메뉴 건너뛰기




Volumn 69, Issue 1, 2006, Pages 288-298

Erratum: Flavopiridol and histone deacetylase inhibitors promote mitochondrial injury and cell death in human leukemia cells that overexpress Bcl-2 (Molecular Pharmacology (2006) 69 (288–298) DOI: 10.1124/mol.105.016154);Flavopiridol and histone deacetylase inhibitors promote mitochondrial injury and cell death in human leukemia cells that overexpress Bcl-2

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; CASPASE; CYCLIN DEPENDENT KINASE INHIBITOR; CYTARABINE; FLAVOPIRIDOL; HISTONE DEACETYLASE INHIBITOR; PROTEIN BCL 2; PROTEIN BCL XL; VORINOSTAT;

EID: 30044436031     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.105.016154retraction     Document Type: Erratum
Times cited : (46)

References (40)
  • 1
    • 0034644659 scopus 로고    scopus 로고
    • Bcl-2 independence of flavopiridol-induced apoptosis. Mitochondrial depolarization in the absence of cytochrome c release
    • Achenbach TV, Muller R, and Slater EP (2000) Bcl-2 independence of flavopiridol-induced apoptosis. Mitochondrial depolarization in the absence of cytochrome c release. J Biol Chem 275:32089-32097.
    • (2000) J Biol Chem , vol.275 , pp. 32089-32097
    • Achenbach, T.V.1    Muller, R.2    Slater, E.P.3
  • 2
    • 0036050151 scopus 로고    scopus 로고
    • Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA)
    • Almenara J, Rosato R, and Grant S (2002) Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA). Leukemia 16:1331-1343.
    • (2002) Leukemia , vol.16 , pp. 1331-1343
    • Almenara, J.1    Rosato, R.2    Grant, S.3
  • 3
    • 0036122494 scopus 로고    scopus 로고
    • Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity
    • Bjerling P, Silverstein RA, Thon G, Caudy A, Grewal S, and Ekwall K (2002) Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity. Mol Cell Biol 22:2170-2181.
    • (2002) Mol Cell Biol , vol.22 , pp. 2170-2181
    • Bjerling, P.1    Silverstein, R.A.2    Thon, G.3    Caudy, A.4    Grewal, S.5    Ekwall, K.6
  • 5
    • 0029665778 scopus 로고    scopus 로고
    • Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (CDK) 2 and CDK4 in human breast carcinoma cells
    • Carlson BA, Dubay MM, Sausville EA, Brizuela L, and Worland PJ (1996) Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (CDK) 2 and CDK4 in human breast carcinoma cells. Cancer Res 56:2973-2978.
    • (1996) Cancer Res , vol.56 , pp. 2973-2978
    • Carlson, B.A.1    Dubay, M.M.2    Sausville, E.A.3    Brizuela, L.4    Worland, P.J.5
  • 6
    • 0036259143 scopus 로고    scopus 로고
    • Synergistic induction of apoptosis in human myeloid leukemia cells by phorbol 12-myristate 13-acetate and flavopiridol proceeds via activation of both the intrinsic and tumor necrosis factor-mediated extrinsic cell death pathways
    • Cartee L, Smith R, Dai Y, Rahmani M, Rosato R, Almenara J, Dent P, and Grant S (2002) Synergistic induction of apoptosis in human myeloid leukemia cells by phorbol 12-myristate 13-acetate and flavopiridol proceeds via activation of both the intrinsic and tumor necrosis factor-mediated extrinsic cell death pathways. Mol Pharmacol 61:1313-1321.
    • (2002) Mol Pharmacol , vol.61 , pp. 1313-1321
    • Cartee, L.1    Smith, R.2    Dai, Y.3    Rahmani, M.4    Rosato, R.5    Almenara, J.6    Dent, P.7    Grant, S.8
  • 7
    • 0035943710 scopus 로고    scopus 로고
    • Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo
    • Chao SH and Price DH (2001) Flavopiridol inactivates P-TEFb and blocks most RNA polymerase II transcription in vivo. J Biol Chem 276:31793-31799.
    • (2001) J Biol Chem , vol.276 , pp. 31793-31799
    • Chao, S.H.1    Price, D.H.2
  • 8
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, and Korsmeyer SJ (2001) BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 8:705-711.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 9
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control and cancer
    • Cress WD and Seto E (2000) Histone deacetylases, transcriptional control and cancer. J Cell Physiol 184:1-16.
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 10
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial NN and Korsmeyer SJ (2004) Cell death: critical control points. Cell 116:205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 11
    • 0036490982 scopus 로고    scopus 로고
    • Loss of the Bcl-2 phosphorylation loop domain is required to protect human myeloid leukemia cells from flavopiridol-mediated mitochondrial damage and apoptosis
    • Decker RH, Wang S, Dai Y, Dent P, and Grant S (2002) Loss of the Bcl-2 phosphorylation loop domain is required to protect human myeloid leukemia cells from flavopiridol-mediated mitochondrial damage and apoptosis. Cancer Biol Ther 1:136-144.
    • (2002) Cancer Biol Ther , vol.1 , pp. 136-144
    • Decker, R.H.1    Wang, S.2    Dai, Y.3    Dent, P.4    Grant, S.5
  • 12
    • 0343457526 scopus 로고    scopus 로고
    • Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A
    • Deng X, Ito T, Carr B, Mumby M, and May WS Jr (1998) Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. J Biol Chem 273:34157-34163.
    • (1998) J Biol Chem , vol.273 , pp. 34157-34163
    • Deng, X.1    Ito, T.2    Carr, B.3    Mumby, M.4    May Jr., W.S.5
  • 14
    • 14044276343 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors down-regulate Bcl-2 expression and induce apoptosis in t(14;18) lymphomas
    • Duan H, Heckman CA, and Boxer LM (2005) Histone deacetylase inhibitors down-regulate Bcl-2 expression and induce apoptosis in t(14;18) lymphomas. Mol Cell Biol 25:1608-1619.
    • (2005) Mol Cell Biol , vol.25 , pp. 1608-1619
    • Duan, H.1    Heckman, C.A.2    Boxer, L.M.3
  • 15
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • Edinger AL and Thompson CB (2004) Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol 16:663-669.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 16
    • 20844444898 scopus 로고    scopus 로고
    • Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3
    • George P, Bali P, Annavarapu S, Scuto A, Fiskus W, Guo F, Sigua C, Sondarva G, Moscinski L, Atadja P, et al. (2005) Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood 105:1768-1776.
    • (2005) Blood , vol.105 , pp. 1768-1776
    • George, P.1    Bali, P.2    Annavarapu, S.3    Scuto, A.4    Fiskus, W.5    Guo, F.6    Sigua, C.7    Sondarva, G.8    Moscinski, L.9    Atadja, P.10
  • 17
    • 0036850211 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1
    • Gojo I, Zhang B, and Fenton RG (2002) The cyclin-dependent kinase inhibitor flavopiridol induces apoptosis in multiple myeloma cells through transcriptional repression and down-regulation of Mcl-1. Clin Cancer Res 8:3527-3538.
    • (2002) Clin Cancer Res , vol.8 , pp. 3527-3538
    • Gojo, I.1    Zhang, B.2    Fenton, R.G.3
  • 18
    • 0034525374 scopus 로고    scopus 로고
    • The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
    • Harris MH and Thompson CB (2000) The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability. Cell Death Differ 7:1182-1191.
    • (2000) Cell Death Differ , vol.7 , pp. 1182-1191
    • Harris, M.H.1    Thompson, C.B.2
  • 19
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-xL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu D, Inohara N, and Nunez G (1998) Bcl-xL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci USA 95:4386-4391.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 22
    • 0034615860 scopus 로고    scopus 로고
    • Failure of Bcl-2 to block cytochrome c redistribution during TRAIL-induced apoptosis
    • Keogh SA, Walczak H, Bouchier-Hayes L, and Martin SJ (2000) Failure of Bcl-2 to block cytochrome c redistribution during TRAIL-induced apoptosis. FEBS Lett 471:93-98.
    • (2000) FEBS Lett , vol.471 , pp. 93-98
    • Keogh, S.A.1    Walczak, H.2    Bouchier-Hayes, L.3    Martin, S.J.4
  • 23
    • 9444222718 scopus 로고    scopus 로고
    • Critical role of reactive oxygen species and mitochondrial membrane potential in Korean mistletoe lectin-induced apoptosis in human hepatocarcinoma cells
    • Kim WH, Park WB, Gao B, and Jung MH (2004) Critical role of reactive oxygen species and mitochondrial membrane potential in Korean mistletoe lectin-induced apoptosis in human hepatocarcinoma cells. Mol Pharmacol 66:1383-1396.
    • (2004) Mol Pharmacol , vol.66 , pp. 1383-1396
    • Kim, W.H.1    Park, W.B.2    Gao, B.3    Jung, M.H.4
  • 24
    • 0037380209 scopus 로고    scopus 로고
    • Histone acetylation and deacetylation in yeast
    • Kurdistani SK and Grunstein M (2003) Histone acetylation and deacetylation in yeast. Nat Rev Mol Cell Biol 4:276-284.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 276-284
    • Kurdistani, S.K.1    Grunstein, M.2
  • 25
    • 0141757205 scopus 로고    scopus 로고
    • Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia
    • Liu FT, Newland AC, and Jia L (2003) Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia. Biochem Biophys Res Commun 310:956-962.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 956-962
    • Liu, F.T.1    Newland, A.C.2    Jia, L.3
  • 26
    • 23744480886 scopus 로고    scopus 로고
    • Leukemia fusion proteins and co-repressor complexes: Changing paradigms
    • Redner RL and Liu JM (2005) Leukemia fusion proteins and co-repressor complexes: changing paradigms. J Cell Biochem 94:864-869.
    • (2005) J Cell Biochem , vol.94 , pp. 864-869
    • Redner, R.L.1    Liu, J.M.2
  • 27
    • 8844228917 scopus 로고    scopus 로고
    • Potent antileukemic interactions between flavopiridol and TRAIL/Apo2L involve flavopiridol-mediated XIAP downregulation
    • Rosato RR, Dai Y, Almenara JA, Maggio SC, and Grant S (2004) Potent antileukemic interactions between flavopiridol and TRAIL/Apo2L involve flavopiridol-mediated XIAP downregulation. Leukemia 18:1780-1788.
    • (2004) Leukemia , vol.18 , pp. 1780-1788
    • Rosato, R.R.1    Dai, Y.2    Almenara, J.A.3    Maggio, S.C.4    Grant, S.5
  • 28
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli AA, Ausserlechner MJ, Bernhard D, Sutton VR, Tainton KM, Kofler R, Smyth MJ, and Johnstone RW (2001) The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc Natl Acad Sci USA 98:10833-10838.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Smyth, M.J.7    Johnstone, R.W.8
  • 29
    • 0033375469 scopus 로고    scopus 로고
    • Flavopiridol: The first cyclin-dependent kinase inhibitor in human clinical trials
    • Senderowicz AM (1999) Flavopiridol: the first cyclin-dependent kinase inhibitor in human clinical trials. Investig New Drugs 17:313-320.
    • (1999) Investig New Drugs , vol.17 , pp. 313-320
    • Senderowicz, A.M.1
  • 30
    • 1042278138 scopus 로고    scopus 로고
    • Flavopiridol inhibits NF-κB activation induced by various carcinogens and inflammatory agents through inhibition of IκBα kinase and p65 phosphorylation: Abrogation of cyclin D1, cyclooxygenase-2 and matrix metalloprotease-9
    • Takada Y and Aggarwal BB (2004) Flavopiridol inhibits NF-κB activation induced by various carcinogens and inflammatory agents through inhibition of IκBα kinase and p65 phosphorylation: abrogation of cyclin D1, cyclooxygenase-2 and matrix metalloprotease-9. J Biol Chem 279:4750-4759.
    • (2004) J Biol Chem , vol.279 , pp. 4750-4759
    • Takada, Y.1    Aggarwal, B.B.2
  • 31
    • 0034670161 scopus 로고    scopus 로고
    • Potentiation of 1-beta-D-arabinofuranosylcytosine-mediated mitochondrial damage and apoptosis in human leukemia cells (U937) overexpressing bcl-2 by the kinase inhibitor 7-hydroxystaurosporine (UCN-01)
    • Tang L, Boise LH, Dent P, and Grant S (2000) Potentiation of 1-beta-D-arabinofuranosylcytosine-mediated mitochondrial damage and apoptosis in human leukemia cells (U937) overexpressing bcl-2 by the kinase inhibitor 7-hydroxystaurosporine (UCN-01). Biochem Pharmacol 60:1445-1456.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1445-1456
    • Tang, L.1    Boise, L.H.2    Dent, P.3    Grant, S.4
  • 32
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-xL, c-Jun and p21CIP1, but independent of p53
    • Vrana JA, Decker RH, Johnson CR, Wang Z, Jarvis WD, Richon VM, Ehinger M, Fisher PB, and Grant S (1999) Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-xL, c-Jun and p21CIP1, but independent of p53. Oncogene 18:7016-7025.
    • (1999) Oncogene , vol.18 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3    Wang, Z.4    Jarvis, W.D.5    Richon, V.M.6    Ehinger, M.7    Fisher, P.B.8    Grant, S.9
  • 33
    • 0031469395 scopus 로고    scopus 로고
    • Agents that down-regulate or inhibit protein kinase C circumvent resistance to 1-β-D-arabinofuranosylcytosine-induced apoptosis in human leukemia cells that overexpress Bcl-2
    • Wang S, Vrana JA, Bartimole TM, Freemerman AJ, Jarvis WD, Kramer LB, Krystal G, Dent P, and Grant S (1997) Agents that down-regulate or inhibit protein kinase C circumvent resistance to 1-β-D-arabinofuranosylcytosine- induced apoptosis in human leukemia cells that overexpress Bcl-2. Mol Pharmacol 52:1000-1009.
    • (1997) Mol Pharmacol , vol.52 , pp. 1000-1009
    • Wang, S.1    Vrana, J.A.2    Bartimole, T.M.3    Freemerman, A.J.4    Jarvis, W.D.5    Kramer, L.B.6    Krystal, G.7    Dent, P.8    Grant, S.9
  • 34
    • 0033609299 scopus 로고    scopus 로고
    • Loss of the Bcl-2 phosphorylation loop domain increases resistance of human leukemia cells (U937) to paclitaxel-mediated mitochondrial dysfunction and apoptosis
    • Wang S, Wang Z, Boise L, Dent P, and Grant S (1999a) Loss of the Bcl-2 phosphorylation loop domain increases resistance of human leukemia cells (U937) to paclitaxel-mediated mitochondrial dysfunction and apoptosis. Biochem Biophys Res Commun 259:67-72.
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 67-72
    • Wang, S.1    Wang, Z.2    Boise, L.3    Dent, P.4    Grant, S.5
  • 35
    • 0032876984 scopus 로고    scopus 로고
    • Bryostatin 1 enhances paclitaxel-induced mitochondrial dysfunction and apoptosis in human leukemia cells (U937) ectopically expressing Bcl-xL
    • Wang S, Wang Z, Boise LH, Dent P, and Grant S (1999b) Bryostatin 1 enhances paclitaxel-induced mitochondrial dysfunction and apoptosis in human leukemia cells (U937) ectopically expressing Bcl-xL. Leukemia 13:1564-1573.
    • (1999) Leukemia , vol.13 , pp. 1564-1573
    • Wang, S.1    Wang, Z.2    Boise, L.H.3    Dent, P.4    Grant, S.5
  • 36
    • 0036830438 scopus 로고    scopus 로고
    • Bcl-xL protects BimEL-induced Bax conformational change and cytochrome C release independent of interacting with Bax or BimEL
    • Yamaguchi H and Wang HG (2002) Bcl-xL protects BimEL-induced Bax conformational change and cytochrome C release independent of interacting with Bax or BimEL. J Biol Chem 277:41604-41612.
    • (2002) J Biol Chem , vol.277 , pp. 41604-41612
    • Yamaguchi, H.1    Wang, H.G.2
  • 38
    • 0028818126 scopus 로고
    • BCL-2 expression delays drug-induced apoptosis but does not increase clonogenic survival after drug treatment in HeLa cells
    • Yin DX and Schimke RT (1995) BCL-2 expression delays drug-induced apoptosis but does not increase clonogenic survival after drug treatment in HeLa cells. Cancer Res 55:4922-4928.
    • (1995) Cancer Res , vol.55 , pp. 4922-4928
    • Yin, D.X.1    Schimke, R.T.2
  • 39
    • 0242493856 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571
    • Yu C, Rahmani M, Conrad D, Subler M, Dent P, and Grant S (2003) The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571. Blood 102:3765-3774.
    • (2003) Blood , vol.102 , pp. 3765-3774
    • Yu, C.1    Rahmani, M.2    Conrad, D.3    Subler, M.4    Dent, P.5    Grant, S.6
  • 40
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha H, Aime-Sempe C, Sato T, and Reed JC (1996) Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem 271:7440-7444.
    • (1996) J Biol Chem , vol.271 , pp. 7440-7444
    • Zha, H.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.