메뉴 건너뛰기




Volumn 67, Issue 7, 2007, Pages 3210-3219

Mitogen-activated protein kinase kinase inhibition enhances nuclear proapoptotic function of p53 in acute myelogenous leukemia cells

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; IMIDAZOLE DERIVATIVE; LEPTOMYCIN B; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NUTLIN 3ALPHA; PROTEIN MDM2; PROTEIN P21; PROTEIN P53; RAF PROTEIN; UNCLASSIFIED DRUG; FLAVONOID; MITOGEN ACTIVATED PROTEIN KINASE KINASE; NUTLIN 3; PIPERAZINE DERIVATIVE; TP53 PROTEIN, HUMAN; UNSATURATED FATTY ACID;

EID: 34248177222     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-06-2712     Document Type: Article
Times cited : (50)

References (53)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000;100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 0038792224 scopus 로고    scopus 로고
    • Map kinase signaling pathways and hematologic malignancies
    • Platanias LC. Map kinase signaling pathways and hematologic malignancies. Blood 2003;101:4667-79.
    • (2003) Blood , vol.101 , pp. 4667-4679
    • Platanias, L.C.1
  • 3
    • 0034823632 scopus 로고    scopus 로고
    • Therapeutic targeting of the MEK/MAPK signal transduction module in acute myeloid leukemia
    • Milella M, Kornblau SM, Estrov Z, et al. Therapeutic targeting of the MEK/MAPK signal transduction module in acute myeloid leukemia. J Clin Invest 2001;108:851-9.
    • (2001) J Clin Invest , vol.108 , pp. 851-859
    • Milella, M.1    Kornblau, S.M.2    Estrov, Z.3
  • 4
    • 0033151533 scopus 로고    scopus 로고
    • Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: Combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1
    • Kim SC, Hahn JS, Min YH, Yoo NC, Ko YW, Lee WJ. Constitutive activation of extracellular signal-regulated kinase in human acute leukemias: combined role of activation of MEK, hyperexpression of extracellular signal-regulated kinase, and downregulation of a phosphatase, PAC1. Blood 1999;93:3893-9.
    • (1999) Blood , vol.93 , pp. 3893-3899
    • Kim, S.C.1    Hahn, J.S.2    Min, Y.H.3    Yoo, N.C.4    Ko, Y.W.5    Lee, W.J.6
  • 5
    • 0030972025 scopus 로고    scopus 로고
    • Constitutive activation of mitogen-activated protein kinase pathway in acute leukemia cells
    • Towatari M, Iida H, Tanimoto M, Iwata H, Hamaguchi M, Saito H. Constitutive activation of mitogen-activated protein kinase pathway in acute leukemia cells. Leukemia 1997;11:479-84.
    • (1997) Leukemia , vol.11 , pp. 479-484
    • Towatari, M.1    Iida, H.2    Tanimoto, M.3    Iwata, H.4    Hamaguchi, M.5    Saito, H.6
  • 6
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden KH, Lu X. Live or let die: the cell's response to p53. Nat Rev Cancer 2002;2:594-604.
    • (2002) Nat Rev Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 8
    • 27644568226 scopus 로고    scopus 로고
    • MDM2 antagonists induce p53-dependent apoptosis in AML: Implications for leukemia therapy
    • Kojima K, Konopleva M, Samudio IJ, et al. MDM2 antagonists induce p53-dependent apoptosis in AML: implications for leukemia therapy. Blood 2005;106:3150-9.
    • (2005) Blood , vol.106 , pp. 3150-3159
    • Kojima, K.1    Konopleva, M.2    Samudio, I.J.3
  • 9
    • 0034332527 scopus 로고    scopus 로고
    • ARF locus deletion and MDM-2 protein expression in adult acute myelogenous leukemia
    • ARF locus deletion and MDM-2 protein expression in adult acute myelogenous leukemia. Cancer 2000;89:1976-82.
    • (2000) Cancer , vol.89 , pp. 1976-1982
    • Faderl, S.1    Kantarjian, H.M.2    Estev, E.3
  • 11
    • 0037329056 scopus 로고    scopus 로고
    • The p53-2 module and the ubiquitin system
    • Michael D, Oren M. The p53-2 module and the ubiquitin system. Semin Cancer Biol 2003;13:49-58.
    • (2003) Semin Cancer Biol , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 12
    • 33746646758 scopus 로고    scopus 로고
    • Mdm2 inhibitor Nutlin-3a induces p53-mediated apoptosis by transcription-dependent and transcription-independent mechanisms and may overcome Atm-mediated resistance to fludarabine in chronic lymphocytic leukemia
    • Kojima K, Konopleva M, McQueen T, O'Brien S, Plunkett W, Andreeff M. Mdm2 inhibitor Nutlin-3a induces p53-mediated apoptosis by transcription-dependent and transcription-independent mechanisms and may overcome Atm-mediated resistance to fludarabine in chronic lymphocytic leukemia. Blood 2006;108:993-1000.
    • (2006) Blood , vol.108 , pp. 993-1000
    • Kojima, K.1    Konopleva, M.2    McQueen, T.3    O'Brien, S.4    Plunkett, W.5    Andreeff, M.6
  • 13
    • 4444240191 scopus 로고    scopus 로고
    • The functional interactions between the p53 and MAPK signaling pathways
    • Wu GS. The functional interactions between the p53 and MAPK signaling pathways. Cancer Biol Ther 2004;3:156-61.
    • (2004) Cancer Biol Ther , vol.3 , pp. 156-161
    • Wu, G.S.1
  • 14
    • 0034652115 scopus 로고    scopus 로고
    • Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases
    • Deng X, Ruvolo P, Carr B, May WS, Jr. Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant Bcl2 kinases. Proc Natl Acad Sci U S A 2000;97:1578-83.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1578-1583
    • Deng, X.1    Ruvolo, P.2    Carr, B.3    May Jr., W.S.4
  • 15
    • 0034644506 scopus 로고    scopus 로고
    • Opposing effects of Ras on p53: Transcriptional activation of mdm2 and induction of p19ARF
    • Ries S, Biederer C, Woods D, et al. Opposing effects of Ras on p53: transcriptional activation of mdm2 and induction of p19ARF. Cell 2000;103:321-30.
    • (2000) Cell , vol.103 , pp. 321-330
    • Ries, S.1    Biederer, C.2    Woods, D.3
  • 16
    • 20444482051 scopus 로고    scopus 로고
    • MEK-ERK signaling controls Hdm2 oncoprotein expression by regulating hdm2 mRNA export to the cytoplasm
    • Phelps M, Phillips A, Darley M, Blaydes JP. MEK-ERK signaling controls Hdm2 oncoprotein expression by regulating hdm2 mRNA export to the cytoplasm. J Biol Chem 2005;280:16651-8.
    • (2005) J Biol Chem , vol.280 , pp. 16651-16658
    • Phelps, M.1    Phillips, A.2    Darley, M.3    Blaydes, J.P.4
  • 21
    • 10044274332 scopus 로고    scopus 로고
    • Cooperative regulation of the cell division cycle by the protein kinases RAF and AKT
    • Mirza AM, Gysin S, Malek N, Nakayama K, Roberts JM, McMahon M. Cooperative regulation of the cell division cycle by the protein kinases RAF and AKT. Mol Cell Biol 2004;24:10868-81.
    • (2004) Mol Cell Biol , vol.24 , pp. 10868-10881
    • Mirza, A.M.1    Gysin, S.2    Malek, N.3    Nakayama, K.4    Roberts, J.M.5    McMahon, M.6
  • 22
    • 0038219632 scopus 로고    scopus 로고
    • Waf1/Cip1 protein stability via a cyclin D1-imposed block in proteasome-mediated degradation
    • Waf1/Cip1 protein stability via a cyclin D1-imposed block in proteasome-mediated degradation. EMBO J 2003;22:2036-46.
    • (2003) EMBO J , vol.22 , pp. 2036-2046
    • Coleman, M.L.1    Marshall, C.J.2    Olson, M.F.3
  • 23
    • 0036594890 scopus 로고    scopus 로고
    • The role of the cyclin-dependent kinase inhibitor p21 in apoptosis
    • Gartel AL, Tyner AL. The role of the cyclin-dependent kinase inhibitor p21 in apoptosis. Mol Cancer Ther 2002;1:639-49.
    • (2002) Mol Cancer Ther , vol.1 , pp. 639-649
    • Gartel, A.L.1    Tyner, A.L.2
  • 25
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode AM, Dong Z. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 2004;4:793-805.
    • (2004) Nat Rev Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 26
    • 13944257800 scopus 로고    scopus 로고
    • Transcription, apoptosis and p53: Catch-22
    • Schuler M, Green DR. Transcription, apoptosis and p53: catch-22. Trends Genet 2005;21:182-7.
    • (2005) Trends Genet , vol.21 , pp. 182-187
    • Schuler, M.1    Green, D.R.2
  • 27
    • 0037349289 scopus 로고    scopus 로고
    • p53 has a direct apoptogenic role at the mitochondria
    • Mihara M, Erster S, Zaika A, et al. p53 has a direct apoptogenic role at the mitochondria. Mol Cell 2003;11:577-90.
    • (2003) Mol Cell , vol.11 , pp. 577-590
    • Mihara, M.1    Erster, S.2    Zaika, A.3
  • 28
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk JE, Kuwana T, Bouchier-Hayes L, et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004;303:1010-4.
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3
  • 30
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999;144:891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 31
    • 0036721455 scopus 로고    scopus 로고
    • Spontaneous and drug-induced apoptosis is mediated by conformational changes of Bax and Bak in B-cell chronic lymphocytic leukemia
    • Bellosillo B, Villamor N, Lopez-Guillermo A, et al. Spontaneous and drug-induced apoptosis is mediated by conformational changes of Bax and Bak in B-cell chronic lymphocytic leukemia Blood 2002;100:1810-6.
    • (2002) Blood , vol.100 , pp. 1810-1816
    • Bellosillo, B.1    Villamor, N.2    Lopez-Guillermo, A.3
  • 32
    • 3042549655 scopus 로고    scopus 로고
    • The phosphorylation status and anti-apoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria
    • Tamura Y, Simizu S, Osada H. The phosphorylation status and anti-apoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria. FEBS Lett 2004;569:249-55.
    • (2004) FEBS Lett , vol.569 , pp. 249-255
    • Tamura, Y.1    Simizu, S.2    Osada, H.3
  • 33
    • 0035353163 scopus 로고    scopus 로고
    • Cytokine-regulated expression of survivin in myeloid leukemia
    • Carter BZ, Milella M, Altieri DC, Andreeff M. Cytokine-regulated expression of survivin in myeloid leukemia. Blood 2001;97:2784-90.
    • (2001) Blood , vol.97 , pp. 2784-2790
    • Carter, B.Z.1    Milella, M.2    Altieri, D.C.3    Andreeff, M.4
  • 34
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by mid-type p53
    • Hoffman WH, Biade S, Zilfou JT, Chen J, Murphy M. Transcriptional repression of the anti-apoptotic survivin gene by mid-type p53. J Biol Chem 2002;277:3247-57.
    • (2002) J Biol Chem , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3    Chen, J.4    Murphy, M.5
  • 35
    • 0035150990 scopus 로고    scopus 로고
    • Growth-factor-dependent mitogenesis requires two distinct phases of signalling
    • Jones SM, Kazlauskas A. Growth-factor-dependent mitogenesis requires two distinct phases of signalling. Nat Cell Biol 2001;3:165-72.
    • (2001) Nat Cell Biol , vol.3 , pp. 165-172
    • Jones, S.M.1    Kazlauskas, A.2
  • 36
    • 27944496435 scopus 로고    scopus 로고
    • The PI3K inhibitor LY294002 prevents p53 induction by DNA damage and attenuates chemotherapy-induced apoptosis
    • Bar J, Lukaschuk N, Zalcenstein A, Wilder S, Seger R, Oren M. The PI3K inhibitor LY294002 prevents p53 induction by DNA damage and attenuates chemotherapy-induced apoptosis. Cell Death Differ 2005;12:1578-87.
    • (2005) Cell Death Differ , vol.12 , pp. 1578-1587
    • Bar, J.1    Lukaschuk, N.2    Zalcenstein, A.3    Wilder, S.4    Seger, R.5    Oren, M.6
  • 37
    • 0033536063 scopus 로고    scopus 로고
    • ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc Natl Acad Sci U S A 1999;96:6937-41.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 38
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo LD, Donner DB. A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc Natl Acad Sci U S A 2001;98:11598-603.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 39
    • 0842269247 scopus 로고    scopus 로고
    • The importance of p53 location: Nuclear or cytoplasmic zip code?
    • O'Brate A, Giannakakou P. The importance of p53 location: nuclear or cytoplasmic zip code? Drug Resist Updat 2003;6:313-22.
    • (2003) Drug Resist Updat , vol.6 , pp. 313-322
    • O'Brate, A.1    Giannakakou, P.2
  • 40
    • 2942744364 scopus 로고    scopus 로고
    • Efficient NES-dependent protein nuclear export requires ongoing synthesis and export of mRNAs
    • O'Hagan HM, Ljungman M. Efficient NES-dependent protein nuclear export requires ongoing synthesis and export of mRNAs. Exp Cell Res 2004;297:548-59.
    • (2004) Exp Cell Res , vol.297 , pp. 548-559
    • O'Hagan, H.M.1    Ljungman, M.2
  • 41
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 42
    • 33845421171 scopus 로고    scopus 로고
    • Concomitant inhibition of MDM2 and Bcl-2 protein function synergistically induce mitochondrial apoptosis in AML
    • Kojima K, Konopleva M, Samudio IJ, Schober WD, Bornmann WG, Andreeff M. Concomitant inhibition of MDM2 and Bcl-2 protein function synergistically induce mitochondrial apoptosis in AML. Cell Cycle 2006;5:2778-86.
    • (2006) Cell Cycle , vol.5 , pp. 2778-2786
    • Kojima, K.1    Konopleva, M.2    Samudio, I.J.3    Schober, W.D.4    Bornmann, W.G.5    Andreeff, M.6
  • 43
    • 33749337234 scopus 로고    scopus 로고
    • Simultaneous activation of multiple signal transduction pathways confers poor prognosis in acute myelogenous leukemia
    • Kornblau SM, Womble M, Qiu YH, et al. Simultaneous activation of multiple signal transduction pathways confers poor prognosis in acute myelogenous leukemia. Blood 2006;108:2358-65.
    • (2006) Blood , vol.108 , pp. 2358-2365
    • Kornblau, S.M.1    Womble, M.2    Qiu, Y.H.3
  • 44
    • 11144224782 scopus 로고    scopus 로고
    • Phosphorylation of p53 on key serines is dispensable for transcriptional activation and apoptosis
    • Thompson T, Tovar C, Yang H, et al. Phosphorylation of p53 on key serines is dispensable for transcriptional activation and apoptosis. J Biol Chem 2004;279:53015-22.
    • (2004) J Biol Chem , vol.279 , pp. 53015-53022
    • Thompson, T.1    Tovar, C.2    Yang, H.3
  • 45
    • 0348134742 scopus 로고    scopus 로고
    • Mono- versus polyubiquitination: Differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W. Mono- versus polyubiquitination: differential control of p53 fate by Mdm2. Science 2003;302:1972-5.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 46
    • 0034642549 scopus 로고    scopus 로고
    • Nuclear exclusion of p53 in a subset of tumors requires MDM2 function
    • Lu W, Pochampally R, Chen L, Traidej M, Wang Y, Chen J. Nuclear exclusion of p53 in a subset of tumors requires MDM2 function. Oncogene 2000;19:232-40.
    • (2000) Oncogene , vol.19 , pp. 232-240
    • Lu, W.1    Pochampally, R.2    Chen, L.3    Traidej, M.4    Wang, Y.5    Chen, J.6
  • 47
    • 0037099586 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Mdm2 by c-Abl: Implications for p53 regulation
    • Goldberg Z, Vogt Sionov R, Berger M, et al. Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation. EMBO J 2002;21:3715-27.
    • (2002) EMBO J , vol.21 , pp. 3715-3727
    • Goldberg, Z.1    Vogt Sionov, R.2    Berger, M.3
  • 48
    • 27744440147 scopus 로고    scopus 로고
    • Myeloid leukemia-associated nucleophosmin mutants perturb p53-dependent and independent activities of the Arf tumor suppressor protein
    • den Besten W, Kuo ML, Williams RT, Sherr CJ. Myeloid leukemia-associated nucleophosmin mutants perturb p53-dependent and independent activities of the Arf tumor suppressor protein. Cell Cycle 2005;4:1593-8.
    • (2005) Cell Cycle , vol.4 , pp. 1593-1598
    • den Besten, W.1    Kuo, M.L.2    Williams, R.T.3    Sherr, C.J.4
  • 49
    • 0034607117 scopus 로고    scopus 로고
    • WAF1/CIP1 inhibits initiator caspase cleavage by TRAIL death receptor DR4
    • WAF1/CIP1 inhibits initiator caspase cleavage by TRAIL death receptor DR4. Biochem Biophys Res Commun 2000;269:179-90.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 179-190
    • Xu, S.Q.1    El-Deiry, W.S.2
  • 51
    • 0034279817 scopus 로고    scopus 로고
    • WAF1 prevents down-modulation of the apoptotic inhibitor protein c-IAP1 and inhibits leukemic apoptosis
    • WAF1 prevents down-modulation of the apoptotic inhibitor protein c-IAP1 and inhibits leukemic apoptosis. Mol Med 2000;6:736-49.
    • (2000) Mol Med , vol.6 , pp. 736-749
    • Steinman, R.A.1    Johnson, D.E.2
  • 53
    • 20144384882 scopus 로고    scopus 로고
    • Gartel AL, Radhakrishnan SK. Lost in transcription: p21 repression, mechanisms, and consequences. Cancer Res 2005;65:3980-5.
    • Gartel AL, Radhakrishnan SK. Lost in transcription: p21 repression, mechanisms, and consequences. Cancer Res 2005;65:3980-5.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.