메뉴 건너뛰기




Volumn 12, Issue 4, 2010, Pages 346-356

The eIF4E/eIF4G interaction inhibitor 4EGI-1 augments trail-mediated apoptosis through c-FLIP down-regulation and DR5 induction independent of inhibition of cap-dependent protein translation

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CYCLIN D1; DEATH RECEPTOR 5; FLICE INHIBITORY PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; INITIATION FACTOR 4E; INITIATION FACTOR 4G; SMALL INTERFERING RNA; SMALL MOLECULE 4EGI 1; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG;

EID: 77951671938     PISSN: 15228002     EISSN: 14765586     Source Type: Journal    
DOI: 10.1593/neo.10144     Document Type: Article
Times cited : (85)

References (55)
  • 1
    • 2542506326 scopus 로고    scopus 로고
    • The mRNA cap-binding protein eIF4E in post-transcriptional gene expression
    • von der Haar T, Gross JD, Wagner G, and McCarthy JE (2004). The mRNA cap-binding protein eIF4E in post-transcriptional gene expression. Nat Struct Mol Biol 11, 503-511.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 503-511
    • von der Haar, T.1    Gross, J.D.2    Wagner, G.3    McCarthy, J.E.4
  • 2
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD and Sonenberg N (2005). Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433, 477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 4
    • 38849180436 scopus 로고    scopus 로고
    • Targeting the eukaryotic translation initiation factor 4E for cancer therapy
    • Graff JR, Konicek BW, Carter JH, and Marcusson EG (2008). Targeting the eukaryotic translation initiation factor 4E for cancer therapy. Cancer Res 68, 631-634.
    • (2008) Cancer Res , vol.68 , pp. 631-634
    • Graff, J.R.1    Konicek, B.W.2    Carter, J.H.3    Marcusson, E.G.4
  • 5
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • De Benedetti A and Graff JR (2004). eIF-4E expression and its role in malignancies and metastases. Oncogene 23, 3189-3199.
    • (2004) Oncogene , vol.23 , pp. 3189-3199
    • de Benedetti, A.1    Graff, J.R.2
  • 7
    • 0033006919 scopus 로고    scopus 로고
    • eIF4E activity is regulated at multiple levels
    • Raught B and Gingras AC (1999). eIF4E activity is regulated at multiple levels. Int J Biochem Cell Biol 31, 43-57.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 43-57
    • Raught, B.1    Gingras, A.C.2
  • 8
    • 35348954728 scopus 로고    scopus 로고
    • Translational control: A target for cancer therapy
    • Thumma SC and Kratzke RA (2007). Translational control: a target for cancer therapy. Cancer Lett 258, 1-8.
    • (2007) Cancer Lett , vol.258 , pp. 1-8
    • Thumma, S.C.1    Kratzke, R.A.2
  • 12
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • Ruggero D, Montanaro L, Ma L, Xu W, Londei P, Cordon-Cardo C, and Pandolfi PP (2004). The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat Med 10, 484-486.
    • (2004) Nat Med , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3    Xu, W.4    Londei, P.5    Cordon-Cardo, C.6    Pandolfi, P.P.7
  • 14
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau D, Gingras AC, Pause A, and Sonenberg N (1996). The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 13, 2415-2420.
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 15
    • 0036195727 scopus 로고    scopus 로고
    • Translational control of cell fate: Availability of phosphorylation sites on translational repressor 4E-BP1 governs its proapoptotic potency
    • Li S, Sonenberg N, Gingras AC, Peterson M, Avdulov S, Polunovsky VA, and Bitterman PB (2002). Translational control of cell fate: availability of phosphorylation sites on translational repressor 4E-BP1 governs its proapoptotic potency. Mol Cell Biol 22, 2853-2861.
    • (2002) Mol Cell Biol , vol.22 , pp. 2853-2861
    • Li, S.1    Sonenberg, N.2    Gingras, A.C.3    Peterson, M.4    Avdulov, S.5    Polunovsky, V.A.6    Bitterman, P.B.7
  • 17
    • 0344063370 scopus 로고    scopus 로고
    • Will mTOR inhibitors make it as cancer drugs?
    • Sawyers CL (2003). Will mTOR inhibitors make it as cancer drugs? Cancer Cell 4,343-348.
    • (2003) Cancer Cell , vol.4 , pp. 343-348
    • Sawyers, C.L.1
  • 18
    • 53849125004 scopus 로고    scopus 로고
    • mTORC1 inhibitors: Is temsirolimus in renal cancer telling us how they really work?
    • Le Tourneau C, Faivre S, Serova M, and Raymond E (2008). mTORC1 inhibitors: is temsirolimus in renal cancer telling us how they really work? Br J Cancer 99,1197-1203.
    • (2008) Br J Cancer , vol.99 , pp. 1197-1203
    • le Tourneau, C.1    Faivre, S.2    Serova, M.3    Raymond, E.4
  • 19
    • 34250619165 scopus 로고    scopus 로고
    • The mammalian target of rapamycin signaling pathway: Twists and turns in the road to cancer therapy
    • Abraham RT and Gibbons JJ (2007). The mammalian target of rapamycin signaling pathway: twists and turns in the road to cancer therapy. Clin Cancer Res 13,3109-3114.
    • (2007) Clin Cancer Res , vol.13 , pp. 3109-3114
    • Abraham, R.T.1    Gibbons, J.J.2
  • 20
    • 3342894130 scopus 로고    scopus 로고
    • Targeting death receptors in cancer with Apo2L/TRAIL
    • Kelley SK and Ashkenazi A (2004). Targeting death receptors in cancer with Apo2L/TRAIL. Curr Opin Pharmacol 4, 333-339.
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 333-339
    • Kelley, S.K.1    Ashkenazi, A.2
  • 21
    • 62449168519 scopus 로고    scopus 로고
    • TRAIL agonists on clinical trials for cancer therapy: The promises and the challenges
    • Bellail AC, Qi L, Mulligan P, Chhabra V, and Hao C (2009). TRAIL agonists on clinical trials for cancer therapy: the promises and the challenges. Rev Recent Clin Trials 4, 34-41.
    • (2009) Rev Recent Clin Trials , vol.4 , pp. 34-41
    • Bellail, A.C.1    Qi, L.2    Mulligan, P.3    Chhabra, V.4    Hao, C.5
  • 22
    • 33644832724 scopus 로고    scopus 로고
    • Targeted induction of apoptosis in cancer management: The emerging role of tumor necrosis factor-related apoptosis-inducing ligand receptor activating agents
    • Rowinsky EK (2005). Targeted induction of apoptosis in cancer management: the emerging role of tumor necrosis factor-related apoptosis-inducing ligand receptor activating agents. J Clin Oncol 23, 9394-9407.
    • (2005) J Clin Oncol , vol.23 , pp. 9394-9407
    • Rowinsky, E.K.1
  • 23
    • 44749085513 scopus 로고    scopus 로고
    • Targeting the extrinsic apoptosis pathway in cancer
    • Ashkenazi A (2008). Targeting the extrinsic apoptosis pathway in cancer. Cytokine Growth Factor Rev 19, 325-331.
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 325-331
    • Ashkenazi, A.1
  • 24
    • 34249663310 scopus 로고    scopus 로고
    • Targeting death- inducing receptors in cancer therapy
    • Takeda K, Stagg J, Yagita H, Okumura K, and Smyth MJ (2007). Targeting death- inducing receptors in cancer therapy. Oncogene 26, 3745-3757.
    • (2007) Oncogene , vol.26 , pp. 3745-3757
    • Takeda, K.1    Stagg, J.2    Yagita, H.3    Okumura, K.4    Smyth, M.J.5
  • 25
    • 14644437742 scopus 로고    scopus 로고
    • Mechanisms of resistance to TRAIL-induced apoptosis in cancer
    • Zhang L and Fang B (2005). Mechanisms of resistance to TRAIL-induced apoptosis in cancer. Cancer Gene Ther 12, 228-237.
    • (2005) Cancer Gene Ther , vol.12 , pp. 228-237
    • Zhang, L.1    Fang, B.2
  • 26
    • 42549124692 scopus 로고    scopus 로고
    • Modulation of death receptors by cancer therapeutic agents
    • Elrod HA and Sun SY (2007). Modulation of death receptors by cancer therapeutic agents. Cancer Biol Ther 7, 163-173.
    • (2007) Cancer Biol Ther , vol.7 , pp. 163-173
    • Elrod, H.A.1    Sun, S.Y.2
  • 27
    • 0035192884 scopus 로고    scopus 로고
    • FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis
    • Krueger A, Baumann S, Krammer PH, and Kirchhoff S (2001). FLICE-inhibitory proteins: regulators of death receptor-mediated apoptosis. Mol Cell Biol 21, 8247-8254.
    • (2001) Mol Cell Biol , vol.21 , pp. 8247-8254
    • Krueger, A.1    Baumann, S.2    Krammer, P.H.3    Kirchhoff, S.4
  • 28
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • Budd RC, Yeh WC, and Tschopp J (2006). cFLIP regulation of lymphocyte activation and development. Nat Rev Immunol 6, 196-204.
    • (2006) Nat Rev Immunol , vol.6 , pp. 196-204
    • Budd, R.C.1    Yeh, W.C.2    Tschopp, J.3
  • 29
    • 2342451904 scopus 로고    scopus 로고
    • Targeting the FLICE inhibitory protein (FLIP) in cancer therapy
    • Wajant H (2003). Targeting the FLICE inhibitory protein (FLIP) in cancer therapy. Mol Interv 3, 124-127.
    • (2003) Mol Interv , vol.3 , pp. 124-127
    • Wajant, H.1
  • 30
    • 19544382901 scopus 로고    scopus 로고
    • The caspase-8 modulator c-FLIP
    • Kataoka T (2005). The caspase-8 modulator c-FLIP. Crit Rev Immunol 25, 31-58.
    • (2005) Crit Rev Immunol , vol.25 , pp. 31-58
    • Kataoka, T.1
  • 31
    • 0037151079 scopus 로고    scopus 로고
    • An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis
    • Kim Y, Suh N, Sporn M, and Reed JC (2002). An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis. J Biol Chem 277, 22320-22329.
    • (2002) J Biol Chem , vol.277 , pp. 22320-22329
    • Kim, Y.1    Suh, N.2    Sporn, M.3    Reed, J.C.4
  • 33
    • 32044447161 scopus 로고    scopus 로고
    • 3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, Kamata H, Solinas G, Luo JL, Maeda S, Venuprasad K, Liu YC, and Karin M (2006). The E3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover. Cell 124, 601-613.
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1    Kamata, H.2    Solinas, G.3    Luo, J.L.4    Maeda, S.5    Venuprasad, K.6    Liu, Y.C.7    Karin, M.8
  • 34
    • 0344393606 scopus 로고    scopus 로고
    • Up-regulation of FLIP in cisplatin-selected HeLa cells causes cross-resistance to CD95/Fas death signalling
    • Kamarajan P, Sun NK, and Chao CC (2003). Up-regulation of FLIP in cisplatin-selected HeLa cells causes cross-resistance to CD95/Fas death signalling. Biochem J 376,253-260.
    • (2003) Biochem J , vol.376 , pp. 253-260
    • Kamarajan, P.1    Sun, N.K.2    Chao, C.C.3
  • 36
    • 4844220794 scopus 로고    scopus 로고
    • Possible role of FLICE-like inhibitory protein (FLIP) in chemoresistant ovarian cancer cells in vitro
    • Abedini MR, Qiu Q, Yan X, and Tsang BK (2004). Possible role of FLICE-like inhibitory protein (FLIP) in chemoresistant ovarian cancer cells in vitro. Oncogene 23,6997-7004.
    • (2004) Oncogene , vol.23 , pp. 6997-7004
    • Abedini, M.R.1    Qiu, Q.2    Yan, X.3    Tsang, B.K.4
  • 40
    • 51049115354 scopus 로고    scopus 로고
    • The natural product honokiol preferentially inhibits cellular FLICE- inhibitory protein and augments death receptor-induced apoptosis
    • Raja SM, Chen S, Yue P, Acker TM, Lefkove B, Arbiser JL, Khuri FR, and Sun SY (2008). The natural product honokiol preferentially inhibits cellular FLICE- inhibitory protein and augments death receptor-induced apoptosis. Mol Cancer Ther 7, 2212-2223.
    • (2008) Mol Cancer Ther , vol.7 , pp. 2212-2223
    • Raja, S.M.1    Chen, S.2    Yue, P.3    Acker, T.M.4    Lefkove, B.5    Arbiser, J.L.6    Khuri, F.R.7    Sun, S.Y.8
  • 41
    • 0030731915 scopus 로고    scopus 로고
    • Differential effects of synthetic nuclear retinoid receptor-selective retinoids on the growth of human non- small cell lung carcinoma cells
    • Sun SY, Yue P, Dawson MI, Shroot B, Michel S, Lamph WW, Heyman RA, Teng M, Chandraratna RA, Shudo K, et al. (1997). Differential effects of synthetic nuclear retinoid receptor-selective retinoids on the growth of human non- small cell lung carcinoma cells. Cancer Res 57, 4931-4939.
    • (1997) Cancer Res , vol.57 , pp. 4931-4939
    • Sun, S.Y.1    Yue, P.2    Dawson, M.I.3    Shroot, B.4    Michel, S.5    Lamph, W.W.6    Heyman, R.A.7    Teng, M.8    Chandraratna, R.A.9    Shudo, K.10
  • 42
    • 0033535608 scopus 로고    scopus 로고
    • Mechanisms of apoptosis induced by the synthetic retinoid CD437 in human non-small cell lung carcinoma cells
    • Sun SY, Yue P, Wu GS, El-Deiry WS, Shroot B, Hong WK, and Lotan R (1999). Mechanisms of apoptosis induced by the synthetic retinoid CD437 in human non-small cell lung carcinoma cells. Oncogene 18, 2357-2365.
    • (1999) Oncogene , vol.18 , pp. 2357-2365
    • Sun, S.Y.1    Yue, P.2    Wu, G.S.3    El-Deiry, W.S.4    Shroot, B.5    Hong, W.K.6    Lotan, R.7
  • 43
    • 10644257370 scopus 로고    scopus 로고
    • Death receptor regulation and celecoxib-induced apoptosis in human lung cancer cells
    • Liu X, Yue P, Zhou Z, Khuri FR, and Sun SY (2004). Death receptor regulation and celecoxib-induced apoptosis in human lung cancer cells. J Natl Cancer Inst 96,1769-1780.
    • (2004) J Natl Cancer Inst , vol.96 , pp. 1769-1780
    • Liu, X.1    Yue, P.2    Zhou, Z.3    Khuri, F.R.4    Sun, S.Y.5
  • 44
    • 34547112563 scopus 로고    scopus 로고
    • The farnesyl- transferase inhibitor lonafarnib induces CCAAT/enhancer-binding protein homologous protein-dependent expression of death receptor 5, leading to induction of apoptosis in human cancer cells
    • Sun SY, Liu X, Zou W, Yue P, Marcus AI, and Khuri FR (2007). The farnesyl- transferase inhibitor lonafarnib induces CCAAT/enhancer-binding protein homologous protein-dependent expression of death receptor 5, leading to induction of apoptosis in human cancer cells. J Biol Chem 282, 18800-18809.
    • (2007) J Biol Chem , vol.282 , pp. 18800-18809
    • Sun, S.Y.1    Liu, X.2    Zou, W.3    Yue, P.4    Marcus, A.I.5    Khuri, F.R.6
  • 45
    • 38449110890 scopus 로고    scopus 로고
    • Methods for studying signal-dependent regulation of translation factor activity
    • Wang X and Proud CG (2007). Methods for studying signal-dependent regulation of translation factor activity. Methods Enzymol 431, 113-142.
    • (2007) Methods Enzymol , vol.431 , pp. 113-142
    • Wang, X.1    Proud, C.G.2
  • 46
    • 18844429239 scopus 로고    scopus 로고
    • Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells
    • Chen C, Sun X, Ran Q, Wilkinson KD, Murphy TJ, Simons JW, and Dong JT (2005). Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells. Oncogene 24, 3319-3327.
    • (2005) Oncogene , vol.24 , pp. 3319-3327
    • Chen, C.1    Sun, X.2    Ran, Q.3    Wilkinson, K.D.4    Murphy, T.J.5    Simons, J.W.6    Dong, J.T.7
  • 47
    • 27944483724 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation
    • Svitkin YV, Herdy B, Costa-Mattioli M, Gingras AC, Raught B, and Sonenberg N (2005). Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation. Mol Cell Biol 25, 10556-10565.
    • (2005) Mol Cell Biol , vol.25 , pp. 10556-10565
    • Svitkin, Y.V.1    Herdy, B.2    Costa-Mattioli, M.3    Gingras, A.C.4    Raught, B.5    Sonenberg, N.6
  • 48
    • 48549103399 scopus 로고    scopus 로고
    • CAAT/enhancer binding protein homologous protein- dependent death receptor 5 induction is a major component of SHetA2-induced apoptosis in lung cancer cells
    • Lin YD, Chen S, Yue P, Zou W, Benbrook D, Liu S, Le TC, Berlin KD, Khuri FR, and Sun SY (2008). CAAT/enhancer binding protein homologous protein- dependent death receptor 5 induction is a major component of SHetA2-induced apoptosis in lung cancer cells. Cancer Res 68, 5335-5344.
    • (2008) Cancer Res , vol.68 , pp. 5335-5344
    • Lin, Y.D.1    Chen, S.2    Yue, P.3    Zou, W.4    Benbrook, D.5    Liu, S.6    Le, T.C.7    Berlin, K.D.8    Khuri, F.R.9    Sun, S.Y.10
  • 49
    • 33747819801 scopus 로고    scopus 로고
    • mTOR and cancer: Insights into a complex relationship
    • Sabatini DM (2006). mTOR and cancer: insights into a complex relationship. Nat Rev Cancer 6, 729-734.
    • (2006) Nat Rev Cancer , vol.6 , pp. 729-734
    • Sabatini, D.M.1
  • 50
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi H and Wang HG (2004). CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem 279, 45495-45502.
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 51
    • 22244472001 scopus 로고    scopus 로고
    • Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells
    • Shiraishi T, Yoshida T, Nakata S, Horinaka M, Wakada M, Mizutani Y, Miki T, and Sakai T (2005). Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells. Cancer Res 65, 6364-6370.
    • (2005) Cancer Res , vol.65 , pp. 6364-6370
    • Shiraishi, T.1    Yoshida, T.2    Nakata, S.3    Horinaka, M.4    Wakada, M.5    Mizutani, Y.6    Miki, T.7    Sakai, T.8
  • 52
    • 26444560914 scopus 로고    scopus 로고
    • mTOR controls FLIPS translation and TRAIL sensitivity in glioblastoma multiforme cells
    • Panner A, James CD, Berger MS, and Pieper RO (2005). mTOR controls FLIPS translation and TRAIL sensitivity in glioblastoma multiforme cells. Mol Cell Biol 25,8809-8823.
    • (2005) Mol Cell Biol , vol.25 , pp. 8809-8823
    • Panner, A.1    James, C.D.2    Berger, M.S.3    Pieper, R.O.4
  • 53
    • 51049112961 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibition broadly sensitizes glioblastoma cells to death receptor- and drug-induced apoptosis
    • Opel D, Westhoff MA, Bender A, Braun V, Debatin KM, and Fulda S (2008). Phosphatidylinositol 3-kinase inhibition broadly sensitizes glioblastoma cells to death receptor- and drug-induced apoptosis. Cancer Res 68, 6271-6280.
    • (2008) Cancer Res , vol.68 , pp. 6271-6280
    • Opel, D.1    Westhoff, M.A.2    Bender, A.3    Braun, V.4    Debatin, K.M.5    Fulda, S.6
  • 54
    • 21344453520 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces death receptor 5 through CCAAT/enhancer-binding protein homologous protein
    • Yoshida T, Shiraishi T, Nakata S, Horinaka M, Wakada M, Mizutani Y, Miki T, and Sakai T (2005). Proteasome inhibitor MG132 induces death receptor 5 through CCAAT/enhancer-binding protein homologous protein. Cancer Res 65, 5662-5667.
    • (2005) Cancer Res , vol.65 , pp. 5662-5667
    • Yoshida, T.1    Shiraishi, T.2    Nakata, S.3    Horinaka, M.4    Wakada, M.5    Mizutani, Y.6    Miki, T.7    Sakai, T.8
  • 55
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S and Mori M (2004). Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 11, 381-389.
    • (2004) Cell Death Differ , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.