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Volumn 64, Issue 10, 2004, Pages 3645-3652

Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINODEMETHOXYGELDANAMYCIN; ANTINEOPLASTIC AGENT; CHAPERONE; FLT3 KINASE; FLT3 LIGAND; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MIDOSTAURIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MYC PROTEIN; ONCOSTATIN M; PHOSPHOTRANSFERASE; PROTEASOME; PROTEIN KINASE B; STAT5 PROTEIN; UNCLASSIFIED DRUG;

EID: 2442695516     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-04-0006     Document Type: Article
Times cited : (126)

References (31)
  • 1
    • 0036720398 scopus 로고    scopus 로고
    • The roles of FLT3 in hematopoiesis and leukemia
    • Gilliland DG, Griffin JD. The roles of FLT3 in hematopoiesis and leukemia. Blood 2002;100:1532-42.
    • (2002) Blood , vol.100 , pp. 1532-1542
    • Gilliland, D.G.1    Griffin, J.D.2
  • 2
    • 0141465061 scopus 로고    scopus 로고
    • The role of FLT3 in haematopoietic malignancies
    • Stirewalt DL, Radich J. The role of FLT3 in haematopoietic malignancies. Nat Rev Cancer 2003;3:650-65.
    • (2003) Nat Rev Cancer , vol.3 , pp. 650-665
    • Stirewalt, D.L.1    Radich, J.2
  • 3
    • 0036093475 scopus 로고    scopus 로고
    • FLT3 internal tandem duplication mutations associated with human acute myeloid leukemias induce myeloproliferative disease in a murine bone marrow transplant model
    • Kelly LM, Liu Q, Kutok JL, Williams IR, Boulton CL, Gilliland DG. FLT3 internal tandem duplication mutations associated with human acute myeloid leukemias induce myeloproliferative disease in a murine bone marrow transplant model. Blood 2002;99:310-8.
    • (2002) Blood , vol.99 , pp. 310-318
    • Kelly, L.M.1    Liu, Q.2    Kutok, J.L.3    Williams, I.R.4    Boulton, C.L.5    Gilliland, D.G.6
  • 4
    • 0033820091 scopus 로고    scopus 로고
    • Constitutive activation of FLT3 stimulates multiple intracellular signal transducers and results in transformation
    • Tse K-F, Mukherjee G, Small D. Constitutive activation of FLT3 stimulates multiple intracellular signal transducers and results in transformation. Leukemia (Baltimore) 2000;14:1766-76.
    • (2000) Leukemia (Baltimore) , vol.14 , pp. 1766-1776
    • Tse, K.-F.1    Mukherjee, G.2    Small, D.3
  • 5
    • 0036659931 scopus 로고    scopus 로고
    • Analysis of FLT3 length mutations in 1003 patients with acute myeloid leukemia: Correlation to cytogenetics, FAB subtype, and prognosis in the AMLCG study and usefulness as a marker for the detection of minimal residual disease
    • Schnittger S, Schoch C, Dugas M, et al. Analysis of FLT3 length mutations in 1003 patients with acute myeloid leukemia: correlation to cytogenetics, FAB subtype, and prognosis in the AMLCG study and usefulness as a marker for the detection of minimal residual disease. Blood 2002;100:59-66.
    • (2002) Blood , vol.100 , pp. 59-66
    • Schnittger, S.1    Schoch, C.2    Dugas, M.3
  • 6
    • 0037186924 scopus 로고    scopus 로고
    • Imatinib mesylate: A new oral targeted therapy
    • Savage DG, Antman KH. Imatinib mesylate: a new oral targeted therapy. N Engl J Med 2002;28:689-93.
    • (2002) N Engl J Med , vol.28 , pp. 689-693
    • Savage, D.G.1    Antman, K.H.2
  • 7
    • 0036595143 scopus 로고    scopus 로고
    • Inhibition of mutant FLT3 receptors in leukemia cells by the small molecule tyrosine kinase inhibitor PKC412
    • Weisberg E, Boulton C, Kelly LM, et al. Inhibition of mutant FLT3 receptors in leukemia cells by the small molecule tyrosine kinase inhibitor PKC412. Cancer Cell 2002;1:433-43.
    • (2002) Cancer Cell , vol.1 , pp. 433-443
    • Weisberg, E.1    Boulton, C.2    Kelly, L.M.3
  • 8
    • 0036595322 scopus 로고    scopus 로고
    • Finding the next Gleevec: FLT3 targeted kinase inhibitor therapy for acute myeloid leukemia
    • Sawyers CL. Finding the next Gleevec: FLT3 targeted kinase inhibitor therapy for acute myeloid leukemia. Cancer Cell 2002;1:413-5.
    • (2002) Cancer Cell , vol.1 , pp. 413-415
    • Sawyers, C.L.1
  • 9
    • 0036050018 scopus 로고    scopus 로고
    • Selective apoptosis of tandemly duplicated FLT3-transformed leukemia cells by Hsp90 inhibitors
    • Minami Y, Kiyoi H, Yamamoto Y, et al. Selective apoptosis of tandemly duplicated FLT3-transformed leukemia cells by Hsp90 inhibitors. Leukemia (Baltimore) 2002;16:1535-40.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 1535-1540
    • Minami, Y.1    Kiyoi, H.2    Yamamoto, Y.3
  • 10
    • 0141925960 scopus 로고    scopus 로고
    • FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases
    • Yao Q, Nishiuchi R, Li Q, Kumar AR, Hudson WA, Kersey JH. FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clin Cancer Res 2003;9:4483-93.
    • (2003) Clin Cancer Res , vol.9 , pp. 4483-4493
    • Yao, Q.1    Nishiuchi, R.2    Li, Q.3    Kumar, A.R.4    Hudson, W.A.5    Kersey, J.H.6
  • 11
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny MV. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia (Baltimore) 2002;16:455-62.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 12
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs HS, Xu W, Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003;3:213-7.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, H.S.1    Xu, W.2    Neckers, L.3
  • 13
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert JP, Sullivan WP, Fadden P, et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem 1997;272:23843-50.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.P.1    Sullivan, W.P.2    Fadden, P.3
  • 14
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of Imatinib Mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R, Fuino L, Bali P, et al. Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of Imatinib Mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res 2003;63:5126-35.
    • (2003) Cancer Res , vol.63 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3
  • 15
    • 0037108879 scopus 로고    scopus 로고
    • Molecular characterization and sensitivity of STI-571 (Imatinib Mesylate, Gleevec)-resistant, Bcr-Abl positive, human acute leukemia cells retain sensitivity to SRC kinase inhibitor PD180970 and 17-allylamino-17-demethoxygeldanamycin (17-AAG)
    • Nimmanapalli R, O'Bryan E, Huang M, et al. Molecular characterization and sensitivity of STI-571 (Imatinib Mesylate, Gleevec)-resistant, Bcr-Abl positive, human acute leukemia cells retain sensitivity to SRC kinase inhibitor PD180970 and 17-allylamino-17-demethoxygeldanamycin (17-AAG). Cancer Res 2002;62:5761-9.
    • (2002) Cancer Res , vol.62 , pp. 5761-5769
    • Nimmanapalli, R.1    O'Bryan, E.2    Huang, M.3
  • 16
    • 0035266132 scopus 로고    scopus 로고
    • Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts
    • Nimmanapalli R, O'Bryan E, Bhalla K. Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts. Cancer Res 2001;61:1799-804.
    • (2001) Cancer Res , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 17
    • 0034665903 scopus 로고    scopus 로고
    • CGP57148 (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl positive human leukemia cells to apoptosis due to antileukemic drugs
    • Fang G, Kim C, Perkins C, et al. CGP57148 (STI-571) induces differentiation and apoptosis and sensitizes Bcr-Abl positive human leukemia cells to apoptosis due to antileukemic drugs. Blood 2000;96:2246-56.
    • (2000) Blood , vol.96 , pp. 2246-2256
    • Fang, G.1    Kim, C.2    Perkins, C.3
  • 18
    • 0029658187 scopus 로고    scopus 로고
    • L overexpression inhibits Taxol-induced Yama protease activity and apoptosis
    • L overexpression inhibits Taxol-induced Yama protease activity and apoptosis. Cell Growth Differ 1996;7:1087-94.
    • (1996) Cell Growth Differ , vol.7 , pp. 1087-1094
    • Ibrado, A.M.1    Huang, Y.2    Fang, G.3    Bhalla, K.4
  • 19
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou TC, Talalay P. Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv Enzyme Regul 1984;22:27-55.
    • (1984) Adv Enzyme Regul , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 21
    • 0037944120 scopus 로고    scopus 로고
    • Suppression of myeloid transcription factors and induction of STAT response genes by AML-specific Flt3 mutations
    • Mizuki M, Schwäble J, Steur C, et al. Suppression of myeloid transcription factors and induction of STAT response genes by AML-specific Flt3 mutations. Blood 2003;101:3164-73.
    • (2003) Blood , vol.101 , pp. 3164-3173
    • Mizuki, M.1    Schwäble, J.2    Steur, C.3
  • 22
    • 0027494860 scopus 로고
    • Mitogenic signaling and substrate specificity of the Flk2/Flt3 receptor tyrosine kinase in fibroblasts and interleukin 3-dependent hematopoietic cells
    • Dosil M, Wang S, Lemischka IR. Mitogenic signaling and substrate specificity of the Flk2/Flt3 receptor tyrosine kinase in fibroblasts and interleukin 3-dependent hematopoietic cells. Mol Cell Biol 1993;13:6572-85.
    • (1993) Mol Cell Biol , vol.13 , pp. 6572-6585
    • Dosil, M.1    Wang, S.2    Lemischka, I.R.3
  • 23
    • 0037838661 scopus 로고    scopus 로고
    • Overexpression and constitutive activation of FLT3 induces STAT5 activation in primary acute myeloid leukemia blast cells
    • Spiekermann K, Bagrintseva K, Schwab R, Schmieja K, Hiddemann W. Overexpression and constitutive activation of FLT3 induces STAT5 activation in primary acute myeloid leukemia blast cells. Clin Cancer Res 2003;9:2140-50.
    • (2003) Clin Cancer Res , vol.9 , pp. 2140-2150
    • Spiekermann, K.1    Bagrintseva, K.2    Schwab, R.3    Schmieja, K.4    Hiddemann, W.5
  • 24
    • 0034605042 scopus 로고    scopus 로고
    • Essential role of signal transducer and activator of transcription (Stat)5a but not Stat5b for Flt3-dependent signaling
    • Zhang S, Fukuda S, Lee Y, et al. Essential role of signal transducer and activator of transcription (Stat)5a but not Stat5b for Flt3-dependent signaling. J Exp Med 2000;192:719-28.
    • (2000) J Exp Med , vol.192 , pp. 719-728
    • Zhang, S.1    Fukuda, S.2    Lee, Y.3
  • 25
    • 0013312329 scopus 로고    scopus 로고
    • Inhibition of FLT3 in MLL: Validation of a therapeutic target identified by gene expression based classification
    • Armstrong SA, Kung AL, Mabon ME, et al. Inhibition of FLT3 in MLL: validation of a therapeutic target identified by gene expression based classification. Cancer Cell 2003;3:173-83.
    • (2003) Cancer Cell , vol.3 , pp. 173-183
    • Armstrong, S.A.1    Kung, A.L.2    Mabon, M.E.3
  • 26
    • 0038156174 scopus 로고    scopus 로고
    • Sensitivity toward tyrosine kinase inhibitors varies between different activating mutations of the FLT3 receptor
    • Grundler R, Thiede C, Miething C, Steudel C, Peschel C, Duyster J. Sensitivity toward tyrosine kinase inhibitors varies between different activating mutations of the FLT3 receptor. Blood 2003;102:646-51.
    • (2003) Blood , vol.102 , pp. 646-651
    • Grundler, R.1    Thiede, C.2    Miething, C.3    Steudel, C.4    Peschel, C.5    Duyster, J.6
  • 27
    • 1842463109 scopus 로고    scopus 로고
    • A randomized Phase 11 trial of the tyrosine kinase inhibitor PKC412 in patients (pt) with acute myeloid leukemia (AML)/high-risk myelodysplastic syndromes (MDS) characterized by wild-type (WT) or mutated FLT3
    • Estey EH, Fisher T, Giles F, et al. A randomized Phase 11 trial of the tyrosine kinase inhibitor PKC412 in patients (pt) with acute myeloid leukemia (AML)/high-risk myelodysplastic syndromes (MDS) characterized by wild-type (WT) or mutated FLT3 [abstract]. Blood 2003;102:2270.
    • (2003) Blood , vol.102 , pp. 2270
    • Estey, E.H.1    Fisher, T.2    Giles, F.3
  • 28
    • 0142124533 scopus 로고    scopus 로고
    • Phase I trial of 17-AAG (17-allylamino-17-demethoxygeldanamycin) in patients (pt) with advanced cancer
    • Solit DB, Anana M, Valentin G, et al. Phase I trial of 17-AAG (17-allylamino-17-demethoxygeldanamycin) in patients (pt) with advanced cancer [abstract]. Proc Am Soc Clin Oncol 2003;22:795.
    • (2003) Proc Am Soc Clin Oncol , vol.22 , pp. 795
    • Solit, D.B.1    Anana, M.2    Valentin, G.3
  • 29
    • 0037108448 scopus 로고    scopus 로고
    • BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90
    • Gorre ME, Ellwood-Yen K, Chiosis G, Rosen N, Sawyers CL. BCR-ABL point mutants isolated from patients with imatinib mesylate-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood 2002;100:3041-4.
    • (2002) Blood , vol.100 , pp. 3041-3044
    • Gorre, M.E.1    Ellwood-Yen, K.2    Chiosis, G.3    Rosen, N.4    Sawyers, C.L.5
  • 31
    • 0042441979 scopus 로고    scopus 로고
    • Synergistic antileukemic interactions between 17-AAG and UCN-01 involve interruption of RAF/MEK- and AKT-related pathways
    • Jia W, Yu C, Rahmani M, et al. Synergistic antileukemic interactions between 17-AAG and UCN-01 involve interruption of RAF/MEK- and AKT-related pathways. Blood 2003;102:1824-32.
    • (2003) Blood , vol.102 , pp. 1824-1832
    • Jia, W.1    Yu, C.2    Rahmani, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.