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Volumn 9, Issue 12, 2003, Pages 4483-4493

FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; CHAPERONE; FLT3 LIGAND; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HERBIMYCIN A; HYBRID PROTEIN; MIXED LINEAGE LEUKEMIA PROTEIN; MLL AF4 FUSION PROTEIN; PHOSPHOTRANSFERASE; PROTEIN KINASE B; PROTEIN P23; RAF PROTEIN; SIGNAL TRANSDUCTION ASSOCIATED KINASE; UNCLASSIFIED DRUG;

EID: 0141925960     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (112)

References (37)
  • 2
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny, M. V. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia (Baltimore), 16: 455-462, 2002.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 3
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B., and Toft, D. O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med., 22: 111-133, 2003.
    • (2003) Exp. Biol. Med. , vol.22 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 4
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E., Russo, A. A., Schneider, C., Rosen, N., Hartl, F. U., and Pavletich, N. P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell, 89: 239-250, 1997.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 5
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte, T. W., and Neckers, L. M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol., 42: 273-279, 1998.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 6
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell, L., and Cook, P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol., 10: 705-712, 1996.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 7
    • 0031586616 scopus 로고    scopus 로고
    • Geldanamycin prevents nuclear translocation of mutant p53
    • Dasgupta, G., and Momand, J. Geldanamycin prevents nuclear translocation of mutant p53. Exp. Cell Res., 237: 29-37, 1997.
    • (1997) Exp. Cell Res. , vol.237 , pp. 29-37
    • Dasgupta, G.1    Momand, J.2
  • 8
    • 0034714283 scopus 로고    scopus 로고
    • Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation
    • Tikhomirov, O., and Carpenter, G. Geldanamycin induces ErbB-2 degradation by proteolytic fragmentation. J. Biol. Chem., 275: 26625-26631, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26625-26631
    • Tikhomirov, O.1    Carpenter, G.2
  • 9
    • 0035839952 scopus 로고    scopus 로고
    • Molecular mechanisms of leuke-mogenesis mediated by MLL fusion proteins
    • Ayton, P. M., and Cleary, M. L. Molecular mechanisms of leuke-mogenesis mediated by MLL fusion proteins. Oncogene, 20: 5695-5707, 2001.
    • (2001) Oncogene , vol.20 , pp. 5695-5707
    • Ayton, P.M.1    Cleary, M.L.2
  • 10
    • 0031656062 scopus 로고    scopus 로고
    • Resistance of t(4;11) (MLL-AF4 fusion gene) leukemias to stress-induced cell death: Possible mechanism for extensive extramedullary accumulation of cells and poor prognosis
    • Kersey, J. H., Wang, D., and Oberto, M. Resistance of t(4;11) (MLL-AF4 fusion gene) leukemias to stress-induced cell death: possible mechanism for extensive extramedullary accumulation of cells and poor prognosis. Leukemia (Baltimore), 12: 1561-1564, 1998.
    • (1998) Leukemia (Baltimore) , vol.12 , pp. 1561-1564
    • Kersey, J.H.1    Wang, D.2    Oberto, M.3
  • 12
    • 0035204051 scopus 로고    scopus 로고
    • Internal tandem duplications of the FLT3 and MLL genes are mainly observed in atypical cases of therapy-related acute myeloid leukemia with a normal karyotype and are unrelated to type of previous therapy
    • Christiansen, D. H., and Pedersen-Bjergaard, J. Internal tandem duplications of the FLT3 and MLL genes are mainly observed in atypical cases of therapy-related acute myeloid leukemia with a normal karyotype and are unrelated to type of previous therapy. Leukemia (Baltimore), 15: 1848-1851, 2001.
    • (2001) Leukemia (Baltimore) , vol.15 , pp. 1848-1851
    • Christiansen, D.H.1    Pedersen-Bjergaard, J.2
  • 17
    • 0001097136 scopus 로고    scopus 로고
    • Tandem duplication of the FLT3 gene is found in acute lymphoblastic leukaemia as well as acute myeloid leukaemia but not in myelodysplastic syndrome or juvenile chronic myelogenous leukaemia in children
    • Xu, F., Taki, T., Yang, H. W., Hanada, R., Hongo, T., Ohnishi, H., Kobayashi, M., Bessho, F., Yanagisawa, M., and Hayashi, Y. Tandem duplication of the FLT3 gene is found in acute lymphoblastic leukaemia as well as acute myeloid leukaemia but not in myelodysplastic syndrome or juvenile chronic myelogenous leukaemia in children. Br. J. Haematol., 105: 155-162, 1999.
    • (1999) Br. J. Haematol. , vol.105 , pp. 155-162
    • Xu, F.1    Taki, T.2    Yang, H.W.3    Hanada, R.4    Hongo, T.5    Ohnishi, H.6    Kobayashi, M.7    Bessho, F.8    Yanagisawa, M.9    Hayashi, Y.10
  • 18
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone
    • Clarke, P. A., Hostein, I., Banerji, U., Stefano, F. D., Maloney, A., Walton, M., Judson, I., and Workman, P. Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the hsp90 molecular chaperone. Oncogene, 19: 4125-4133, 2000.
    • (2000) Oncogene , vol.19 , pp. 4125-4133
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3    Stefano, F.D.4    Maloney, A.5    Walton, M.6    Judson, I.7    Workman, P.8
  • 19
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein, I., Robertson, D., DiStefano, F., Workman, P., and Clarke, P. A. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res., 61: 4003-4009, 2001.
    • (2001) Cancer Res. , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 20
    • 0036050018 scopus 로고    scopus 로고
    • Selective apoptosis of tandemly duplicated FLT3-transformed leukemia cells by Hsp90 inhibitors
    • Minami, Y., Kiyoi, H., Yamamoto, Y., Yamamoto, K., Ueda, R., Saito, H., and Naoe, T. Selective apoptosis of tandemly duplicated FLT3-transformed leukemia cells by Hsp90 inhibitors. Leukemia (Baltimore), 16: 1535-1540, 2002.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 1535-1540
    • Minami, Y.1    Kiyoi, H.2    Yamamoto, Y.3    Yamamoto, K.4    Ueda, R.5    Saito, H.6    Naoe, T.7
  • 21
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter, K., and Buchner, J. Hsp90: chaperoning signal transduction. J. Cell. Physiol., 188: 281-290, 2001.
    • (2001) J. Cell. Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 22
    • 0036530301 scopus 로고    scopus 로고
    • 165 promotes survival of leukemic cells by Hsp90-mediated induction of Bcl-2 expression and apoptosis inhibition
    • 165 promotes survival of leukemic cells by Hsp90-mediated induction of Bcl-2 expression and apoptosis inhibition. Blood, 99: 2532-2540, 2002.
    • (2002) Blood , vol.99 , pp. 2532-2540
    • Dias, S.1    Shmelkov, S.V.2    Lam, G.3    Rafii, S.4
  • 23
    • 0034895025 scopus 로고    scopus 로고
    • Inhibition of FLT3-mediated transformation by use of a tyrosine kinase inhibitor
    • Tse, K. F., Novelli, E., Civin, C. I., Bohmer, F. D., and Small, D. Inhibition of FLT3-mediated transformation by use of a tyrosine kinase inhibitor. Leukemia (Baltimore), 15: 1001-1010, 2001.
    • (2001) Leukemia (Baltimore) , vol.15 , pp. 1001-1010
    • Tse, K.F.1    Novelli, E.2    Civin, C.I.3    Bohmer, F.D.4    Small, D.5
  • 24
    • 0035437140 scopus 로고    scopus 로고
    • A FLT3 tyrosine kinase inhibitor is selectively cytotoxic to acute myeloid leukemia blasts harboring FLT3 internal tandem duplication mutations
    • Levis, M., Tse, K. F., Smith, B. D., Garrett, E., and Small, D. A FLT3 tyrosine kinase inhibitor is selectively cytotoxic to acute myeloid leukemia blasts harboring FLT3 internal tandem duplication mutations. Blood, 98: 885-887, 2001.
    • (2001) Blood , vol.98 , pp. 885-887
    • Levis, M.1    Tse, K.F.2    Smith, B.D.3    Garrett, E.4    Small, D.5
  • 27
    • 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, L. M., Manley, P., Fabbro, D., Meyer, T., Gilliland, D. G., and Griffin, J. D. Inhibition of mutant FLT3 receptors in leukemia cells by the small molecule tyrosine kinase inhibitor PKC412. Cancer Cell, 1: 433-443, 2002.
    • (2002) Cancer Cell , vol.1 , pp. 433-443
    • Weisberg, E.1    Boulton, C.2    Kelly, L.M.3    Manley, P.4    Fabbro, D.5    Meyer, T.6    Gilliland, D.G.7    Griffin, J.D.8
  • 30
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L. F., Chow, Y. H., Hutchison, K. A., Perdew, G. H., Jove, R., and Pratt, W. B. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem., 268: 21711-21716, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 31
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato, S., Fujita, N., and Tsuruo, T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. USA., 97: 10832-10837, 2000.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 32
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An, W. G., Schulte, T. W., and Neckers, L. M. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ., 11: 355-360, 2000.
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 33
    • 0034649210 scopus 로고    scopus 로고
    • Flt3 ligand induces tyrosine phosphorylation of gab1 and gab2 and their association with shp-2, grb2, and PI3 kinase
    • Zhang, S., and Broxmeyer, H. E. Flt3 ligand induces tyrosine phosphorylation of gab1 and gab2 and their association with shp-2, grb2, and PI3 kinase. Biochem. Biophys. Res. Commun., 277: 195-199, 2000.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 195-199
    • Zhang, S.1    Broxmeyer, H.E.2
  • 34
    • 0036167084 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line
    • Srinivasa, S. P., and Doshi, P. D. Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line. Leukemia (Baltimore), 16: 244-253, 2002.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 244-253
    • Srinivasa, S.P.1    Doshi, P.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.