메뉴 건너뛰기




Volumn 1238, Issue , 2015, Pages 677-688

Recent progress in the discovery of epigenetic inhibitors for the treatment of cancer

(1)  Verma, Sharad K a  

a NONE

Author keywords

Chromatin; Epigenetics; Histone methyltransferases; Nucleosome; Posttranslational modifi cation; S Adenosylmethionine (SAM)

Indexed keywords

HISTONE LYSINE METHYLTRANSFERASE; HISTONE LYSINE METHYLTRANSFERASE DOT1L; HISTONE LYSINE METHYLTRANSFERASE EZH2; HISTONE METHYLTRANSFERASE INHIBITOR; METHYLTRANSFERASE INHIBITOR; UNCLASSIFIED DRUG; DOT1L PROTEIN, HUMAN; EZH2 PROTEIN, HUMAN; METHYLTRANSFERASE; POLYCOMB REPRESSIVE COMPLEX 2;

EID: 84955379914     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-1804-1_35     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 0003964363 scopus 로고    scopus 로고
    • American Cancer Society, American Cancer Society, Atlanta
    • American Cancer Society (2013) Cancer Facts & Figures 2013. American Cancer Society, Atlanta
    • (2013) Cancer Facts & Figures , pp. 2013
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifi cations and their function
    • Kouzarides T (2007) Chromatin modifi cations and their function. Cell 128:693–705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB (2007) The epigenomics of cancer. Cell 128:683–692
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 4
    • 58849092225 scopus 로고    scopus 로고
    • Epigenetic control of T-helper-cell differentiation
    • Wilson CB, Rowell E, Sekimata M (2009) Epigenetic control of T-helper-cell differentiation. Nat Rev Immunol 9:91–105
    • (2009) Nat Rev Immunol , vol.9 , pp. 91-105
    • Wilson, C.B.1    Rowell, E.2    Sekimata, M.3
  • 6
    • 84874789539 scopus 로고    scopus 로고
    • Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics
    • Copeland RA, Moyer MP, Richon VM (2013) Targeting genetic alterations in protein methyltransferases for personalized cancer therapeutics. Oncogene 32:939–946
    • (2013) Oncogene , vol.32 , pp. 939-946
    • Copeland, R.A.1    Moyer, M.P.2    Richon, V.M.3
  • 7
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland RA, Solomon ME, Richon VM (2009) Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov 8:724–732
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 8
    • 55949136562 scopus 로고    scopus 로고
    • Roles of the EZH2 histone methyltransferase in cancer epigenetics
    • Simon JA, Lange CA (2008) Roles of the EZH2 histone methyltransferase in cancer epigenetics. Mutat Res 647:21–29
    • (2008) Mutat Res , vol.647 , pp. 21-29
    • Simon, J.A.1    Lange, C.A.2
  • 9
    • 34147149505 scopus 로고    scopus 로고
    • Structural dynamics of protein lysine methylation and demethylation
    • Cheng X, Zhang X (2007) Structural dynamics of protein lysine methylation and demethylation. Mutat Res 618:102–115
    • (2007) Mutat Res , vol.618 , pp. 102-115
    • Cheng, X.1    Zhang, X.2
  • 10
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon SC, Zhang X, Trievel RC (2005) The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 6:227
    • (2005) Genome Biol , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3
  • 11
    • 58149239686 scopus 로고    scopus 로고
    • Genomic loss of microRNA-101 leads to overexpression of histone methyltransferase EZH2 in cancer
    • Varambally S, Cao Q, Ram-Shankar M et al (2008) Genomic loss of microRNA-101 leads to overexpression of histone methyltransferase EZH2 in cancer. Science 322:1695–1699
    • (2008) Science , vol.322 , pp. 1695-1699
    • Varambally, S.1    Cao, Q.2    Ram-shankar, M.3
  • 12
    • 18644382388 scopus 로고    scopus 로고
    • The polycomb group protein EZH2 is involved in progression of prostate cancer
    • Varambally S, Dhanasekaran S, Zhou M et al (2002) The polycomb group protein EZH2 is involved in progression of prostate cancer. Nature 419:624–629
    • (2002) Nature , vol.419 , pp. 624-629
    • Varambally, S.1    Dhanasekaran, S.2    Zhou, M.3
  • 13
    • 0141816752 scopus 로고    scopus 로고
    • EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
    • Kleer CG, Cao Q, Varambally S et al (2003) EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells. Proc Natl Acad Sci U S A 100:11606–11611
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11606-11611
    • Kleer, C.G.1    Cao, Q.2    Varambally, S.3
  • 14
    • 77957282672 scopus 로고    scopus 로고
    • Enhancer of zeste homolog 2 (EZH2) expression is an independent prognostic factor in renal cell carcinoma
    • Wagener N et al (2010) Enhancer of zeste homolog 2 (EZH2) expression is an independent prognostic factor in renal cell carcinoma. BMC Cancer 10:524
    • (2010) BMC Cancer , vol.10 , pp. 524
    • Wagener, N.1
  • 15
    • 79959267832 scopus 로고    scopus 로고
    • Validation of the histone methyltransferase EZH2 as a therapeutic target for various types of human cancer and as a prognostic marker
    • Takawa M, Masuda K, Kunizaki M et al (2011) Validation of the histone methyltransferase EZH2 as a therapeutic target for various types of human cancer and as a prognostic marker. Cancer Sci 102:1298–1305
    • (2011) Cancer Sci , vol.102 , pp. 1298-1305
    • Takawa, M.1    Masuda, K.2    Kunizaki, M.3
  • 16
    • 80052029516 scopus 로고    scopus 로고
    • Frequent mutation of histonemodifying genes in non-Hodgkin lymphoma
    • Morin RD, Mendez-Lago M, Mungall AJ et al (2011) Frequent mutation of histonemodifying genes in non-Hodgkin lymphoma. Nature 476:298–303
    • (2011) Nature , vol.476 , pp. 298-303
    • Morin, R.D.1    Mendez-lago, M.2    Mungall, A.J.3
  • 17
    • 75749124332 scopus 로고    scopus 로고
    • Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin
    • Morin RD, Johnson NA, Severson TM et al (2010) Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin. Nat Genet 42:181–185
    • (2010) Nat Genet , vol.42 , pp. 181-185
    • Morin, R.D.1    Johnson, N.A.2    Severson, T.M.3
  • 18
    • 80052269038 scopus 로고    scopus 로고
    • Analysis of the coding genome of diffuse large B-cell lymphoma
    • Pasqualucci L, Trifonov V, Fabbri G et al (2011) Analysis of the coding genome of diffuse large B-cell lymphoma. Nat Genet 43:830–837
    • (2011) Nat Genet , vol.43 , pp. 830-837
    • Pasqualucci, L.1    Trifonov, V.2    Fabbri, G.3
  • 19
    • 84863165348 scopus 로고    scopus 로고
    • Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)
    • McCabe MT, Graves AP, Ganji G et al (2012) Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27). Proc Natl Acad Sci U S A 109: 2989–2994
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 2989-2994
    • Mc cabe, M.T.1    Graves, A.P.2    Ganji, G.3
  • 20
    • 78650454078 scopus 로고    scopus 로고
    • Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas
    • Sneeringer CJ, Scott MP, Kuntz KW et al (2010) Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas. Proc Natl Acad Sci U S A 107:20980–20985
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20980-20985
    • Sneeringer, C.J.1    Scott, M.P.2    Kuntz, K.W.3
  • 21
    • 80053279825 scopus 로고    scopus 로고
    • The Y641C mutation of EZH2 alters substrate specifi city for histone H3 lysine 27 methylation states
    • Wigle TJ, Knutson SK, Jin L et al (2011) The Y641C mutation of EZH2 alters substrate specifi city for histone H3 lysine 27 methylation states. FEBS Lett 585:3011–3014
    • (2011) FEBS Lett , vol.585 , pp. 3011-3014
    • Wigle, T.J.1    Knutson, S.K.2    Jin, L.3
  • 22
    • 79952167230 scopus 로고    scopus 로고
    • Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation
    • Yap DB, Chu J, Berg T et al (2011) Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation. Blood 117:2451–2459
    • (2011) Blood , vol.117 , pp. 2451-2459
    • Yap, D.B.1    Chu, J.2    Berg, T.3
  • 23
    • 77955085750 scopus 로고    scopus 로고
    • Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders
    • Ernst T, Chase AJ, Score J et al (2010) Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders. Nat Genet 42:722–726
    • (2010) Nat Genet , vol.42 , pp. 722-726
    • Ernst, T.1    Chase, A.J.2    Score, J.3
  • 24
    • 67649371461 scopus 로고    scopus 로고
    • DZNep is a global histone methylation inhibitor that reactivates developmental genes not silenced by DNA methylation
    • Miranda TB, Cortez C, Yoo C et al (2009) DZNep is a global histone methylation inhibitor that reactivates developmental genes not silenced by DNA methylation. Mol Cancer Ther 8:1579–1588
    • (2009) Mol Cancer Ther , vol.8 , pp. 1579-1588
    • Miranda, T.B.1    Cortez, C.2    Yoo, C.3
  • 25
    • 0021227696 scopus 로고
    • A potent inhibitor of S-adenosylhomocysteine hydrolase and of vaccinia virus multiplication in mouse L929 cells
    • Borchardt RT, Keller BT, Patel-Thombre U, Neplanocin A (1984) A potent inhibitor of S-adenosylhomocysteine hydrolase and of vaccinia virus multiplication in mouse L929 cells. J Biol Chem 259:4353–4358
    • (1984) J Biol Chem , vol.259 , pp. 4353-4358
    • Borchardt, R.T.1    Keller, B.T.2    Patel-thombre, U.3    Neplanocin, A.4
  • 26
    • 0031934077 scopus 로고    scopus 로고
    • Biological effects of inhibitors of S-adenosylhomocysteine hydrolase
    • Chiang PK (1998) Biological effects of inhibitors of S-adenosylhomocysteine hydrolase. Pharmacol Ther 77:115–134
    • (1998) Pharmacol Ther , vol.77 , pp. 115-134
    • Chiang, P.K.1
  • 27
    • 84871248432 scopus 로고    scopus 로고
    • Identifi cation of potent, selective, cell-active inhibitors of the histone lysine methyltransferase EZH2
    • Verma SK, Tian X, LaFrance LV et al (2012) Identifi cation of potent, selective, cell-active inhibitors of the histone lysine methyltransferase EZH2. ACS Med Chem Lett 3(12): 1091–1096
    • (2012) ACS Med Chem Lett , vol.3 , Issue.12 , pp. 1091-1096
    • Verma, S.K.1    Tian, X.2    Lafrance, L.V.3
  • 28
    • 84921745409 scopus 로고    scopus 로고
    • http://www.thesgc.org/scientists/chemical_probes
  • 29
    • 84870573126 scopus 로고    scopus 로고
    • EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
    • McCabe MT, Ott HM, Ganji G et al (2012) EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature 492:108–112
    • (2012) Nature , vol.492 , pp. 108-112
    • Mc cabe, M.T.1    Ott, H.M.2    Ganji, G.3
  • 30
    • 84871841675 scopus 로고    scopus 로고
    • Selective inhibition of EZH2 by a small molecule inhibitor blocks tumor cells proliferation
    • Qi W, Chan H, Teng L et al (2012) Selective inhibition of EZH2 by a small molecule inhibitor blocks tumor cells proliferation. Proc Natl Acad Sci U S A 109(52):21360–21365
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.52 , pp. 21360-21365
    • Qi, W.1    Chan, H.2    Teng, L.3
  • 31
    • 84867632489 scopus 로고    scopus 로고
    • A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
    • Knutson S, Wigle TJ, Warholic NM et al (2012) A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells. Nat Chem Biol 8:890–896
    • (2012) Nat Chem Biol , vol.8 , pp. 890-896
    • Knutson, S.1    Wigle, T.J.2    Warholic, N.M.3
  • 32
    • 84898034702 scopus 로고    scopus 로고
    • Discovery and optimization of tetramethylpiperidine benzamides as inhibitors of EZH2
    • Nasveschuk CG, Gagnon A, Garapaty-Rao S et al (2014) Discovery and optimization of tetramethylpiperidine benzamides as inhibitors of EZH2. ACS Med Chem Lett 5:378-383
    • (2014) ACS Med Chem Lett , vol.5 , pp. 378-383
    • Nasveschuk, C.G.1    Gagnon, A.2    Garapaty-rao, S.3
  • 33
    • 84888303259 scopus 로고    scopus 로고
    • Identifi cation of EZH2 and EZH1 small molecule inhibitors with selective impact on diffuse large B cell lymphoma cell growth
    • Garapaty-Rao S, Nasvechuk C, Gagnon A et al (2013) Identifi cation of EZH2 and EZH1 small molecule inhibitors with selective impact on diffuse large B cell lymphoma cell growth. Chem Biol 20:1–11
    • (2013) Chem Biol , vol.20 , pp. 1-11
    • Garapaty-rao, S.1    Nasvechuk, C.2    Gagnon, A.3
  • 35
    • 84921782415 scopus 로고    scopus 로고
    • A phase I open-label, dose escalation study to investigate the safety, pharmacokinetics
    • pharmacodynamics and clinical activity of GSK2816126 in subjects with relapsed/refractory diffuse large, NCT02082977
    • A phase I open-label, dose escalation study to investigate the safety, pharmacokinetics, pharmacodynamics and clinical activity of GSK2816126 in subjects with relapsed/refractory diffuse large B cell and transformed follicular lymphoma. NCT02082977
    • B cell and transformed follicular lymphoma
  • 36
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH et al (2013) Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 12:1052–1058
    • (2013) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3
  • 37
    • 79960058024 scopus 로고    scopus 로고
    • Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor
    • Daigle SR, Olhava EJ, Therkelsen CA et al (2011) Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor. Cancer Cell 20:53–65
    • (2011) Cancer Cell , vol.20 , pp. 53-65
    • Daigle, S.R.1    Olhava, E.J.2    Therkelsen, C.A.3
  • 38
    • 79960044951 scopus 로고    scopus 로고
    • MLL-rearranged leukemia is dependent on aberrant H3K79 methylation by DOT1LL
    • Bernt KM, Zhu N, Sinha AU et al (2011) MLL-rearranged leukemia is dependent on aberrant H3K79 methylation by DOT1LL. Cancer Cell 20:66–78
    • (2011) Cancer Cell , vol.20 , pp. 66-78
    • Bernt, K.M.1    Zhu, N.2    Sinha, A.U.3
  • 39
    • 84886864184 scopus 로고    scopus 로고
    • Potent inhibition of DOT1L as treatment of MLL-fusion leukemia
    • Daigle SR, Olhava EJ, Therkelsen CA et al (2013) Potent inhibition of DOT1L as treatment of MLL-fusion leukemia. Blood 122:1017–1025
    • (2013) Blood , vol.122 , pp. 1017-1025
    • Daigle, S.R.1    Olhava, E.J.2    Therkelsen, C.A.3
  • 40
    • 84921726350 scopus 로고    scopus 로고
    • http://clinicaltrials.gov/ct2/show/NCT01 684150?term=mixed+lineage+leukemia&ran k=1
  • 41
    • 84884532954 scopus 로고    scopus 로고
    • Targeted disruption of the EZH2–EED complex inhib- its EZH2-dependent cancer
    • Kim W, Bird G, Neff T et al (2013) Targeted disruption of the EZH2–EED complex inhib- its EZH2-dependent cancer. Nat Chem Biol 9:643–650
    • (2013) Nat Chem Biol , vol.9 , pp. 643-650
    • Kim, W.1    Bird, G.2    Neff, T.3
  • 42
    • 84884567164 scopus 로고    scopus 로고
    • Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer
    • Verma SK, Kinght SD (2013) Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer. Future Med Chem 5:1661–1670
    • (2013) Future Med Chem , vol.5 , pp. 1661-1670
    • Verma, S.K.1    Kinght, S.D.2
  • 43
    • 59649090382 scopus 로고    scopus 로고
    • N-benzyl-1-heteroaryl-3-(trifluoromethyl)- 1H-pyrazole-5-carboxamides as Inhibitors of co-activator associated arginine methyltransferase 1 (CARM1)
    • Allan M, Manku S, Therrien E et al (2009) N-benzyl-1-heteroaryl-3-(trifluoromethyl)- 1H-pyrazole-5-carboxamides as Inhibitors of co-activator associated arginine methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19: 1218–1223
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 1218-1223
    • Allan, M.1    Manku, S.2    Therrien, E.3
  • 44
    • 73249124141 scopus 로고    scopus 로고
    • Discovery of a 2,4-diamino-7- aminoalkoxy quinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a
    • Liu F, Chen X, Allali-Hassani A et al (2009) Discovery of a 2,4-diamino-7- aminoalkoxy quinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a. J Med Chem 52:7950–7953
    • (2009) J Med Chem , vol.52 , pp. 7950-7953
    • Liu, F.1    Chen, X.2    Allali-hassani, A.3
  • 45
    • 77955363182 scopus 로고    scopus 로고
    • Protein lysine methyltransferase g9a inhibitors: Design, synthesis, and structure activity relationships of 2,4-diamino-7-aminoalkoxy-quinazolines
    • Liu F, Chen X, Allali-Hassani A et al (2010) Protein lysine methyltransferase g9a inhibitors: design, synthesis, and structure activity relationships of 2,4-diamino-7-aminoalkoxy-quinazolines. J Med Chem 53:5844–5857
    • (2010) J Med Chem , vol.53 , pp. 5844-5857
    • Liu, F.1    Chen, X.2    Allali-hassani, A.3
  • 46
    • 80052473151 scopus 로고    scopus 로고
    • Structural basis of substrate methylation and inhibition of SMYD2
    • Ferguson AD, Larsen NA, Howard T et al (2011) Structural basis of substrate methylation and inhibition of SMYD2. Structure 19: 1262–1273
    • (2011) Structure , vol.19 , pp. 1262-1273
    • Ferguson, A.D.1    Larsen, N.A.2    Howard, T.3
  • 47
    • 79960493567 scopus 로고    scopus 로고
    • A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
    • Vedadi M, Barsyte-Lovejoy D, Liu F et al (2011) A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells. Nat Chem Biol 7:566–574
    • (2011) Nat Chem Biol , vol.7 , pp. 566-574
    • Vedadi, M.1    Barsyte-lovejoy, D.2    Liu, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.