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Volumn 583, Issue 12, 2009, Pages 1859-1866

Transcriptomic and proteomic approach to studying SNX-2112-induced K562 cells apoptosis and anti-leukemia activity in K562-NOD/SCID mice

Author keywords

Apoptosis; K562 cell; Mitochondria dysfunction; Proteomic; SNX 2112; Transcriptomic

Indexed keywords

ANTILEUKEMIC AGENT; CASPASE; PROTEIN KINASE B; SNX 2112; TANESPIMYCIN; UNCLASSIFIED DRUG;

EID: 67349255247     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.04.046     Document Type: Article
Times cited : (38)

References (34)
  • 1
    • 0035989680 scopus 로고    scopus 로고
    • Hsp90 as a new therapeutic target for cancer therapy: the story unfolds
    • Maloney A., and Workman P. Hsp90 as a new therapeutic target for cancer therapy: the story unfolds. Exp. Opin. Biol. Ther. 2 (2002) 3-24
    • (2002) Exp. Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 2
    • 17444404622 scopus 로고    scopus 로고
    • Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer
    • Ruden D.M., Xiao L., Garfinkel M.D., and Lu X. Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer. Hum. Mol. Genet. 14 (2005) 149-155
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 149-155
    • Ruden, D.M.1    Xiao, L.2    Garfinkel, M.D.3    Lu, X.4
  • 3
    • 40749103835 scopus 로고    scopus 로고
    • SNX2112, a synthetic heat shock protein 90 inhibitor, has potent antitumor activity against HER kinase-dependent cancers
    • Chandarlapaty S., et al. SNX2112, a synthetic heat shock protein 90 inhibitor, has potent antitumor activity against HER kinase-dependent cancers. Clin. Cancer Res. 14 (2008) 240-248
    • (2008) Clin. Cancer Res. , vol.14 , pp. 240-248
    • Chandarlapaty, S.1
  • 4
    • 44649202705 scopus 로고    scopus 로고
    • Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90
    • Barta T.E., et al. Discovery of benzamide tetrahydro-4H-carbazol-4-ones as novel small molecule inhibitors of Hsp90. Bioorg. Med. Chem. Lett. 18 (2008) 3517-3521
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3517-3521
    • Barta, T.E.1
  • 5
    • 0242559054 scopus 로고    scopus 로고
    • Pathway studio the analysis and navigation of molecular networks
    • Nikitin A., Egorov S., Daraselia N., and Mazo I. Pathway studio the analysis and navigation of molecular networks. Bioinformatics 19 (2003) 2155-2157
    • (2003) Bioinformatics , vol.19 , pp. 2155-2157
    • Nikitin, A.1    Egorov, S.2    Daraselia, N.3    Mazo, I.4
  • 6
    • 0033516674 scopus 로고    scopus 로고
    • Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway
    • Pastorino J.G., Tafani M., and Farber J.L. Tumor necrosis factor induces phosphorylation and translocation of BAD through a phosphatidylinositide-3-OH kinase-dependent pathway. J. Biol. Chem. 274 (1999) 19411-19416
    • (1999) J. Biol. Chem. , vol.274 , pp. 19411-19416
    • Pastorino, J.G.1    Tafani, M.2    Farber, J.L.3
  • 7
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat protein 90
    • Kelland L.R., Sharp S.Y., Rogers P.M., Myers T.G., and Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat protein 90. J. Natl. Cancer Inst. 91 (1999) 1940-1949
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 8
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson D.W., et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376 (1995) 3-43
    • (1995) Nature , vol.376 , pp. 3-43
    • Nicholson, D.W.1
  • 9
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 326 (1997) 1-16
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 10
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 88 (1997) 355-365
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 12
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39 (2005) 359-407
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 13
    • 64149088232 scopus 로고    scopus 로고
    • HNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis
    • Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H.L., and Farquhar M.G. HNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis. J. Biol. Chem. 284 (2009) 5414-5424
    • (2009) J. Biol. Chem. , vol.284 , pp. 5414-5424
    • Tang, T.1    Zheng, B.2    Chen, S.H.3    Murphy, A.N.4    Kudlicka, K.5    Zhou, H.L.6    Farquhar, M.G.7
  • 14
    • 0035116301 scopus 로고    scopus 로고
    • Anticancer drugs induce increased mitochondrial cytochrome c expression that precedes cell death
    • Sánchez-Alcázar J.A., Khodjakov A., and Schneider E. Anticancer drugs induce increased mitochondrial cytochrome c expression that precedes cell death. Cancer Res. 61 (2001) 1038-1044
    • (2001) Cancer Res. , vol.61 , pp. 1038-1044
    • Sánchez-Alcázar, J.A.1    Khodjakov, A.2    Schneider, E.3
  • 15
    • 63649114106 scopus 로고    scopus 로고
    • Global transcriptional response of Saccharomyces cerevisiae to the deletion of SDH3
    • Cimini D., Patil K.R., Schiraldi C., and Nielsen J. Global transcriptional response of Saccharomyces cerevisiae to the deletion of SDH3. BMC Syst. Biol. 3 (2009) 17
    • (2009) BMC Syst. Biol. , vol.3 , pp. 17
    • Cimini, D.1    Patil, K.R.2    Schiraldi, C.3    Nielsen, J.4
  • 17
    • 35748967258 scopus 로고    scopus 로고
    • Mitochondrial targeting of human peroxiredoxin V protein and regulation of PRDX5 gene expression by nuclear transcription factors controlling biogenesis of mitochondria
    • Kropotov A., Usmanova N., Serikov V., Zhivotovsky B., and Tomilin N. Mitochondrial targeting of human peroxiredoxin V protein and regulation of PRDX5 gene expression by nuclear transcription factors controlling biogenesis of mitochondria. FEBS J. 274 (2007) 5804-5814
    • (2007) FEBS J. , vol.274 , pp. 5804-5814
    • Kropotov, A.1    Usmanova, N.2    Serikov, V.3    Zhivotovsky, B.4    Tomilin, N.5
  • 18
    • 17644386166 scopus 로고    scopus 로고
    • Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide
    • Banmeyer I., Marchand C., Clippe A., and Knoops B. Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide. FEBS Lett. 579 (2005) 2327-2333
    • (2005) FEBS Lett. , vol.579 , pp. 2327-2333
    • Banmeyer, I.1    Marchand, C.2    Clippe, A.3    Knoops, B.4
  • 19
    • 0344875598 scopus 로고    scopus 로고
    • Reduction of Fe(III) ions complexed to physiological ligands by lipoyl dehydrogenase and other flavoenzymes in vitro: implications for an enzymatic reduction of Fe(III) ions of the labile iron pool
    • Petrat F., Paluch S., Dogruoz E., Dorfler P., Kirsch M., Korth H.G., Sustmann R., and de Groot H. Reduction of Fe(III) ions complexed to physiological ligands by lipoyl dehydrogenase and other flavoenzymes in vitro: implications for an enzymatic reduction of Fe(III) ions of the labile iron pool. J. Biol. Chem. 278 (2003) 46403-46413
    • (2003) J. Biol. Chem. , vol.278 , pp. 46403-46413
    • Petrat, F.1    Paluch, S.2    Dogruoz, E.3    Dorfler, P.4    Kirsch, M.5    Korth, H.G.6    Sustmann, R.7    de Groot, H.8
  • 20
    • 57749085555 scopus 로고    scopus 로고
    • Timosaponin A-III induces autophagy preceding mitochondria-mediated apoptosis in HeLa cancer cells
    • Sy L.K., Yan S.C., Lok C.N., Man R.Y., and Che C.M. Timosaponin A-III induces autophagy preceding mitochondria-mediated apoptosis in HeLa cancer cells. Cancer Res. 68 (2008) 10229-10237
    • (2008) Cancer Res. , vol.68 , pp. 10229-10237
    • Sy, L.K.1    Yan, S.C.2    Lok, C.N.3    Man, R.Y.4    Che, C.M.5
  • 21
    • 0026485034 scopus 로고
    • Inhibition of enoyl-CoA hydratase by long-chain L-3-hydroxyacyl-CoA and its possible effect on fatty acid
    • He X.Y., Yang S.Y., and Schulz H. Inhibition of enoyl-CoA hydratase by long-chain L-3-hydroxyacyl-CoA and its possible effect on fatty acid. Arch Biochem. Biophys. 298 (1992) 527-531
    • (1992) Arch Biochem. Biophys. , vol.298 , pp. 527-531
    • He, X.Y.1    Yang, S.Y.2    Schulz, H.3
  • 22
    • 0141509869 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration: a novel strategy to enhance drug-induced apoptosis in human leukemia cells by a reactive oxygen species-mediated mechanism
    • Pelicano H., Feng L., Zhou Y., Carew J.S., Hileman E.O., Plunkett W., Keating M.J., and Huang P. Inhibition of mitochondrial respiration: a novel strategy to enhance drug-induced apoptosis in human leukemia cells by a reactive oxygen species-mediated mechanism. J. Biol. Chem. 278 (2003) 37832-37839
    • (2003) J. Biol. Chem. , vol.278 , pp. 37832-37839
    • Pelicano, H.1    Feng, L.2    Zhou, Y.3    Carew, J.S.4    Hileman, E.O.5    Plunkett, W.6    Keating, M.J.7    Huang, P.8
  • 23
    • 36248980938 scopus 로고    scopus 로고
    • Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis
    • Montesano G.N., Chirico G., Pirozzi G., Costantino E., Landriscina M., and Esposito F. Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis. Stress 10 (2007) 342-350
    • (2007) Stress , vol.10 , pp. 342-350
    • Montesano, G.N.1    Chirico, G.2    Pirozzi, G.3    Costantino, E.4    Landriscina, M.5    Esposito, F.6
  • 24
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi Y. The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54 (1985) 1015-1069
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 25
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome c: can't live with it - can't live without it
    • Reed J.C. Cytochrome c: can't live with it - can't live without it. Cell 91 (1997) 559-562
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 26
    • 33751104472 scopus 로고    scopus 로고
    • Detection in primary chronic myeloid leukaemia cells of p210BCR-ABL1 in complexes with adaptor proteins CBL, CRKL, and GRB2
    • Patel H., Marley S.B., and Gordon M.Y. Detection in primary chronic myeloid leukaemia cells of p210BCR-ABL1 in complexes with adaptor proteins CBL, CRKL, and GRB2. Genes Chromosomes Cancer 45 (2006) 1121-1129
    • (2006) Genes Chromosomes Cancer , vol.45 , pp. 1121-1129
    • Patel, H.1    Marley, S.B.2    Gordon, M.Y.3
  • 27
    • 0029669975 scopus 로고    scopus 로고
    • The proto-oncogene product p120CBL and the adaptor proteins CRKL and c-CRK link c-ABL, p190BCR/ABL and p210BCR/ABL to the phosphatidylinositol-3′ kinase pathway
    • Sattler M., et al. The proto-oncogene product p120CBL and the adaptor proteins CRKL and c-CRK link c-ABL, p190BCR/ABL and p210BCR/ABL to the phosphatidylinositol-3′ kinase pathway. Oncogene 12 (1996) 839-846
    • (1996) Oncogene , vol.12 , pp. 839-846
    • Sattler, M.1
  • 28
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG - mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao R., et al. HDAC6 inhibition enhances 17-AAG - mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 112 (2008) 1886-1893
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1
  • 29
    • 33847324723 scopus 로고    scopus 로고
    • Different target range and cytotoxic specificity of adaphostin and 17-allylamino-17-demethoxygeldanamycin in imatinib-resistant and sensitive cell lines
    • Barnes D.J., De S., van Hensbergen P., Moravcsik E., and Melo J.V. Different target range and cytotoxic specificity of adaphostin and 17-allylamino-17-demethoxygeldanamycin in imatinib-resistant and sensitive cell lines. Leukemia 21 (2007) 421-426
    • (2007) Leukemia , vol.21 , pp. 421-426
    • Barnes, D.J.1    De, S.2    van Hensbergen, P.3    Moravcsik, E.4    Melo, J.V.5
  • 30
    • 58149379046 scopus 로고    scopus 로고
    • Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway
    • Park T.J., and Curran T. Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway. J. Neurosci. 28 (2008) 13551-13562
    • (2008) J. Neurosci. , vol.28 , pp. 13551-13562
    • Park, T.J.1    Curran, T.2
  • 31
    • 33747340770 scopus 로고    scopus 로고
    • The adaptor protein Gab1 couples the stimulation of vascular endothelial growth factor receptor-2 to the activation of phosphoinositide 3-kinase
    • Dance M., Montagner A., Yart A., Masri B., Audigier Y., Perret B., Salles J.P., and Raynal P. The adaptor protein Gab1 couples the stimulation of vascular endothelial growth factor receptor-2 to the activation of phosphoinositide 3-kinase. J. Biol. Chem. 281 (2006) 23285-23295
    • (2006) J. Biol. Chem. , vol.281 , pp. 23285-23295
    • Dance, M.1    Montagner, A.2    Yart, A.3    Masri, B.4    Audigier, Y.5    Perret, B.6    Salles, J.P.7    Raynal, P.8
  • 32
    • 40549133440 scopus 로고    scopus 로고
    • Abl tyrosine kinases modulate cadherin-dependent adhesion upstream and downstream of Rho family GTPases
    • Zandy N.L., and Pendergast A.M. Abl tyrosine kinases modulate cadherin-dependent adhesion upstream and downstream of Rho family GTPases. Cell Cycle 7 (2007) 444-448
    • (2007) Cell Cycle , vol.7 , pp. 444-448
    • Zandy, N.L.1    Pendergast, A.M.2
  • 33
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta S.R., Dudek H., Tao X., Masters S., Fu H., Gotoh Y., and Greenberg M.E. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91 (1997) 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 34
    • 0035525787 scopus 로고    scopus 로고
    • Establishment of a murine model for therapy-treated chronic myelogenous leukemia using the tyrosine kinase inhibitor STI571
    • Wolff N.C., and Ilaria Jr. R.L. Establishment of a murine model for therapy-treated chronic myelogenous leukemia using the tyrosine kinase inhibitor STI571. Blood 98 (2001) 2808-2816
    • (2001) Blood , vol.98 , pp. 2808-2816
    • Wolff, N.C.1    Ilaria Jr., R.L.2


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