메뉴 건너뛰기




Volumn 442, Issue 3, 2012, Pages 693-701

Oligoamine analogues in combination with 2-difluoromethylornithine synergistically induce re-expression of aberrantly silenced tumour-suppressor genes

Author keywords

Epigenetic; Histone; Lysine specific demethylase 1 (LSD1); Ornithine decarboxylase; Polyamine

Indexed keywords

EFLORNITHINE; LYSINE SPECIFIC DEMETHYLASE 1; POLYAMINE DERIVATIVE; SECRETED FRIZZLED RELATED PROTEIN 2; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 84863232569     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111271     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 33644846509 scopus 로고    scopus 로고
    • Epigenetic gene silencing in cancer - A mechanism for early oncogenic pathway addiction?
    • DOI 10.1038/nrc1799, PII N1799
    • Baylin, S. B. and Ohm, J. E. (2006) Epigenetic gene silencing in cancer: a mechanism for early oncogenic pathway addiction? Nat. Rev. Cancer 6, 107-116 (Pubitemid 43361543)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.2 , pp. 107-116
    • Baylin, S.B.1    Ohm, J.E.2
  • 3
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic Regulation of Histone Lysine Methylation by Demethylases
    • DOI 10.1016/j.molcel.2006.12.010, PII S1097276506008689
    • Shi, Y. and Whetstine, J. R. (2007) Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25, 1-14 (Pubitemid 46049067)
    • (2007) Molecular Cell , vol.25 , Issue.1 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 4
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A. and Casero, R. A. (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953 (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 5
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • DOI 10.1038/nature04021, PII N04021
    • Lee, M. G., Wynder, C., Cooch, N. and Shiekhattar, R. (2005) An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 437, 432-435 (Pubitemid 41613507)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 6
    • 77449090884 scopus 로고    scopus 로고
    • Polyamine analogues targeting epigenetic gene regulation
    • Huang, Y., Marton, L. J., Woster, P. M. and Casero, R. A. (2009) Polyamine analogues targeting epigenetic gene regulation. Essays Biochem. 46, 95-110
    • (2009) Essays Biochem. , vol.46 , pp. 95-110
    • Huang, Y.1    Marton, L.J.2    Woster, P.M.3    Casero, R.A.4
  • 8
    • 77954691054 scopus 로고    scopus 로고
    • (Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators
    • Sharma, S. K., Wu, Y., Steinbergs, N., Crowley, M. L., Hanson, A. S., Casero, R. A. and Woster, P. M. (2010) (Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators. J. Med. Chem. 53, 5197-5212
    • (2010) J. Med. Chem. , vol.53 , pp. 5197-5212
    • Sharma, S.K.1    Wu, Y.2    Steinbergs, N.3    Crowley, M.L.4    Hanson, A.S.5    Casero, R.A.6    Woster, P.M.7
  • 9
    • 84861715426 scopus 로고    scopus 로고
    • Polyamine analogues modulate gene expression by inhibiting lysine-specific dementhylase 1 (LSD1) and altering chromatin structure in human breast cancer cells
    • doi:10.1007/s00726-011-1004-1
    • Zhu, Q., Huang, Y., Marton, L. J., Woster, P. M., Davidson, N. E. and Casero, R. A. (2011) Polyamine analogues modulate gene expression by inhibiting lysine-specific dementhylase 1 (LSD1) and altering chromatin structure in human breast cancer cells. Amino Acids, doi:10.1007/s00726-011-1004-1
    • (2011) Amino Acids
    • Zhu, Q.1    Huang, Y.2    Marton, L.J.3    Woster, P.M.4    Davidson, N.E.5    Casero, R.A.6
  • 11
    • 34248228763 scopus 로고    scopus 로고
    • Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases
    • DOI 10.1038/nrd2243, PII NRD2243
    • Casero, Jr., R. and Marton, L. (2007) Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases. Nat. Rev. Drug Discov. 6, 373-390 (Pubitemid 46705201)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.5 , pp. 373-390
    • Casero, R.A.1    Marton, L.J.2
  • 12
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryotes
    • Pegg, A. E. (1986) Recent advances in the biochemistry of polyamines in eukaryotes. Biochem. J. 234, 249-262
    • (1986) Biochem. J. , vol.234 , pp. 249-262
    • Pegg, A.E.1
  • 13
    • 0033956687 scopus 로고    scopus 로고
    • The physiological role of the polyamines
    • Wallace, H. M. (2000) The physiological role of the polyamines. Eur. J. Clin. Invest. 30, 1-3
    • (2000) Eur. J. Clin. Invest. , vol.30 , pp. 1-3
    • Wallace, H.M.1
  • 14
    • 0037398881 scopus 로고    scopus 로고
    • Polyamines and their role in human disease: An introduction
    • Wallace, H. M. (2003) Polyamines and their role in human disease: an introduction. Biochem. Soc. Trans. 31, 354-355
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 354-355
    • Wallace, H.M.1
  • 15
    • 0018097605 scopus 로고
    • Anti-proliferative properties of DL-α-difluoromethyl ornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylase
    • DOI 10.1016/0006-291X(78)91630-3
    • Mamont, P. S., Duchesne, M. C., Grove, J. and Bey, P. (1978) Anti-proliferative properties of DL-α-difluoromethyl ornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylase. Biochem. Biophys. Res. Commun. 81, 58-66 (Pubitemid 8307801)
    • (1978) Biochemical and Biophysical Research Communications , vol.81 , Issue.1 , pp. 58-66
    • Mamont, P.S.1    Duchesne, M.-C.2    Grove, J.3    Bey, P.4
  • 16
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann, P. P. and Pegg, A. E. (1992) Ornithine decarboxylase as an enzyme target for therapy. Pharmacol. Ther. 54, 195-215
    • (1992) Pharmacol. Ther. , vol.54 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 17
    • 0022490910 scopus 로고
    • Solid-phase extraction and determination of dansyl derivatives of unconjugated and acetylated polyamines by reversed-phase liquid chromatography: Improved separation systems for polyamines in cerebrospinal fluid, urine and tissue
    • Kabra, P. M., Lee, H. K., Lubich, W. P. and Marton, L. J. (1986) Solid-phase extraction and determination of dansyl derivatives of unconjugated and acetylated polyamines by reversed-phase liquid chromatography: improved separation systems for polyamines in cerebrospinal fluid, urine and tissue. J. Chromatogr. 380, 19-32 (Pubitemid 16049858)
    • (1986) Journal of Chromatography - Biomedical Applications , vol.380 , Issue.1 , pp. 19-32
    • Kabra, P.M.1    Lee, H.K.2    Lubich, W.P.3    Marton, L.J.4
  • 19
    • 0025253542 scopus 로고
    • Molecular mechanics of the interactions of spermine with DNA: DNA bending as a result of ligand binding
    • Feuerstein, B. G., Pattabiraman, N. and Marton, L. J. (1990) Molecular mechanics of the interactions of spermine with DNA: DNA bending as a result of ligand binding. Nucleic Acids Res. 18, 1271-1282
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1271-1282
    • Feuerstein, B.G.1    Pattabiraman, N.2    Marton, L.J.3
  • 20
    • 0035804314 scopus 로고    scopus 로고
    • Terminally alkylated polyamine analogues as chemotherapeutic agents
    • DOI 10.1021/jm000084m
    • Casero, Jr., R. A. and Woster, P. M. (2001) Terminally alkylated polyamine analogues as chemotherapeutic agents. J. Med. Chem. 44, 1-26 (Pubitemid 32049778)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.1 , pp. 1-26
    • Casero Jr., R.A.1    Woster, P.M.2
  • 21
    • 34547691625 scopus 로고    scopus 로고
    • Antizyme and antizyme inhibitor activities influence cellular responses to polyamine analogs
    • DOI 10.1007/s00726-007-0523-2, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Mitchell, J. L., Thane, T. K., Sequeira, J. M., Marton, L. J. and Thokala, R. (2007) Antizyme and antizyme inhibitor activities influence cellular responses to polyamine analogs. Amino Acids 33, 291-297 (Pubitemid 47222969)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 291-297
    • Mitchell, J.L.A.1    Thane, T.K.2    Sequeira, J.M.3    Marton, L.J.4    Thokala, R.5
  • 23
    • 0036613250 scopus 로고    scopus 로고
    • A genomic screen for genes upregulated by demethylation and histone deacetylase inhibition in human colorectal cancer
    • Suzuki, H., Gabrielson, E., Chen, W., Anbazhagan, R., van Engeland, M., Weijenberg, M., Herman, J. and Baylin, S. (2002) A genomic screen for genes upregulated by demethylation and histone deacetylase inhibition in human colorectal cancer. Nat. Genet. 31, 141-149
    • (2002) Nat. Genet. , vol.31 , pp. 141-149
    • Suzuki, H.1    Gabrielson, E.2    Chen, W.3    Anbazhagan, R.4    Van Engeland, M.5    Weijenberg, M.6    Herman, J.7    Baylin, S.8
  • 24
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • Lee, M. G., Wynder, C., Schmidt, D. M., McCafferty, D. G. and Shiekhattar, R. (2006) Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem. Biol. 13, 563-567
    • (2006) Chem. Biol. , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhattar, R.5
  • 25
    • 34147173308 scopus 로고    scopus 로고
    • trans-2-phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1
    • DOI 10.1021/bi0618621
    • Schmidt, D. M. and McCafferty, D. G. (2007) trans-2- Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1. Biochemistry 46, 4408-4416 (Pubitemid 46559406)
    • (2007) Biochemistry , vol.46 , Issue.14 , pp. 4408-4416
    • Schmidt, D.M.Z.1    McCafferty, D.G.2
  • 26
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine
    • DOI 10.1021/bi700664y
    • Yang, M., Culhane, J. C., Szewczuk, L. M., Jalili, P., Ball, H. L., Machius, M., Cole, P. A. and Yu, H. (2007) Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2- phenylcyclopropylamine. Biochemistry 46, 8058-8065 (Pubitemid 47051641)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 8058-8065
    • Yang, M.1    Culhane, J.C.2    Szewczuk, L.M.3    Jalili, P.4    Ball, H.L.5    Machius, M.6    Cole, P.A.7    Yu, H.8
  • 27
    • 1542285163 scopus 로고    scopus 로고
    • A concerted DNA methylation/histone methylation switch regulates rRNA gene dosage control and nucleolar dominance
    • DOI 10.1016/S1097-2765(04)00064-4, PII S1097276504000644
    • Lawrence, R. J., Earley, K., Pontes, O., Silva, M., Chen, Z. J., Neves, N., Viegas, W. and Pikaard, C. S. (2004) A concerted DNA methylation/histone methylation switch regulates rRNA gene dosage control and nucleolar dominance. Mol. Cell 13, 599-609 (Pubitemid 38299386)
    • (2004) Molecular Cell , vol.13 , Issue.4 , pp. 599-609
    • Lawrence, R.J.1    Earley, K.2    Pontes, O.3    Silva, M.4    Chen, Z.J.5    Neves, N.6    Viegas, W.7    Pikaard, C.S.8
  • 28
    • 0020482713 scopus 로고
    • Effect of inhibition of polyamine synthesis on the content of decarboxylated S-adenosylmethionine
    • Pegg, A. E., Poso, H., Shuttleworth, K. and Bennett, R. A. (1982) Effect of inhibition of polyamine synthesis on the content of decarboxylated S-adenosylmethionine. Biochem. J. 202, 519-526
    • (1982) Biochem. J. , vol.202 , pp. 519-526
    • Pegg, A.E.1    Poso, H.2    Shuttleworth, K.3    Bennett, R.A.4
  • 29
    • 0031058038 scopus 로고    scopus 로고
    • Interference with DNA methyltransferase activity and genome methylation during F9 teratocarcinoma stem cell differentiation induced by polyamine depletion
    • DOI 10.1074/jbc.272.7.4359
    • Frostesjo, L., Holm, I., Grahn, B., Page, A. W., Bestor, T. H. and Heby, O. (1997) Interference with DNA methyltransferase activity and genome methylation during F9 teratocarcinoma stem cell differentiation induced by polyamine depletion. J. Biol. Chem. 272, 4359-4366 (Pubitemid 27078511)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 4359-4366
    • Frostesjo, L.1    Holm, I.2    Grahn, B.3    Page, A.W.4    Bestor, T.H.5    Heby, O.6
  • 30
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein, T. and Allis, C. D. (2001) Translating the histone code. Science 293, 1074-1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 31
    • 33847065486 scopus 로고    scopus 로고
    • The Epigenomics of Cancer
    • DOI 10.1016/j.cell.2007.01.029, PII S0092867407001274
    • Jones, P. A. and Baylin, S. B. (2007) The epigenomics of cancer. Cell 128, 683-692 (Pubitemid 46273572)
    • (2007) Cell , vol.128 , Issue.4 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 32
    • 62849104641 scopus 로고    scopus 로고
    • Efficacy of azacitidine compared with that of conventional care regimens in the treatment of higher-risk myelodysplastic syndromes: A randomised, open-label, phase III study
    • Fenaux, P., Mufti, G. J., Hellstrom-Lindberg, E., Santini, V., Finelli, C., Giagounidis, A., Schoch, R., Gattermann, N., Sanz, G., List, A. et al. (2009) Efficacy of azacitidine compared with that of conventional care regimens in the treatment of higher-risk myelodysplastic syndromes: a randomised, open-label, phase III study. Lancet Oncol. 10, 223-232
    • (2009) Lancet Oncol. , vol.10 , pp. 223-232
    • Fenaux, P.1    Mufti, G.J.2    Hellstrom-Lindberg, E.3    Santini, V.4    Finelli, C.5    Giagounidis, A.6    Schoch, R.7    Gattermann, N.8    Sanz, G.9    List, A.10
  • 36
    • 34547400070 scopus 로고    scopus 로고
    • Polyamine analogues: Potent inducers of nucleosomal array oligomerization and inhibitors of yeast cell growth
    • DOI 10.1042/BJ20061347
    • Carruthers, L. M., Marton, L. J. and Peterson, C. L. (2007) Polyamine analogues: potent inducers of nucleosomal array oligomerization and inhibitors of yeast cell growth. Biochem. J. 405, 541-545 (Pubitemid 47172052)
    • (2007) Biochemical Journal , vol.405 , Issue.3 , pp. 541-545
    • Carruthers, L.M.1    Marton, L.J.2    Peterson, C.L.3
  • 37
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor- dependent transcription
    • DOI 10.1038/nature04020, PII N04020
    • Metzger, E., Wissmann, M., Yin, N., Muller, J. M., Schneider, R., Peters, A. H., Gunther, T., Buettner, R. and Schule, R. (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437, 436-439 (Pubitemid 41613508)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5    Peters, A.H.F.M.6    Gunther, T.7    Buettner, R.8    Schule, R.9
  • 40
    • 77950868547 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology
    • Lim, S., Janzer, A., Becker, A., Zimmer, A., Schule, R., Buettner, R. and Kirfel, J. (2010) Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology. Carcinogenesis 31, 512-520
    • (2010) Carcinogenesis , vol.31 , pp. 512-520
    • Lim, S.1    Janzer, A.2    Becker, A.3    Zimmer, A.4    Schule, R.5    Buettner, R.6    Kirfel, J.7
  • 42
    • 77958610739 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme induces hypomethylation of genome DNA and histone H3 lysine 9 dimethylation (H3K9me2) in human oral cancer cell line
    • Yamamoto, D., Shima, K., Matsuo, K., Nishioka, T., Chen, C. Y., Hu, G. F., Sasaki, A. and Tsuji, T. (2010) Ornithine decarboxylase antizyme induces hypomethylation of genome DNA and histone H3 lysine 9 dimethylation (H3K9me2) in human oral cancer cell line. PLoS ONE 5, e12554
    • (2010) PLoS ONE , vol.5
    • Yamamoto, D.1    Shima, K.2    Matsuo, K.3    Nishioka, T.4    Chen, C.Y.5    Hu, G.F.6    Sasaki, A.7    Tsuji, T.8
  • 44
    • 0036142967 scopus 로고    scopus 로고
    • Deregulation of polyamine biosynthesis alters intrinsic histone acetyltransferase and deacetylase activities in murine skin and tumors
    • Hobbs, C. A., Paul, B. A. and Gilmour, S. K. (2002) Deregulation of polyamine biosynthesis alters intrinsic histone acetyltransferase and deacetylase activities in murine skin and tumors. Cancer Res. 62, 67-74 (Pubitemid 34073988)
    • (2002) Cancer Research , vol.62 , Issue.1 , pp. 67-74
    • Hobbs, C.A.1    Paul, B.A.2    Gilmour, S.K.3
  • 45
    • 0142121430 scopus 로고    scopus 로고
    • Elevated levels of polyamines alter chromatin in murine skin and tumors without global changes in nucleosome acetylation
    • DOI 10.1016/S0014-4827(03)00352-5
    • Hobbs, C. A., Paul, B. A. and Gilmour, S. K. (2003) Elevated levels of polyamines alter chromatin in murine skin and tumors without global changes in nucleosome acetylation. Exp. Cell Res. 290, 427-436 (Pubitemid 37272185)
    • (2003) Experimental Cell Research , vol.290 , Issue.2 , pp. 427-436
    • Hobbs, C.A.1    Paul, B.A.2    Gilmour, S.K.3
  • 46
    • 34547899201 scopus 로고    scopus 로고
    • Polyamine-mediated regulation of protein acetylation in murine skin and tumors
    • DOI 10.1002/mc.20350
    • Wei, G., Hobbs, C. A., Defeo, K., Hayes, C. S. and Gilmour, S. K. (2007) Polyamine-mediated regulation of protein acetylation in murine skin and tumors. Mol. Carcinog. 46, 611-617 (Pubitemid 47255176)
    • (2007) Molecular Carcinogenesis , vol.46 , Issue.8 , pp. 611-617
    • Wei, G.1    Hobbs, C.A.2    DeFeo, K.3    Hayes, C.S.4    Gilmour, S.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.