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Volumn 66, Issue 8, 2006, Pages 4368-4377

Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CAMBINOL; ETOPOSIDE; HEAT SHOCK PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NSC 112546; PACLITAXEL; PROTEIN BCL 6; PROTEIN P53; SILENT INFORMATION REGULATOR PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 1; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTUIN; TRICHOSTATIN A; TUBULIN; UNCLASSIFIED DRUG;

EID: 33646254136     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-3617     Document Type: Article
Times cited : (444)

References (56)
  • 1
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 2000;64:435-59.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 3
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000; 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 4
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
    • U S A
    • Tanner KG, Landry J, Sternglanz R, Denu JM. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci U S A 2000;97:14178-82.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 7
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′ -O-acetyl ADP ribose and histone peptide
    • Camb
    • Zhao K, Chai X, Marmorstein R. Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′ -O-acetyl ADP ribose and histone peptide. Structure (Camb) 2003;11:1403-11.
    • (2003) Structure , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 8
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM. Crystal structure of a SIR2 homolog-NAD complex. Cell 2001;105:269-79.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 9
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • North BJ, Verdin E. Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol 2004;5:224-30.
    • (2004) Genome Biol , vol.5 , pp. 224-230
    • North, B.J.1    Verdin, E.2
  • 10
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G, Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem 2004;73:417-35.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 11
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye RA. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 2000;273:793-8.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 12
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E, et al. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 2001;107:149-59.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3
  • 13
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell 2001;107:137-48.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3
  • 14
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • Cohen HY, Lavu S, Bitterman KJ, et al. Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. Mol Cell 2004;13:627-38.
    • (2004) Mol Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3
  • 15
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004;303:2011-5.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 16
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki T, Sasaki Y, Milbrandt J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 2004;305:1010-3.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 17
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, et al. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 2004;305:390-2.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3
  • 18
    • 0036898253 scopus 로고    scopus 로고
    • Acetylation inactivates the transcriptional repressor BCL6
    • Bereshchenko OR, Gu W, Dalla-Favera R. Acetylation inactivates the transcriptional repressor BCL6. Nat Genet 2002;32:606-13.
    • (2002) Nat Genet , vol.32 , pp. 606-613
    • Bereshchenko, O.R.1    Gu, W.2    Dalla-Favera, R.3
  • 19
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M, Schiltz RL, Iezzi S, et al. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 2003;12:51-62.
    • (2003) Mol Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3
  • 20
    • 3042681042 scopus 로고    scopus 로고
    • Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
    • Picard F, Kurtev M, Chung N, et al. Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature 2004;429:771-6.
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1    Kurtev, M.2    Chung, N.3
  • 21
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD dependent tubulin deacetylase. Mol Cell 2003;11:437-44.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 22
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B, North BJ, Frye RA, Ott M, Verdin E. The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 2002;158:647-57.
    • (2002) J Cell Biol , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 23
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997;90:595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 24
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama A, Shimazu T, Sumida Y, et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J 2002;21:6820-31.
    • (2002) EMBO J , vol.21 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3
  • 26
    • 0036301281 scopus 로고    scopus 로고
    • Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms
    • Sandor V, Bakke S, Robey RW, et al. Phase I trial of the histone deacetylase inhibitor, depsipeptide (FR901228, NSC 630176), in patients with refractory neoplasms. Clin Cancer Res 2002;8:718-28.
    • (2002) Clin Cancer Res , vol.8 , pp. 718-728
    • Sandor, V.1    Bakke, S.2    Robey, R.W.3
  • 27
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • Piekarz RL, Robey R, Sandor V, et al. Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: a case report. Blood 2001;98:2865-8.
    • (2001) Blood , vol.98 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3
  • 28
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • U S A
    • Cheng HL, Mostoslavsky R, Saito S, et al. Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc Natl Acad Sci U S A 2003;100:10794-9.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3
  • 29
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2α protein has a role in embryogenesis and gametogenesis
    • McBurney MW, Yang X, Jardine K, et al. The mammalian SIR2α protein has a role in embryogenesis and gametogenesis. Mol Cell Biol 2003;23:38-54.
    • (2003) Mol Cell Biol , vol.23 , pp. 38-54
    • McBurney, M.W.1    Yang, X.2    Jardine, K.3
  • 31
    • 0346101749 scopus 로고    scopus 로고
    • +-dependent deacetylases using phenotypic screens in yeast
    • +-dependent deacetylases using phenotypic screens in yeast. J Biol Chem 2003;278:52773-82.
    • (2003) J Biol Chem , vol.278 , pp. 52773-52782
    • Hirao, M.1    Posakony, J.2    Nelson, M.3
  • 33
    • 0141781063 scopus 로고    scopus 로고
    • NAD-dependent deacetylase Hst1p controls biosynthesis and cellular NAD levels in Saccharomyces cerevisiae
    • Bedalov A, Hirao M, Posakony J, Nelson M, Simon J. NAD-dependent deacetylase Hst1p controls biosynthesis and cellular NAD levels in Saccharomyces cerevisiae. Mol Cell Biol 2003;23:7044-54.
    • (2003) Mol Cell Biol , vol.23 , pp. 7044-7054
    • Bedalov, A.1    Hirao, M.2    Posakony, J.3    Nelson, M.4    Simon, J.5
  • 34
    • 5644236831 scopus 로고    scopus 로고
    • Identification and characterization of Sir2 inhibitors through phenotypic assays in yeast
    • Posakony J, Hirao M, Bedalov A. Identification and characterization of Sir2 inhibitors through phenotypic assays in yeast. Comb Chem High Throughput Screen 2004;7:661-8.
    • (2004) Comb Chem High Throughput Screen , vol.7 , pp. 661-668
    • Posakony, J.1    Hirao, M.2    Bedalov, A.3
  • 35
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J Biol Chem 2001;276:38837-43.
    • (2001) J Biol Chem , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 36
    • 0038152845 scopus 로고    scopus 로고
    • Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a
    • Castrillon DH, Miao L, Kollipara R, Horner JW, DePinho RA. Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a. Science 2003;301:215-8.
    • (2003) Science , vol.301 , pp. 215-218
    • Castrillon, D.H.1    Miao, L.2    Kollipara, R.3    Horner, J.W.4    Depinho, R.A.5
  • 37
    • 5344280456 scopus 로고    scopus 로고
    • MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation
    • Fujita N, Jaye DL, Geigerman C, et al. MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation. Cell 2004;119:75-86.
    • (2004) Cell , vol.119 , pp. 75-86
    • Fujita, N.1    Jaye, D.L.2    Geigerman, C.3
  • 38
    • 0035016355 scopus 로고    scopus 로고
    • Thymidine incorporation is highly predictive of colony formation and can be used for high throughput screening
    • Lamb JR, Goehle S, Ludlow C, Simon JA. Thymidine incorporation is highly predictive of colony formation and can be used for high throughput screening. Biotechniques 2001;30:1118-20.
    • (2001) Biotechniques , vol.30 , pp. 1118-1120
    • Lamb, J.R.1    Goehle, S.2    Ludlow, C.3    Simon, J.A.4
  • 39
    • 0024847290 scopus 로고
    • What is synergy?
    • Berenbaum MC. What is synergy? Pharmacol Rev 1989;41:93-141.
    • (1989) Pharmacol Rev , vol.41 , pp. 93-141
    • Berenbaum, M.C.1
  • 40
    • 0042161855 scopus 로고    scopus 로고
    • BCL6 controls the expression of the B7-1/CD80 costimulatory receptor in germinal center B cells
    • Niu H, Cattoretti G, Dalla-Favera R. BCL6 controls the expression of the B7-1/CD80 costimulatory receptor in germinal center B cells. J Exp Med 2003;198:211-21.
    • (2003) J Exp Med , vol.198 , pp. 211-221
    • Niu, H.1    Cattoretti, G.2    Dalla-Favera, R.3
  • 41
    • 10344247666 scopus 로고    scopus 로고
    • The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B cells
    • Phan RT, Dalla-Favera R. The BCL6 proto-oncogene suppresses p53 expression in germinal-centre B cells. Nature 2004;432:635-9.
    • (2004) Nature , vol.432 , pp. 635-639
    • Phan, R.T.1    Dalla-Favera, R.2
  • 42
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, Guardiola A, Shao R, et al. HDAC6 is a microtubule-associated deacetylase. Nature 2002;417:455-8.
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 43
    • 0023293040 scopus 로고
    • Microtubules containing acetylated α-tubulin in mammalian cells in culture
    • Piperno G, LeDizet M, Chang XJ. Microtubules containing acetylated α-tubulin in mammalian cells in culture. J Cell Biol 1987;104:289-302.
    • (1987) J Cell Biol , vol.104 , pp. 289-302
    • Piperno, G.1    LeDizet, M.2    Chang, X.J.3
  • 44
    • 0027319521 scopus 로고
    • p53 is required for radiation-induced apoptosis in mouse thymocytes
    • Lowe SW, Schmitt EM, Smith SW, Osborne BA, Jacks T. p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 1993;362:847-9.
    • (1993) Nature , vol.362 , pp. 847-849
    • Lowe, S.W.1    Schmitt, E.M.2    Smith, S.W.3    Osborne, B.A.4    Jacks, T.5
  • 45
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata M, Sasaki MS, Sonoda E, et al. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J 1998;17:5497-508.
    • (1998) EMBO J , vol.17 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3
  • 48
    • 18244408596 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes
    • Costanzo A, Merlo P, Pediconi N, et al. DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes. Mol Cell 2002;9:175-86.
    • (2002) Mol Cell , vol.9 , pp. 175-186
    • Costanzo, A.1    Merlo, P.2    Pediconi, N.3
  • 50
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-κB action regulated by reversible acetylation
    • Chen LF, Fischle W, Verdin E, Greene WC. Duration of nuclear NF-κB action regulated by reversible acetylation. Science 2001;293:1653-7.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.F.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 51
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, et al. Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 2004;23:2369-80.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 53
    • 0027495491 scopus 로고
    • Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-cell lymphoma
    • Ye BH, Lista F, Lo Coco F, et al. Alterations of a zinc finger-encoding gene, BCL-6, in diffuse large-cell lymphoma. Science 1993;262:747-50.
    • (1993) Science , vol.262 , pp. 747-750
    • Ye, B.H.1    Lista, F.2    Lo Coco, F.3
  • 54
    • 11144277489 scopus 로고    scopus 로고
    • Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells
    • Polo JM, Dell'oso T, Ranuncolo SM, et al. Specific peptide interference reveals BCL6 transcriptional and oncogenic mechanisms in B-cell lymphoma cells. Nat Med 2004;10:1329-35.
    • (2004) Nat Med , vol.10 , pp. 1329-1335
    • Polo, J.M.1    Dell'oso, T.2    Ranuncolo, S.M.3
  • 55
    • 1642430733 scopus 로고    scopus 로고
    • Myc pathways provoking cell suicide and cancer
    • Nilsson JA, Cleveland JL. Myc pathways provoking cell suicide and cancer. Oncogene 2003;22:9007-21.
    • (2003) Oncogene , vol.22 , pp. 9007-9021
    • Nilsson, J.A.1    Cleveland, J.L.2
  • 56
    • 0037087737 scopus 로고    scopus 로고
    • A senescence rescue screen identifies BCL6 as an inhibitor of anti-proliferative p19(ARF)-p53 signaling
    • Shvarts A, Brummelkamp TR, Scheeren F, et al. A senescence rescue screen identifies BCL6 as an inhibitor of anti-proliferative p19(ARF)-p53 signaling. Genes Dev 2002;16:681-6.
    • (2002) Genes Dev , vol.16 , pp. 681-686
    • Shvarts, A.1    Brummelkamp, T.R.2    Scheeren, F.3


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