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Volumn 24, Issue 4, 2010, Pages 729-739

Targeting PKCδ-mediated topoisomerase IIΒ overexpression subverts the differentiation block in a retinoic acid-resistant APL cell line

Author keywords

Acute promyelocytic leukemia; Protein kinase C delta; Resistance; Retinoic acid; Topoisomerase II beta

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN; CYTOCHROME P450 26A1; DNA TOPOISOMERASE (ATP HYDROLYSING); GLYCOPROTEIN P 15095; PROTEIN KINASE C DELTA; RETINOIC ACID; RETINOIC ACID INDUCIBLE PROTEIN I; TOPOISOMERASE II BETA; UNCLASSIFIED DRUG;

EID: 77950925303     PISSN: 08876924     EISSN: 14765551     Source Type: Journal    
DOI: 10.1038/leu.2010.27     Document Type: Article
Times cited : (22)

References (68)
  • 1
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The H, Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 1991; 66: 675-684.
    • (1991) Cell , vol.66 , pp. 675-684
    • De The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 2
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor
    • Kakizuka A, Miller Jr WH, Umesono K, Warrell Jr RP, Frankel SR, Murty VV et al. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 1991; 66: 663-674.
    • (1991) PML. Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller Jr, W.H.2    Umesono, K.3    Warrell Jr, R.P.4    Frankel, S.R.5    Murty, V.V.6
  • 3
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties
    • Pandolfi PP, Grignani F, Alcalay M, Mencarelli A, Biondi A, LoCoco F et al. Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene 1991; 6: 1285-1292.
    • (1991) Oncogene , vol.6 , pp. 1285-1292
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3    Mencarelli, A.4    Biondi, A.5    Lococo, F.6
  • 4
    • 0027368561 scopus 로고
    • Effect of all transretinoic acid in newly diagnosed acute promyelocytic leukemia. Results of a multicenter randomized trial. European APL 91 Group
    • Fenaux P, Le Deley MC, Castaigne S, Archimbaud E, Chomienne C, Link H et al. Effect of all transretinoic acid in newly diagnosed acute promyelocytic leukemia. Results of a multicenter randomized trial. European APL 91 Group. Blood 1993; 82: 3241-3249.
    • (1993) Blood , vol.82 , pp. 3241-3249
    • Fenaux, P.1    Le Deley, M.C.2    Castaigne, S.3    Archimbaud, E.4    Chomienne, C.5    Link, H.6
  • 5
    • 0029086266 scopus 로고
    • Induction of retinoid resistance by all-trans retinoic acid in acute promyelocytic leukemia after remission
    • Cornic M, Chomienne C. Induction of retinoid resistance by all-trans retinoic acid in acute promyelocytic leukemia after remission. Leuk Lymphoma 1995; 18: 249-257.
    • (1995) Leuk Lymphoma , vol.18 , pp. 249-257
    • Cornic, M.1    Chomienne, C.2
  • 6
    • 0027102364 scopus 로고
    • A retinoid acid 'resistant' t(15;17) acute promyelocytic leukemia cell line: Isolation, morphological, immunological, and molecular features
    • Duprez E, Ruchaud S, Houge G, Martin-Thouvenin V, Valensi F, Kastner P et al. A retinoid acid 'resistant' t(15;17) acute promyelocytic leukemia cell line: isolation, morphological, immunological, and molecular features. Leukemia 1992; 6: 1281-1287.
    • (1992) Leukemia , vol.6 , pp. 1281-1287
    • Duprez, E.1    Ruchaud, S.2    Houge, G.3    Martin-Thouvenin, V.4    Valensi, F.5    Kastner, P.6
  • 7
    • 0032528520 scopus 로고    scopus 로고
    • Mutations in the E-domain of RAR portion of the PML/RAR chimeric gene may confer clinical resistance to all-trans retinoic acid in acute promyelocytic leukemia
    • Imaizumi M, Suzuki H, Yoshinari M, Sato A, Saito T, Sugawara A et al. Mutations in the E-domain of RAR portion of the PML/RAR chimeric gene may confer clinical resistance to all-trans retinoic acid in acute promyelocytic leukemia. Blood 1998; 92: 374-382.
    • (1998) Blood , vol.92 , pp. 374-382
    • Imaizumi, M.1    Suzuki, H.2    Yoshinari, M.3    Sato, A.4    Saito, T.5    Sugawara, A.6
  • 8
    • 0032529284 scopus 로고    scopus 로고
    • Leukemic cellular retinoic acid resistance and missense mutations in the PML-RARalpha fusion gene after relapse of acute promye-locytic leukemia from treatment with all-trans retinoic acid and intensive chemotherapy
    • Ding W, Li YP, Nobile LM, Grills G, Carrera I, Paietta E et al. Leukemic cellular retinoic acid resistance and missense mutations in the PML-RARalpha fusion gene after relapse of acute promye-locytic leukemia from treatment with all-trans retinoic acid and intensive chemotherapy. Blood 1998; 92: 1172-1183.
    • (1998) Blood , vol.92 , pp. 1172-1183
    • Ding, W.1    Li, Y.P.2    Nobile, L.M.3    Grills, G.4    Carrera, I.5    Paietta, E.6
  • 9
    • 0032753459 scopus 로고    scopus 로고
    • Missense mutations in the PML/RARalpha ligand binding domain in ATRA-resistant As(2)O(3) sensitive relapsed acute promyelocytic leukemia
    • Marasca R, Zucchini P, Galimberti S, Leonardi G, Vaccari P, Donelli A et al. Missense mutations in the PML/RARalpha ligand binding domain in ATRA-resistant As(2)O(3) sensitive relapsed acute promyelocytic leukemia. Haematologica 1999; 84: 963-968.
    • (1999) Haematologica , vol.84 , pp. 963-968
    • Marasca, R.1    Zucchini, P.2    Galimberti, S.3    Leonardi, G.4    Vaccari, P.5    Donelli, A.6
  • 10
    • 0037082488 scopus 로고    scopus 로고
    • Frequent mutations in the ligand-binding domain of PML-RARalpha after multiple relapses of acute promyelocytic leukemia: Analysis for functional relationship to response to all-trans retinoic acid and histone deacetylase inhibitors in vitro and in vivo
    • Zhou DC, Kim SH, Ding W, Schultz C, Warrell Jr RP, Gallagher RE. Frequent mutations in the ligand-binding domain of PML-RARalpha after multiple relapses of acute promyelocytic leukemia: analysis for functional relationship to response to all-trans retinoic acid and histone deacetylase inhibitors in vitro and in vivo. Blood 2002; 99: 1356-1363.
    • (2002) Blood , vol.99 , pp. 1356-1363
    • Zhou, D.C.1    Kim, S.H.2    Ding, W.3    Schultz, C.4    Warrell Jr, R.P.5    Gallagher, R.E.6
  • 11
    • 0029793469 scopus 로고    scopus 로고
    • Alterations in expression, binding to ligand and DNA, and transcriptional activity of rearranged and wild-type retinoid receptors in retinoid-resistant acute promyelocytic leukemia cell lines
    • Rosenauer A, Raelson JV, Nervi C, Eydoux P, DeBlasio A, Miller Jr WH. Alterations in expression, binding to ligand and DNA, and transcriptional activity of rearranged and wild-type retinoid receptors in retinoid-resistant acute promyelocytic leukemia cell lines. Blood 1996; 88: 2671-2682.
    • (1996) Blood , vol.88 , pp. 2671-2682
    • Rosenauer, A.1    Raelson, J.V.2    Nervi, C.3    Eydoux, P.4    Deblasio, A.5    Miller Jr, W.H.6
  • 12
    • 0030992905 scopus 로고    scopus 로고
    • A retinoid-resistant acute promyelocytic leukemia subclone expresses a dominant negative PML-RAR alpha mutation
    • Shao W, Benedetti L, Lamph WW, Nervi C, Miller Jr WH. A retinoid-resistant acute promyelocytic leukemia subclone expresses a dominant negative PML-RAR alpha mutation. Blood 1997; 89: 4282-4289.
    • (1997) Blood , vol.89 , pp. 4282-4289
    • Shao, W.1    Benedetti, L.2    Lamph, W.W.3    Nervi, C.4    Miller Jr, W.H.5
  • 13
    • 40349114500 scopus 로고    scopus 로고
    • Topoisomerase II{beta} negatively modulates RAR{alpha} function - A novel mechanism of retinoic acid resistance
    • McNamara S, Wang H, Hanna N, Miller Jr WH. Topoisomerase II{beta} negatively modulates RAR{alpha} function-a novel mechanism of retinoic acid resistance. Mol Cell Biol 2008; 28: 2066-2077.
    • (2008) Mol Cell Biol , vol.28 , pp. 2066-2077
    • McNamara, S.1    Wang, H.2    Hanna, N.3    Miller Jr., W.H.4
  • 14
    • 0032032797 scopus 로고    scopus 로고
    • Eukaryotic DNA topoisomerase II beta
    • Austin CA, Marsh KL. Eukaryotic DNA topoisomerase II beta. Bioessays 1998; 20: 215-226.
    • (1998) Bioessays , vol.20 , pp. 215-226
    • Austin, C.A.1    Marsh, K.L.2
  • 15
    • 37549023863 scopus 로고    scopus 로고
    • Structural basis for gate-DNA recognition and bending by type IIA topoisomerases
    • Dong KC, Berger JM. Structural basis for gate-DNA recognition and bending by type IIA topoisomerases. Nature 2007; 450: 1201-1205.
    • (2007) Nature , vol.450 , pp. 1201-1205
    • Dong, K.C.1    Berger, J.M.2
  • 16
    • 0028174984 scopus 로고
    • DNA topoisomerases: Essential enzymes and lethal targets
    • Chen AY, Liu LF. DNA topoisomerases: essential enzymes and lethal targets. Annu Rev Pharmacol Toxicol 1994; 34: 191-218.
    • (1994) Annu Rev Pharmacol Toxicol , vol.34 , pp. 191-218
    • Chen, A.Y.1    Liu, L.F.2
  • 17
    • 0027413177 scopus 로고
    • Regulation of topoisomerase II by phosphorylation: A role for casein kinase II
    • Cardenas ME, Gasser SM. Regulation of topoisomerase II by phosphorylation: a role for casein kinase II. J Cell Sci 1993; 104 (Part 2): 219-225.
    • (1993) J Cell Sci , vol.104 , Issue.PART 2 , pp. 219-225
    • Cardenas, M.E.1    Gasser, S.M.2
  • 18
    • 0032532041 scopus 로고    scopus 로고
    • Altered expression and activity of topoisome-rases during all-trans retinoic acid-induced differentiation of HL-60 cells
    • Aoyama M, Grabowski DR, Isaacs RJ, Krivacic KA, Rybicki LA, Bukowski RM et al. Altered expression and activity of topoisome-rases during all-trans retinoic acid-induced differentiation of HL-60 cells. Blood 1998; 92: 2863-2870.
    • (1998) Blood , vol.92 , pp. 2863-2870
    • Aoyama, M.1    Grabowski, D.R.2    Isaacs, R.J.3    Krivacic, K.A.4    Rybicki, L.A.5    Bukowski, R.M.6
  • 19
    • 33846631886 scopus 로고    scopus 로고
    • Topoisomerase II binds importin alpha isoforms and exportin/CRM1 but does not shuttle between the nucleus and cytoplasm in proliferating cells
    • Mirski SE, Sparks KE, Friedrich B, Kohler M, Mo YY, Beck WT et al. Topoisomerase II binds importin alpha isoforms and exportin/CRM1 but does not shuttle between the nucleus and cytoplasm in proliferating cells. Exp Cell Res 2007; 313: 627-637.
    • (2007) Exp Cell Res , vol.313 , pp. 627-637
    • Mirski, S.E.1    Sparks, K.E.2    Friedrich, B.3    Kohler, M.4    Mo, Y.Y.5    Beck, W.T.6
  • 20
    • 0034330993 scopus 로고    scopus 로고
    • Altered ligand binding and transcriptional regulation by mutations in the PML/RARalpha ligand-binding domain arising in retinoic acid-resistant patients with acute promyelocytic leukemia
    • Cote S, Zhou D, Bianchini A, Nervi C, Gallagher RE, Miller Jr WH. Altered ligand binding and transcriptional regulation by mutations in the PML/RARalpha ligand-binding domain arising in retinoic acid-resistant patients with acute promyelocytic leukemia. Blood 2000; 96: 3200-3208.
    • (2000) Blood , vol.96 , pp. 3200-3208
    • Cote, S.1    Zhou, D.2    Bianchini, A.3    Nervi, C.4    Gallagher, R.E.5    Miller Jr, W.H.6
  • 21
    • 54049154237 scopus 로고    scopus 로고
    • A novel arsenical has antitumor activity toward As2O3-resistant and MRP1/ABCC1-overexpressing cell lines
    • Diaz Z, Mann KK, Marcoux S, Kourelis M, Colombo M, Komarnitsky PB et al. A novel arsenical has antitumor activity toward As2O3-resistant and MRP1/ABCC1-overexpressing cell lines. Leukemia 2008; 22: 1853-1863.
    • (2008) Leukemia , vol.22 , pp. 1853-1863
    • Diaz, Z.1    Mann, K.K.2    Marcoux, S.3    Kourelis, M.4    Colombo, M.5    Komarnitsky, P.B.6
  • 22
    • 0025009391 scopus 로고
    • Effect of 5-aza-2-deoxycytidine and retinoic acid on differentiation and c-myc expression in HL-60 myeloid leukemic cells
    • Momparler RL, Dore BT, Momparler LF. Effect of 5-aza-2-deoxycytidine and retinoic acid on differentiation and c-myc expression in HL-60 myeloid leukemic cells. Cancer Lett 1990; 54: 21-28.
    • (1990) Cancer Lett , vol.54 , pp. 21-28
    • Momparler, R.L.1    Dore, B.T.2    Momparler, L.F.3
  • 23
    • 33646257584 scopus 로고    scopus 로고
    • Protein kinase C delta activates topoisomerase IIalpha to induce apoptotic cell death in response to DNA damage
    • Yoshida K, Yamaguchi T, Shinagawa H, Taira N, Nakayama KI, Miki Y. Protein kinase C delta activates topoisomerase IIalpha to induce apoptotic cell death in response to DNA damage. Mol Cell Biol 2006; 26: 3414-3431.
    • (2006) Mol Cell Biol , vol.26 , pp. 3414-3431
    • Yoshida, K.1    Yamaguchi, T.2    Shinagawa, H.3    Taira, N.4    Nakayama, K.I.5    Miki, Y.6
  • 24
    • 0025751626 scopus 로고
    • Expression of protein kinase C genes in hemopoietic cells is cell-type-and B cell-differentiation stage specific
    • Mischak H, Kolch W, Goodnight J, Davidson WF, Rapp U, Rose-John S et al. Expression of protein kinase C genes in hemopoietic cells is cell-type-and B cell-differentiation stage specific. J Immunol 1991; 147: 3981-3987.
    • (1991) J Immunol , vol.147 , pp. 3981-3987
    • Mischak, H.1    Kolch, W.2    Goodnight, J.3    Davidson, W.F.4    Rapp, U.5    Rose-John, S.6
  • 26
    • 11244280921 scopus 로고    scopus 로고
    • Retinoic acid mediates degradation of IRS-1 by the ubiquitin-proteasome pathway, via a PKC-dependant mechanism
    • del Rincon SV, Guo Q, Morelli C, Shiu HY, Surmacz E, Miller WH. Retinoic acid mediates degradation of IRS-1 by the ubiquitin-proteasome pathway, via a PKC-dependant mechanism. Onco-gene 2004; 23: 9269-9279.
    • (2004) Onco-gene , vol.23 , pp. 9269-9279
    • Del Rincon, S.V.1    Guo, Q.2    Morelli, C.3    Shiu, H.Y.4    Surmacz, E.5    Miller, W.H.6
  • 28
    • 0030829055 scopus 로고    scopus 로고
    • Isoform specificity of activators and inhibitors of protein kinase C γ and δ
    • DOI 10.1016/S0014-5793(97)01104-6, PII S0014579397011046
    • Keenan C, Goode N, Pears C. Isoform specificity of activators and inhibitors of protein kinase C gamma and delta. FEBS Lett 1997; 415: 101-108. (Pubitemid 27402058)
    • (1997) FEBS Letters , vol.415 , Issue.1 , pp. 101-108
    • Keenan, C.1    Goode, N.2    Pears, C.3
  • 29
    • 0034725570 scopus 로고    scopus 로고
    • Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta
    • Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA et al. Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem 2000; 275: 23065-23073.
    • (2000) J Biol Chem , vol.275 , pp. 23065-23073
    • Frasch, S.C.1    Henson, P.M.2    Kailey, J.M.3    Richter, D.A.4    Janes, M.S.5    Fadok, V.A.6
  • 30
    • 9444260940 scopus 로고    scopus 로고
    • Protein kinase Cdelta mediates retinoic acid and phorbol myristate acetate-induced phospholipid scramblase 1 gene expression: Its role in leukemic cell differentiation
    • Zhao KW, Li X, Zhao Q, Huang Y, Li D, Peng ZG et al. Protein kinase Cdelta mediates retinoic acid and phorbol myristate acetate-induced phospholipid scramblase 1 gene expression: its role in leukemic cell differentiation. Blood 2004; 104: 3731-3738.
    • (2004) Blood , vol.104 , pp. 3731-3738
    • Zhao, K.W.1    Li, X.2    Zhao, Q.3    Huang, Y.4    Li, D.5    Peng, Z.G.6
  • 31
    • 20944452041 scopus 로고    scopus 로고
    • Role of protein kinase C-delta (PKC-delta) in the generation of the effects of IFN-alpha in chronic myelogenous leukemia cells
    • Kaur S, Parmar S, Smith J, Katsoulidis E, Li Y, Sassano A et al. Role of protein kinase C-delta (PKC-delta) in the generation of the effects of IFN-alpha in chronic myelogenous leukemia cells. Exp Hematol 2005; 33: 550-557.
    • (2005) Exp Hematol , vol.33 , pp. 550-557
    • Kaur, S.1    Parmar, S.2    Smith, J.3    Katsoulidis, E.4    Li, Y.5    Sassano, A.6
  • 32
    • 0034911097 scopus 로고    scopus 로고
    • Inhibition of protein kinase C delta has negative effect on anchorage-independent growth of BCR-ABL-transformed Rat1 cells
    • Kin Y, Shibuya M, Maru Y. Inhibition of protein kinase C delta has negative effect on anchorage-independent growth of BCR-ABL-transformed Rat1 cells. Leuk Res 2001; 25: 821-825.
    • (2001) Leuk Res , vol.25 , pp. 821-825
    • Kin, Y.1    Shibuya, M.2    Maru, Y.3
  • 33
    • 19444365828 scopus 로고    scopus 로고
    • The PKC delta inhibitor, rottlerin, induces apoptosis of haematopoietic cell lines through mitochondrial membrane depolarization and caspases' cascade
    • Liao YF, Hung YC, Chang WH, Tsay GJ, Hour TC, Hung HC et al. The PKC delta inhibitor, rottlerin, induces apoptosis of haematopoietic cell lines through mitochondrial membrane depolarization and caspases' cascade. Life Sci 2005; 77: 707-719.
    • (2005) Life Sci , vol.77 , pp. 707-719
    • Liao, Y.F.1    Hung, Y.C.2    Chang, W.H.3    Tsay, G.J.4    Hour, T.C.5    Hung, H.C.6
  • 34
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351 (Part 1): 95-105.
    • (2000) Biochem J , vol.351 , Issue.PART 1 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 35
    • 0033805221 scopus 로고    scopus 로고
    • Rottlerin, a PKC isozyme-selective inhibitor, affects signaling events and cytokine production in human monocytes
    • Kontny E, Kurowska M, Szczepanska K, Maslinski W. Rottlerin, a PKC isozyme-selective inhibitor, affects signaling events and cytokine production in human monocytes. J Leukoc Biol 2000; 67: 249-258.
    • (2000) J Leukoc Biol , vol.67 , pp. 249-258
    • Kontny, E.1    Kurowska, M.2    Szczepanska, K.3    Maslinski, W.4
  • 37
    • 0005123113 scopus 로고
    • Phosphorylation of DNA topoisomerase II by casein kinase II: Modulation of eukaryotic topoisomerase II activity in vitro
    • Ackerman P, Glover CV, Osheroff N. Phosphorylation of DNA topoisomerase II by casein kinase II: modulation of eukaryotic topoisomerase II activity in vitro. Proc Natl Acad Sci USA 1985; 82: 3164-3168.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3164-3168
    • Ackerman, P.1    Glover, C.V.2    Osheroff, N.3
  • 38
    • 0019321213 scopus 로고
    • Decatenation of kinetoplast DNA by topoisomerases
    • Marini JC, Miller KG, Englund PT. Decatenation of kinetoplast DNA by topoisomerases. J Biol Chem 1980; 255: 4976-4979.
    • (1980) J Biol Chem , vol.255 , pp. 4976-4979
    • Marini, J.C.1    Miller, K.G.2    Englund, P.T.3
  • 40
    • 0024453524 scopus 로고
    • In vivo phosphorylation of the 170-kDa form of eukaryotic DNA topoisomerase II. Cell cycle analysis
    • Heck MM, Hittelman WN, Earnshaw WC. In vivo phosphorylation of the 170-kDa form of eukaryotic DNA topoisomerase II. Cell cycle analysis. J Biol Chem 1989; 264: 15161-15164.
    • (1989) J Biol Chem , vol.264 , pp. 15161-15164
    • Heck, M.M.1    Hittelman, W.N.2    Earnshaw, W.C.3
  • 41
    • 0028043440 scopus 로고
    • Identification of the nature of modification that causes the shift of DNA topoisomerase II beta to apparent higher molecular weight forms in the M phase
    • Kimura K, Nozaki N, Saijo M, Kikuchi A, Ui M, Enomoto T. Identification of the nature of modification that causes the shift of DNA topoisomerase II beta to apparent higher molecular weight forms in the M phase. J Biol Chem 1994; 269: 24523-24526.
    • (1994) J Biol Chem , vol.269 , pp. 24523-24526
    • Kimura, K.1    Nozaki, N.2    Saijo, M.3    Kikuchi, A.4    Ui, M.5    Enomoto, T.6
  • 42
    • 0028670198 scopus 로고
    • Phosphorylation of the alpha-and beta-isoforms of DNA topoisomerase II is qualitatively different in interphase and mitosis in Chinese hamster ovary cells
    • Burden DA, Sullivan DM. Phosphorylation of the alpha-and beta-isoforms of DNA topoisomerase II is qualitatively different in interphase and mitosis in Chinese hamster ovary cells. Biochemistry 1994; 33: 14651-14655.
    • (1994) Biochemistry , vol.33 , pp. 14651-14655
    • Burden, D.A.1    Sullivan, D.M.2
  • 43
    • 0028114974 scopus 로고
    • Serine 1524 is a major site of phosphorylation on human topoisomerase II alpha protein in vivo and is a substrate for casein kinase II in vitro
    • Wells NJ, Addison CM, Fry AM, Ganapathi R, Hickson ID. Serine 1524 is a major site of phosphorylation on human topoisomerase II alpha protein in vivo and is a substrate for casein kinase II in vitro. J Biol Chem 1994; 269: 29746-29751.
    • (1994) J Biol Chem , vol.269 , pp. 29746-29751
    • Wells, N.J.1    Addison, C.M.2    Fry, A.M.3    Ganapathi, R.4    Hickson, I.D.5
  • 44
    • 59649117396 scopus 로고    scopus 로고
    • Casein kinase i delta/epsilon phosphorylates topoisomerase IIalpha at serine-1106 and modulates DNA cleavage activity
    • Grozav AG, Chikamori K, Kozuki T, Grabowski DR, Bukowski RM, Willard B et al. Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at serine-1106 and modulates DNA cleavage activity. Nucleic Acids Res 2009; 37: 382-392.
    • (2009) Nucleic Acids Res , vol.37 , pp. 382-392
    • Grozav, A.G.1    Chikamori, K.2    Kozuki, T.3    Grabowski, D.R.4    Bukowski, R.M.5    Willard, B.6
  • 45
    • 44449103826 scopus 로고    scopus 로고
    • Plk1-dependent phosphorylation regulates functions of DNA topoisomerase IIalpha in cell cycle progression
    • Li H, Wang Y, Liu X. Plk1-dependent phosphorylation regulates functions of DNA topoisomerase IIalpha in cell cycle progression. J Biol Chem 2008; 283: 6209-6221.
    • (2008) J Biol Chem , vol.283 , pp. 6209-6221
    • Li, H.1    Wang, Y.2    Liu, X.3
  • 46
    • 0037630385 scopus 로고    scopus 로고
    • Phosphorylation of serine 1106 in the catalytic domain of topoisomerase II alpha regulates enzymatic activity and drug sensitivity
    • Chikamori K, Grabowski DR, Kinter M, Willard BB, Yadav S, Aebersold RH et al. Phosphorylation of serine 1106 in the catalytic domain of topoisomerase II alpha regulates enzymatic activity and drug sensitivity. J Biol Chem 2003; 278: 12696-12702.
    • (2003) J Biol Chem , vol.278 , pp. 12696-12702
    • Chikamori, K.1    Grabowski, D.R.2    Kinter, M.3    Willard, B.B.4    Yadav, S.5    Aebersold, R.H.6
  • 47
    • 0032705595 scopus 로고    scopus 로고
    • Altered drug interaction and regulation of topoisomerase IIbeta: Potential mechanisms governing sensitivity of HL-60 cells to amsacrine and etoposide
    • Grabowski DR, Holmes KA, Aoyama M, Ye Y, Rybicki LA, Bukowski RM et al. Altered drug interaction and regulation of topoisomerase IIbeta: potential mechanisms governing sensitivity of HL-60 cells to amsacrine and etoposide. Mol Pharmacol 1999; 56: 1340-1345.
    • (1999) Mol Pharmacol , vol.56 , pp. 1340-1345
    • Grabowski, D.R.1    Holmes, K.A.2    Aoyama, M.3    Ye, Y.4    Rybicki, L.A.5    Bukowski, R.M.6
  • 48
    • 0034745050 scopus 로고    scopus 로고
    • Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress
    • Buschmann T, Potapova O, Bar-Shira A, Ivanov VN, Fuchs SY, Henderson S et al. Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress. Mol Cell Biol 2001; 21: 2743-2754.
    • (2001) Mol Cell Biol , vol.21 , pp. 2743-2754
    • Buschmann, T.1    Potapova, O.2    Bar-Shira, A.3    Ivanov, V.N.4    Fuchs, S.Y.5    Henderson, S.6
  • 49
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki K, Sagata N. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J 1995; 14: 5048-5059.
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 50
    • 0034698126 scopus 로고    scopus 로고
    • Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy
    • Radominska-Pandya A, Chen G, Czernik PJ, Little JM, Samokyszyn VM, Carter CA et al. Direct interaction of all-trans-retinoic acid with protein kinase C (PKC). Implications for PKC signaling and cancer therapy. J Biol Chem 2000; 275: 22324-22330.
    • (2000) J Biol Chem , vol.275 , pp. 22324-22330
    • Radominska-Pandya, A.1    Chen, G.2    Czernik, P.J.3    Little, J.M.4    Samokyszyn, V.M.5    Carter, C.A.6
  • 51
    • 0032528172 scopus 로고    scopus 로고
    • Retinoic acid induced mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest
    • Yen A, Roberson MS, Varvayanis S, Lee AT. Retinoic acid induced mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest. Cancer Res 1998; 58: 3163-3172.
    • (1998) Cancer Res , vol.58 , pp. 3163-3172
    • Yen, A.1    Roberson, M.S.2    Varvayanis, S.3    Lee, A.T.4
  • 52
    • 0036240711 scopus 로고    scopus 로고
    • Importance of MEK-1/-2 signaling in monocytic and granulocytic differentiation of myeloid cell lines
    • Miranda MB, McGuire TF, Johnson DE. Importance of MEK-1/-2 signaling in monocytic and granulocytic differentiation of myeloid cell lines. Leukemia 2002; 16: 683-692.
    • (2002) Leukemia , vol.16 , pp. 683-692
    • Miranda, M.B.1    McGuire, T.F.2    Johnson, D.E.3
  • 53
    • 0035830842 scopus 로고    scopus 로고
    • Activation of Rac1 and the p38 mitogen-activated protein kinase pathway in response to all-trans-retinoic acid
    • Alsayed Y, Uddin S, Mahmud N, Lekmine F, Kalvakolanu DV, Minucci S et al. Activation of Rac1 and the p38 mitogen-activated protein kinase pathway in response to all-trans-retinoic acid. J Biol Chem 2001; 276: 4012-4019.
    • (2001) J Biol Chem , vol.276 , pp. 4012-4019
    • Alsayed, Y.1    Uddin, S.2    Mahmud, N.3    Lekmine, F.4    Kalvakolanu, D.V.5    Minucci, S.6
  • 54
    • 62649160930 scopus 로고    scopus 로고
    • Epidermal growth factor-dependent cyclooxygenase-2 induction in gliomas requires protein kinase C-delta
    • Xu K, Chang CM, Gao H, Shu HK. Epidermal growth factor-dependent cyclooxygenase-2 induction in gliomas requires protein kinase C-delta. Oncogene 2009; 28: 1410-1420.
    • (2009) Oncogene , vol.28 , pp. 1410-1420
    • Xu, K.1    Chang, C.M.2    Gao, H.3    Shu, H.K.4
  • 55
    • 19944427098 scopus 로고    scopus 로고
    • Identification of new classes among acute myelogenous leukaemias with normal karyotype using gene expression profiling
    • Vey N, Mozziconacci MJ, Groulet-Martinec A, Debono S, Finetti P, Carbuccia N et al. Identification of new classes among acute myelogenous leukaemias with normal karyotype using gene expression profiling. Oncogene 2004; 23: 9381-9391.
    • (2004) Oncogene , vol.23 , pp. 9381-9391
    • Vey, N.1    Mozziconacci, M.J.2    Groulet-Martinec, A.3    Debono, S.4    Finetti, P.5    Carbuccia, N.6
  • 56
    • 33847185954 scopus 로고    scopus 로고
    • Gene expression profiling of B lymphocytes and plasma cells from Waldenstrom's macroglobulinemia: Comparison with expression patterns of the same cell counterparts from chronic lymphocytic leukemia, multiple myeloma and normal individuals
    • Gutierrez NC, Ocio EM, de Las Rivas J, Maiso P, Delgado M, Ferminan E et al. Gene expression profiling of B lymphocytes and plasma cells from Waldenstrom's macroglobulinemia: comparison with expression patterns of the same cell counterparts from chronic lymphocytic leukemia, multiple myeloma and normal individuals. Leukemia 2007; 21: 541-549.
    • (2007) Leukemia , vol.21 , pp. 541-549
    • Gutierrez, N.C.1    Ocio, E.M.2    De Las Rivas, J.3    Maiso, P.4    Delgado, M.5    Ferminan, E.6
  • 57
    • 0028048465 scopus 로고
    • Topoisomerase II alpha expression in acute myeloid leukaemia and its relationship to clinical outcome
    • McKenna SL, West RR, Whittaker JA, Padua RA, Holmes JA. Topoisomerase II alpha expression in acute myeloid leukaemia and its relationship to clinical outcome. Leukemia 1994; 8: 1498-1502.
    • (1994) Leukemia , vol.8 , pp. 1498-1502
    • McKenna, S.L.1    West, R.R.2    Whittaker, J.A.3    Padua, R.A.4    Holmes, J.A.5
  • 58
    • 0033957570 scopus 로고    scopus 로고
    • Modulation of DNA topoisomerase II activity and expression in melanoma cells with acquired drug resistance
    • Lage H, Helmbach H, Dietel M, Schadendorf D. Modulation of DNA topoisomerase II activity and expression in melanoma cells with acquired drug resistance. Br J Cancer 2000; 82: 488-491.
    • (2000) Br J Cancer , vol.82 , pp. 488-491
    • Lage, H.1    Helmbach, H.2    Dietel, M.3    Schadendorf, D.4
  • 59
    • 0032222419 scopus 로고    scopus 로고
    • Absence of topoisomerase IIbeta in an amsacrine-resistant human leukemia cell line with mutant topoisomerase IIalpha
    • Herzog CE, Holmes KA, Tuschong LM, Ganapathi R, Zwelling LA. Absence of topoisomerase IIbeta in an amsacrine-resistant human leukemia cell line with mutant topoisomerase IIalpha. Cancer Res 1998; 58: 5298-5300.
    • (1998) Cancer Res , vol.58 , pp. 5298-5300
    • Herzog, C.E.1    Holmes, K.A.2    Tuschong, L.M.3    Ganapathi, R.4    Zwelling, L.A.5
  • 60
    • 33744991353 scopus 로고    scopus 로고
    • Topoisomerase IIalpha gene amplification and response to anthracycline-containing adjuvant chemotherapy in breast cancer
    • Buzdar AU. Topoisomerase IIalpha gene amplification and response to anthracycline-containing adjuvant chemotherapy in breast cancer. J Clin Oncol 2006; 24: 2409-2411.
    • (2006) J Clin Oncol , vol.24 , pp. 2409-2411
    • Buzdar, A.U.1
  • 61
    • 0030825408 scopus 로고    scopus 로고
    • Molecular remission in PML/RAR alpha-positive acute promyelocytic leukemia by combined all-trans retinoic acid and idarubicin (AIDA) therapy
    • Gruppo Italiano-Malattie Ematologiche Maligne dell'Adulto and Associazione Italiana di Ematologia ed Oncologia Pediatrica Cooperative Groups
    • Mandelli F, Diverio D, Avvisati G, Luciano A, Barbui T, Bernasconi C et al. Molecular remission in PML/RAR alpha-positive acute promyelocytic leukemia by combined all-trans retinoic acid and idarubicin (AIDA) therapy. Gruppo Italiano-Malattie Ematologiche Maligne dell'Adulto and Associazione Italiana di Ematologia ed Oncologia Pediatrica Cooperative Groups. Blood 1997; 90: 1014-1021.
    • (1997) Blood , vol.90 , pp. 1014-1021
    • Mandelli, F.1    Diverio, D.2    Avvisati, G.3    Luciano, A.4    Barbui, T.5    Bernasconi, C.6
  • 62
    • 18744374448 scopus 로고    scopus 로고
    • RAR agonists stimulate SOX9 gene expression in breast cancer cell lines: Evidence for a role in retinoid-mediated growth inhibition
    • Afonja O, Raaka BM, Huang A, Das S, Zhao X, Helmer E et al. RAR agonists stimulate SOX9 gene expression in breast cancer cell lines: evidence for a role in retinoid-mediated growth inhibition. Oncogene 2002; 21: 7850-7860.
    • (2002) Oncogene , vol.21 , pp. 7850-7860
    • Afonja, O.1    Raaka, B.M.2    Huang, A.3    Das, S.4    Zhao, X.5    Helmer, E.6
  • 63
    • 0242389807 scopus 로고    scopus 로고
    • C/EBPbeta: A major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells
    • Duprez E, Wagner K, Koch H, Tenen DG. C/EBPbeta: a major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells. EMBO J 2003; 22: 5806-5816.
    • (2003) EMBO J , vol.22 , pp. 5806-5816
    • Duprez, E.1    Wagner, K.2    Koch, H.3    Tenen, D.G.4
  • 64
    • 0029432726 scopus 로고
    • Antiproliferative actions of insulin-like growth factor binding protein (IGFBP)-3 in human breast cancer cells
    • Oh Y, Gucev Z, Ng L, Muller HL, Rosenfeld RG. Antiproliferative actions of insulin-like growth factor binding protein (IGFBP)-3 in human breast cancer cells. Prog Growth Factor Res 1995; 6: 503-512.
    • (1995) Prog Growth Factor Res , vol.6 , pp. 503-512
    • Oh, Y.1    Gucev, Z.2    Ng, L.3    Muller, H.L.4    Rosenfeld, R.G.5
  • 65
    • 0033768476 scopus 로고    scopus 로고
    • Defect in the regulation of 4E-BP1 and 2, two repressors of translation initiation, in the retinoid acid resistant cell lines, NB4-R1 and NB4-R2
    • Grolleau A, Wietzerbin J, Beretta L. Defect in the regulation of 4E-BP1 and 2, two repressors of translation initiation, in the retinoid acid resistant cell lines, NB4-R1 and NB4-R2. Leukemia 2000; 14: 1909-1914.
    • (2000) Leukemia , vol.14 , pp. 1909-1914
    • Grolleau, A.1    Wietzerbin, J.2    Beretta, L.3
  • 66
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcrip-tional activation by nuclear receptors and other regulated transcription factors
    • Perissi V, Aggarwal A, Glass CK, Rose DW, Rosenfeld MG. A corepressor/coactivator exchange complex required for transcrip-tional activation by nuclear receptors and other regulated transcription factors. Cell 2004; 116: 511-526.
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 67
    • 5644293177 scopus 로고    scopus 로고
    • Molecular interaction of retinoic acid receptors with coregulators PCAF and RIP140
    • Chen Y, Hu X, Wei LN. Molecular interaction of retinoic acid receptors with coregulators PCAF and RIP140. Mol Cell Endocrinol 2004; 226: 43-50.
    • (2004) Mol Cell Endocrinol , vol.226 , pp. 43-50
    • Chen, Y.1    Hu, X.2    Wei, L.N.3
  • 68
    • 64949159656 scopus 로고    scopus 로고
    • The Ski protein can inhibit ligand induced RARalpha and HDAC3 degradation in the retinoic acid signaling pathway
    • Zhao HL, Ueki N, Marcelain K, Hayman MJ. The Ski protein can inhibit ligand induced RARalpha and HDAC3 degradation in the retinoic acid signaling pathway. Biochem Biophys Res Commun 2009; 383: 119-124.
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 119-124
    • Zhao, H.L.1    Ueki, N.2    Marcelain, K.3    Hayman, M.J.4


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