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Volumn 70, Issue 11, 2010, Pages 4318-4326

Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; EPOXOMICIN; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 45; ML 912; MLN 2238; MLN 4924; MYC PROTEIN; PROTEASOME INHIBITOR; PROTEIN NOXA; PROTEIN P53; PUTRESCINE; SALINOSPORAMIDE A; SMALL INTERFERING RNA; SPERMIDINE; THAPSIGARGIN; UNCLASSIFIED DRUG;

EID: 77953163141     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-09-4428     Document Type: Article
Times cited : (83)

References (35)
  • 1
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • Orlowski RZ, Kuhn DJ. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res 2008;14:1649-1657
    • (2008) Clin Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 2
    • 53049083867 scopus 로고    scopus 로고
    • Mechanisms of proteasome inhibitor action and resistance in cancer
    • McConkey DJ, Zhu K. Mechanisms of proteasome inhibitor action and resistance in cancer. Drug Resist Updat 2008;11:164-179
    • (2008) Drug Resist Updat , vol.11 , pp. 164-179
    • McConkey, D.J.1    Zhu, K.2
  • 4
    • 33751189389 scopus 로고    scopus 로고
    • Proteasome inhibitor induces apoptosis through induction of endoplasmic reticulum stress
    • Fribley A, Wang CY. Proteasome inhibitor induces apoptosis through induction of endoplasmic reticulum stress. Cancer Biol Ther 2006;5: 745-748
    • (2006) Cancer Biol Ther , vol.5 , pp. 745-748
    • Fribley, A.1    Wang, C.Y.2
  • 5
  • 6
    • 34147198467 scopus 로고    scopus 로고
    • Synthetic lethal screen identification of chemosensitizer loci in cancer cells
    • Whitehurst AW, Bodemann BO, Cardenas J, et al. Synthetic lethal screen identification of chemosensitizer loci in cancer cells. Nature 2007;446:815-819
    • (2007) Nature , vol.446 , pp. 815-819
    • Whitehurst, A.W.1    Bodemann, B.O.2    Cardenas, J.3
  • 7
    • 58049208190 scopus 로고    scopus 로고
    • Genome-wide loss-of-function screen reveals an important role for the proteasome in HDAC inhibitor-induced apoptosis
    • Fotheringham S, Epping MT, Stimson L, et al. Genome-wide loss-of-function screen reveals an important role for the proteasome in HDAC inhibitor-induced apoptosis. Cancer Cell 2009;15:57-66.
    • (2009) Cancer Cell , vol.15 , pp. 57-66
    • Fotheringham, S.1    Epping, M.T.2    Stimson, L.3
  • 8
    • 70350010207 scopus 로고    scopus 로고
    • An intermittent live cell imaging screen for siRNA enhancers and suppressors of a kinesin-5 inhibitor
    • Tsui M, Xie T, Orth JD, et al. An intermittent live cell imaging screen for siRNA enhancers and suppressors of a kinesin-5 inhibitor. PLoS One 2009;4:e7339.
    • (2009) PLoS One , vol.4
    • Tsui, M.1    Xie, T.2    Orth, J.D.3
  • 9
    • 2942692143 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer
    • Papandreou CN, Daliani DD, Nix D, et al. Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer. J Clin Oncol 2004;22:2108-2121
    • (2004) J Clin Oncol , vol.22 , pp. 2108-2121
    • Papandreou, C.N.1    Daliani, D.D.2    Nix, D.3
  • 10
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • Crawford LJ, Walker B, Ovaa H, et al. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res 2006;66:6379-6386
    • (2006) Cancer Res , vol.66 , pp. 6379-6386
    • Crawford, L.J.1    Walker, B.2    Ovaa, H.3
  • 11
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • Nawrocki ST, Carew JS, Dunner K, Jr., et al. Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res 2005;65: 11510-11519
    • (2005) Cancer Res , vol.65 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner Jr., K.3
  • 12
    • 35948986297 scopus 로고    scopus 로고
    • Absence of Bax switched MG132-induced apoptosis to non-apoptotic cell death that could be suppressed by transcriptional or translational inhibition
    • Ding WX, Ni HM, Yin XM. Absence of Bax switched MG132-induced apoptosis to non-apoptotic cell death that could be suppressed by transcriptional or translational inhibition. Apoptosis 2007;12: 2233-2244
    • (2007) Apoptosis , vol.12 , pp. 2233-2244
    • Ding, W.X.1    Ni, H.M.2    Yin, X.M.3
  • 13
    • 0035868428 scopus 로고    scopus 로고
    • A complete map of the human ribosomal protein genes: Assignment of 80 genes to the cytogenetic map and implications for human disorders
    • DOI 10.1006/geno.2000.6470
    • Uechi T, Tanaka T, Kenmochi N. A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders. Genomics 2001;72: 223-230 (Pubitemid 32281523)
    • (2001) Genomics , vol.72 , Issue.3 , pp. 223-230
    • Uechi, T.1    Tanaka, T.2    Kenmochi, N.3
  • 14
    • 0344629427 scopus 로고    scopus 로고
    • Ubiquitin depletion as a key mediator of toxicity by translational inhibitors
    • Hanna J, Leggett DS, Finley D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol Cell Biol 2003;23:9251-9261
    • (2003) Mol Cell Biol , vol.23 , pp. 9251-9261
    • Hanna, J.1    Leggett, D.S.2    Finley, D.3
  • 15
    • 0037134480 scopus 로고    scopus 로고
    • 4E-binding proteins, the suppressors of eukaryotic initiation factor 4E, are down-regulated in cells with acquired or intrinsic resistance to rapamycin
    • Dilling MB, Germain GS, Dudkin L, et al. 4E-binding proteins, the suppressors of eukaryotic initiation factor 4E, are down-regulated in cells with acquired or intrinsic resistance to rapamycin. J Biol Chem 2002;277:13907-13917
    • (2002) J Biol Chem , vol.277 , pp. 13907-13917
    • Dilling, M.B.1    Germain, G.S.2    Dudkin, L.3
  • 16
    • 67650445202 scopus 로고    scopus 로고
    • Repression of protein translation and mTOR signaling by proteasome inhibitor in colon cancer cells
    • Wu WK, Volta V, Cho CH, et al. Repression of protein translation and mTOR signaling by proteasome inhibitor in colon cancer cells. Biochem Biophys Res Commun 2009;386:598-601.
    • (2009) Biochem Biophys Res Commun , vol.386 , pp. 598-601
    • Wu, W.K.1    Volta, V.2    Cho, C.H.3
  • 17
    • 54549089738 scopus 로고    scopus 로고
    • Hypoxia signalling through mTOR and the unfolded protein response in cancer
    • Wouters BG, Koritzinsky M. Hypoxia signalling through mTOR and the unfolded protein response in cancer. Nat Rev Cancer 2008;8: 851-864
    • (2008) Nat Rev Cancer , vol.8 , pp. 851-864
    • Wouters, B.G.1    Koritzinsky, M.2
  • 18
    • 60549106248 scopus 로고    scopus 로고
    • Inhibition of eIF2α dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy
    • Schewe DM, Aguirre-Ghiso JA. Inhibition of eIF2α dephosphorylation maximizes bortezomib efficiency and eliminates quiescent multiple myeloma cells surviving proteasome inhibitor therapy. Cancer Res 2009;69:1545-1552
    • (2009) Cancer Res , vol.69 , pp. 1545-1552
    • Schewe, D.M.1    Aguirre-Ghiso, J.A.2
  • 19
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng EA, Carlson LM, Gutman DM, et al. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 2006;107:4907-4916
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3
  • 20
    • 77953147974 scopus 로고    scopus 로고
    • Inhibition of mTORC1 activity by REDD1 induction in myeloma cells resistant to bortezomib cytotoxicity
    • Decaux O, Clement M, Magrangeas F, et al. Inhibition of mTORC1 activity by REDD1 induction in myeloma cells resistant to bortezomib cytotoxicity. Cancer Sci 2009;101:889-897
    • (2009) Cancer Sci , vol.101 , pp. 889-897
    • Decaux, O.1    Clement, M.2    Magrangeas, F.3
  • 21
    • 37649000950 scopus 로고    scopus 로고
    • Tumor cell-selective regulation of NOXA by c-MYC in response to proteasome inhibition
    • Nikiforov MA, Riblett M, Tang WH, et al. Tumor cell-selective regulation of NOXA by c-MYC in response to proteasome inhibition. Proc Natl Acad Sci U S A 2007;104:19488-19493
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19488-19493
    • Nikiforov, M.A.1    Riblett, M.2    Tang, W.H.3
  • 22
    • 23144464363 scopus 로고    scopus 로고
    • Transcriptional regulation and transformation by Myc proteins
    • Adhikary S, Eilers M. Transcriptional regulation and transformation by Myc proteins. Nat Rev Mol Cell Biol 2005;6:635-645
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 635-645
    • Adhikary, S.1    Eilers, M.2
  • 23
    • 2342645571 scopus 로고    scopus 로고
    • The role of c-myc in regulation of translation initiation
    • Schmidt EV. The role of c-myc in regulation of translation initiation. Oncogene 2004;23:3217-3221
    • (2004) Oncogene , vol.23 , pp. 3217-3221
    • Schmidt, E.V.1
  • 24
    • 36849048654 scopus 로고    scopus 로고
    • Role of hypusinated eukaryotic translation initiation factor 5A in polyamine depletion-induced cytostasis
    • Hyvönen MT, Keinänen TA, Cerrada-Gimenez M, et al. Role of hypusinated eukaryotic translation initiation factor 5A in polyamine depletion-induced cytostasis. J Biol Chem 2007;282:34700-34706
    • (2007) J Biol Chem , vol.282 , pp. 34700-34706
    • Hyvönen, M.T.1    Keinänen, T.A.2    Cerrada-Gimenez, M.3
  • 25
    • 0042066415 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitin-proteasome effects: Insight into the function of eukaryotic initiation factor 5A
    • Jin BF, He K, Wang HX, et al. Proteomic analysis of ubiquitin-proteasome effects: insight into the function of eukaryotic initiation factor 5A. Oncogene 2003;22:4819-4830
    • (2003) Oncogene , vol.22 , pp. 4819-4830
    • Jin, B.F.1    He, K.2    Wang, H.X.3
  • 26
    • 0031469938 scopus 로고    scopus 로고
    • Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (eIF-5A) and induces apoptosis
    • Tome ME, Fiser SM, Payne CM, Gerner EW. Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (eIF-5A) and induces apoptosis. Biochem J 1997;328: 847-854
    • (1997) Biochem J , vol.328 , pp. 847-854
    • Tome, M.E.1    Fiser, S.M.2    Payne, C.M.3    Gerner, E.W.4
  • 28
    • 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, et al. The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis. Nat Med 2004;10:484-486
    • (2004) Nat Med , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3
  • 29
    • 34547628200 scopus 로고    scopus 로고
    • Proteasome function is required for DNA damage response and Fanconi anemia pathway activation
    • Jacquemont C, Taniguchi T. Proteasome function is required for DNA damage response and Fanconi anemia pathway activation. Cancer Res 2007;67:7395-7405
    • (2007) Cancer Res , vol.67 , pp. 7395-7405
    • Jacquemont, C.1    Taniguchi, T.2
  • 30
    • 34548807121 scopus 로고    scopus 로고
    • Inhibitors of the proteasome suppress homologous DNA recombination in mammalian cells
    • Murakawa Y, Sonoda E, Barber LJ, et al. Inhibitors of the proteasome suppress homologous DNA recombination in mammalian cells. Cancer Res 2007;67:8536-8543
    • (2007) Cancer Res , vol.67 , pp. 8536-8543
    • Murakawa, Y.1    Sonoda, E.2    Barber, L.J.3
  • 31
    • 57649130600 scopus 로고    scopus 로고
    • Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation
    • Shi W, Ma Z, Willers H, et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J Biol Chem 2008; 283:31608-31616
    • (2008) J Biol Chem , vol.283 , pp. 31608-31616
    • Shi, W.1    Ma, Z.2    Willers, H.3
  • 32
    • 50449086728 scopus 로고    scopus 로고
    • Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma
    • San Miguel JF, Schlag R, Khuageva NK, et al. Bortezomib plus melphalan and prednisone for initial treatment of multiple myeloma. N Engl J Med 2008;359:906-917
    • (2008) N Engl J Med , vol.359 , pp. 906-917
    • San Miguel, J.F.1    Schlag, R.2    Khuageva, N.K.3
  • 33
    • 22144466584 scopus 로고    scopus 로고
    • The FA/BRCA pathway is involved in melphalan-induced DNA interstrand cross-link repair and accounts for melphalan resistance in multiple myeloma cells
    • Chen Q, Van der Sluis PC, Boulware D, Hazlehurst LA, Dalton WS. The FA/BRCA pathway is involved in melphalan-induced DNA interstrand cross-link repair and accounts for melphalan resistance in multiple myeloma cells. Blood 2005;106:698-705.
    • (2005) Blood , vol.106 , pp. 698-705
    • Chen, Q.1    Van Der Sluis, P.C.2    Boulware, D.3    Hazlehurst, L.A.4    Dalton, W.S.5
  • 34
    • 0035802230 scopus 로고    scopus 로고
    • In vitro evidence for homologous recombinational repair in resistance to melphalan
    • Wang ZM, Chen ZP, Xu ZY, et al. In vitro evidence for homologous recombinational repair in resistance to melphalan. J Natl Cancer Inst 2001;93:1473-1478
    • (2001) J Natl Cancer Inst , vol.93 , pp. 1473-1478
    • Wang, Z.M.1    Chen, Z.P.2    Xu, Z.Y.3
  • 35
    • 73649119600 scopus 로고    scopus 로고
    • Targeting the Fanconi anemia/BRCA pathway circumvents drug resistance in multiple myeloma
    • Yarde DN, Oliveira V, Mathews L, et al. Targeting the Fanconi anemia/BRCA pathway circumvents drug resistance in multiple myeloma. Cancer Res 2009;69:9367-9375
    • (2009) Cancer Res , vol.69 , pp. 9367-9375
    • Yarde, D.N.1    Oliveira, V.2    Mathews, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.