Cell Death Differ , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 27
    • 30344478870 scopus 로고    scopus 로고
    • A global map of p53 transcription-factor binding sites in the human genome
    • Wei CL, Wu Q, Vega VB, Chiu KP, Ng P, Zhang T, et al. A global map of p53 transcription-factor binding sites in the human genome. Cell 2006;124:207-19.
    • (2006) Cell , vol.124 , pp. 207-219
    • Wei, C.L.1    Wu, Q.2    Vega, V.B.3    Chiu, K.P.4    Ng, P.5    Zhang, T.6
  • 28
    • 33846148980 scopus 로고    scopus 로고
    • Outcomes of p53 activation-spoilt for choice
    • Vousden KH. Outcomes of p53 activation-spoilt for choice. J Cell Sci 2006;119:5015-20.
    • (2006) J Cell Sci , vol.119 , pp. 5015-5020
    • Vousden, K.H.1
  • 29
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • Vousden KH, Prives C. Blinded by the light: the growing complexity of p53. Cell 2009;137:413-31.
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 30
    • 79952463019 scopus 로고    scopus 로고
    • Neuronal cell surface ATP synthase mediates synthesis of extracellular ATP and regulation of intracellular pH
    • Xing SL, Yan J, Yu ZH, Zhu CQ. Neuronal cell surface ATP synthase mediates synthesis of extracellular ATP and regulation of intracellular pH. Cell Biol Int 2011;35:81-6.
    • (2011) Cell Biol Int , vol.35 , pp. 81-86
    • Xing, S.L.1    Yan, J.2    Yu, Z.H.3    Zhu, C.Q.4
  • 31
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner M, Pluquet O, Bouchecareilh M, Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res 2007;67:10631-4.
    • (2007) Cancer Res , vol.67 , pp. 10631-10634
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 32
    • 34248571826 scopus 로고    scopus 로고
    • GRP78 induction in cancer: Therapeutic and prognostic implications
    • Lee AS. GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res 2007;67:3496-9.
    • (2007) Cancer Res , vol.67 , pp. 3496-3499
    • Lee, A.S.1
  • 33
    • 33748076770 scopus 로고    scopus 로고
    • GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer
    • Lee E, Nichols P, Spicer D, Groshen S, Yu MC, Lee AS. GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res 2006;66:7849-53.
    • (2006) Cancer Res , vol.66 , pp. 7849-7853
    • Lee, E.1    Nichols, P.2    Spicer, D.3    Groshen, S.4    Yu, M.C.5    Lee, A.S.6
  • 34
    • 33751193479 scopus 로고    scopus 로고
    • Glucose regulated proteins in cancer progression, drug resistance and immunotherapy
    • Fu Y, Lee AS. Glucose regulated proteins in cancer progression, drug resistance and immunotherapy. Cancer Biol Ther 2006;5:741-4.
    • (2006) Cancer Biol Ther , vol.5 , pp. 741-744
    • Fu, Y.1    Lee, A.S.2
  • 35
    • 35448967382 scopus 로고    scopus 로고
    • The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas
    • Pyrko P, Schonthal AH, Hofman FM, Chen TC, Lee AS. The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas. Cancer Res 2007;67:9809-16.
    • (2007) Cancer Res , vol.67 , pp. 9809-9816
    • Pyrko, P.1    Schonthal, A.H.2    Hofman, F.M.3    Chen, T.C.4    Lee, A.S.5
  • 36
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin i
    • Wang Q, Li L, Ye Y. Inhibition of p97-dependent protein degradation by Eeyarestatin I. J Biol Chem 2008;283:7445-54.
    • (2008) J Biol Chem , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 37
    • 70350218853 scopus 로고    scopus 로고
    • Nitrosative stress induced S-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response
    • Townsend DM, Manevich Y, He L, Xiong Y, Bowers RR, Hutchens S, et al. Nitrosative stress induced S-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response. Cancer Res 2009;69:7626-34.
    • (2009) Cancer Res , vol.69 , pp. 7626-7634
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Xiong, Y.4    Bowers, R.R.5    Hutchens, S.6
  • 38
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • Ma Y, Hendershot LM. The role of the unfolded protein response in tumour development: friend or foe? Nat Rev Cancer 2004;4:966-77.
    • (2004) Nat Rev Cancer , vol.4 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 39
    • 79960066445 scopus 로고    scopus 로고
    • Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy
    • Liu Y, Ye Y. Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy. Cell Res 2011;21:867-83.
    • (2011) Cell Res , vol.21 , pp. 867-883
    • Liu, Y.1    Ye, Y.2
  • 40
    • 77951638914 scopus 로고    scopus 로고
    • Basal release of ATP: An autocrine-paracrine mechanism for cell regulation
    • Corriden R, Insel P. Basal release of ATP: an autocrine-paracrine mechanism for cell regulation. Sci Signal 2010;3:re1.
    • (2010) Sci Signal , vol.3
    • Corriden, R.1    Insel, P.2
  • 41
    • 0021288758 scopus 로고
    • Stimulation of P1-purinoceptors by ATP depends partly on its conversion toAMPand adenosine and partly on direct action
    • Moody CJ, Meghji P, Burnstock G. Stimulation of P1-purinoceptors by ATP depends partly on its conversion toAMPand adenosine and partly on direct action. Eur J Pharmacol 1984;97:47-54.
    • (1984) Eur J Pharmacol , vol.97 , pp. 47-54
    • Moody, C.J.1    Meghji, P.2    Burnstock, G.3
  • 42
    • 0034697314 scopus 로고    scopus 로고
    • Cellular release of and response to ATP as key determinants of the set-point of signal transduction pathways
    • Ostrom RS, Gregorian C, Insel PA. Cellular release of and response to ATP as key determinants of the set-point of signal transduction pathways. J Biol Chem 2000;275:11735-9.
    • (2000) J Biol Chem , vol.275 , pp. 11735-11739
    • Ostrom, R.S.1    Gregorian, C.2    Insel, P.A.3
  • 43
    • 84863010960 scopus 로고    scopus 로고
    • Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis
    • Yang Y, Li Z, Mo W, Ambadipudi R, Arnold RJ, Hrncirova P, et al. Human ABCC1 interacts and colocalizes with ATP synthase α, revealed by interactive proteomics analysis. J Proteome Res 2012;11:1364-72.
    • (2012) J Proteome Res , vol.11 , pp. 1364-1372
    • Yang, Y.1    Li, Z.2    Mo, W.3    Ambadipudi, R.4    Arnold, R.J.5    Hrncirova, P.6
  • 45
    • 34250304605 scopus 로고    scopus 로고
    • Angiostatin-like activity of a monoclonal antibody to the catalytic subunit of F1F0 ATP synthase
    • Chi SL, Wahl ML, Mowery YM, Shan S, Mukhopadhyay S, Hilderbrand SC, et al. Angiostatin-like activity of a monoclonal antibody to the catalytic subunit of F1F0 ATP synthase. Cancer Res 2007;67:4716-24.
    • (2007) Cancer Res , vol.67 , pp. 4716-4724
    • Chi, S.L.1    Wahl, M.L.2    Mowery, Y.M.3    Shan, S.4    Mukhopadhyay, S.5    Hilderbrand, S.C.6
  • 46
    • 79960427057 scopus 로고    scopus 로고
    • Selective killing of cancer cells by a small molecule targeting the stress response to ROS
    • Raj L, Ide T, Gurkar AU, Foley M, Schenone M, Li X, et al. Selective killing of cancer cells by a small molecule targeting the stress response to ROS. Nature 2011;475:231-4.
    • (2011) Nature , vol.475 , pp. 231-234
    • Raj, L.1    Ide, T.2    Gurkar, A.U.3    Foley, M.4    Schenone, M.5    Li, X.6
  • 47
    • 1942453308 scopus 로고    scopus 로고
    • The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants
    • Mattiazzi M, Vijayvergiya C, Gajewski CD, DeVivo DC, Lenaz G, Wiedmann M, et al. The mtDNA T8993G (NARP) mutation results in an impairment of oxidative phosphorylation that can be improved by antioxidants. Hum Mol Genet 2004;13:869-79.
    • (2004) Hum Mol Genet , vol.13 , pp. 869-879
    • Mattiazzi, M.1    Vijayvergiya, C.2    Gajewski, C.D.3    DeVivo, D.C.4    Lenaz, G.5    Wiedmann, M.6
  • 48
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007;9:2277-93.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 50
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Hoyer-Hansen M, Jaattela M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 2007;14:1576-82.
    • (2007) Cell Death Differ , vol.14 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.