메뉴 건너뛰기




Volumn 28, Issue 10, 2014, Pages 4265-4279

Overexpression of histone deacetylases in cancer cells is controlled by interplay of transcription factors and epigenetic modulators

Author keywords

P300; SET1; Sp1; Sp3

Indexed keywords

HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE SET1; TRANSCRIPTION FACTOR SP1; TRANSCRIPTION FACTOR SP3; UNCLASSIFIED DRUG; HDAC1 PROTEIN, HUMAN; HDAC2 PROTEIN, HUMAN; HISTONE LYSINE METHYLTRANSFERASE; SETD1A PROTEIN, HUMAN;

EID: 84907697952     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.14-250654     Document Type: Article
Times cited : (57)

References (58)
  • 1
    • 77956153243 scopus 로고    scopus 로고
    • The language of histone crosstalk
    • Lee, J. S., Smith, E., and Shilatifard, A. (2010) The language of histone crosstalk. Cell 142, 682-685
    • (2010) Cell , vol.142 , pp. 682-685
    • Lee, J.S.1    Smith, E.2    Shilatifard, A.3
  • 2
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: Intricacy of writing and readinga single epigenetic mark
    • Ruthenburg, A. J., Allis, C. D., and Wysocka, J. (2007) Methylation of lysine 4 on histone H3: intricacy of writing and readinga single epigenetic mark. Mol. Cell 25, 15-30
    • (2007) Mol. Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 4
    • 84875537133 scopus 로고    scopus 로고
    • Epigenetic reprogramming in cancer
    • Suva, M. L., Riggi, N., and Bernstein, B. E. (2013) Epigenetic reprogramming in cancer. Science 339, 1567-1570
    • (2013) Science , vol.339 , pp. 1567-1570
    • Suva, M.L.1    Riggi, N.2    Bernstein, B.E.3
  • 5
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: From mechanism to therapy
    • Dawson, M.A., and Kouzarides, T. (2012) Cancer epigenetics: from mechanism to therapy. Cell 150, 12-27
    • (2012) Cell , vol.150 , pp. 12-27
    • Dawson, M.A.1    Kouzarides, T.2
  • 6
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang, X. J., and Seto, E. (2007) HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene 26, 5310-5318
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.2
  • 7
    • 33744956666 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) and other class i HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer
    • Wilson, A. J., Byun, D. S., Popova, N., Murray, L. B., L'Italien, K., Sowa, Y., Arango, D., Velcich, A., Augenlicht, L. H., and Mariadason, J. M. (2006) Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer. J. Biol. Chem. 281, 13548-13558
    • (2006) J. Biol. Chem. , vol.281 , pp. 13548-13558
    • Wilson, A.J.1    Byun, D.S.2    Popova, N.3    Murray, L.B.4    L'italien, K.5    Sowa, Y.6    Arango, D.7    Velcich, A.8    Augenlicht, L.H.9    Mariadason, J.M.10
  • 8
    • 17144378591 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 2 increases apoptosis and p21Cip1/WAF1 expression, independent of histone deacetylase 1
    • Huang, B. H., Laban, M., Leung, C.H., Lee, L., Lee, C. K., Salto-Tellez, M., Raju, G. C., and Hooi, S. C. (2005) Inhibition of histone deacetylase 2 increases apoptosis and p21Cip1/WAF1 expression, independent of histone deacetylase 1. Cell Death Differ. 12, 395-404
    • (2005) Cell Death Differ. , vol.12 , pp. 395-404
    • Huang, B.H.1    Laban, M.2    Leung, C.H.3    Lee, L.4    Lee, C.K.5    Salto-Tellez, M.6    Raju, G.C.7    Hooi, S.C.8
  • 9
    • 13944284147 scopus 로고    scopus 로고
    • Specific and redundant functions of histone deacetylases in regulation of cell cycle and apoptosis
    • Zhu, P., Huber, E., Kiefer, F., and Gottlicher, M. (2004) Specific and redundant functions of histone deacetylases in regulation of cell cycle and apoptosis. Cell Cycle 3, 1240-1242
    • (2004) Cell Cycle , vol.3 , pp. 1240-1242
    • Zhu, P.1    Huber, E.2    Kiefer, F.3    Gottlicher, M.4
  • 12
    • 34248631385 scopus 로고    scopus 로고
    • The role of histone deacetylases (HDACs) in human cancer
    • Ropero, S., and Esteller, M. (2007) The role of histone deacetylases (HDACs) in human cancer. Mol. Oncol. 1, 19-25
    • (2007) Mol. Oncol. , vol.1 , pp. 19-25
    • Ropero, S.1    Esteller, M.2
  • 14
    • 1842631408 scopus 로고    scopus 로고
    • Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer
    • Halkidou, K., Gaughan, L., Cook, S., Leung, H. Y., Neal, D. E., and Robson, C. N. (2004) Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer. Prostate 59, 177-189
    • (2004) Prostate , vol.59 , pp. 177-189
    • Halkidou, K.1    Gaughan, L.2    Cook, S.3    Leung, H.Y.4    Neal, D.E.5    Robson, C.N.6
  • 15
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange, S., Wagner, T., Heinzel, T., and Kramer, O. H. (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 41, 185-198
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 16
    • 70349227061 scopus 로고    scopus 로고
    • Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation
    • Brunmeir, R., Lagger, S., and Seiser, C. (2009) Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation. Int. J. Dev. Biol. 53, 275-289
    • (2009) Int. J. Dev. Biol. , vol.53 , pp. 275-289
    • Brunmeir, R.1    Lagger, S.2    Seiser, C.3
  • 18
    • 84893824155 scopus 로고    scopus 로고
    • HSETD1A regulates Wnt target genes and controls tumor growth of colorectal cancer cells
    • Salz, T., Li, G., Kaye, F. J., Zhou, L., Qiu, Y., and Huang, S. (2014) hSETD1A regulates Wnt target genes and controls tumor growth of colorectal cancer cells. Cancer Res. 74, 775-786
    • (2014) Cancer Res. , vol.74 , pp. 775-786
    • Salz, T.1    Li, G.2    Kaye, F.J.3    Zhou, L.4    Qiu, Y.5    Huang, S.6
  • 20
    • 80054123169 scopus 로고    scopus 로고
    • Cancer associated epigenetic transitions identified by genome-wide histone methylation binding profiles in human colorectal cancer samples and paired normal mucosa
    • Enroth, S., Rada-Iglesisas, A., Andersson, R., Wallerman, O., Wanders, A., Pahlman, L., Komorowski, J., and Wadelius, C. (2011) Cancer associated epigenetic transitions identified by genome-wide histone methylation binding profiles in human colorectal cancer samples and paired normal mucosa. BMC Cancer 11, 450
    • (2011) BMC Cancer , vol.11 , pp. 450
    • Enroth, S.1    Rada-Iglesisas, A.2    Andersson, R.3    Wallerman, O.4    Wanders, A.5    Pahlman, L.6    Komorowski, J.7    Wadelius, C.8
  • 22
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequencespecific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W., and Roeder, R. G. (1997) Activation of p53 sequencespecific DNA binding by acetylation of the p53 C-terminal domain. Cell 90, 595-606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 23
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan, Z. L., Guan, Y. J., Chatterjee, D., and Chin, Y. E. (2005) Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 307, 269-273
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 25
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen, L. F., Mu, Y., and Greene, W. C. (2002) Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J. 21, 6539-6548
    • (2002) EMBO J. , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 26
    • 78349272461 scopus 로고    scopus 로고
    • HIF-1 and HIF-2 transcription factors-similar but not identical
    • Loboda, A., Jozkowicz, A., and Dulak, J. (2010) HIF-1 and HIF-2 transcription factors-similar but not identical. Mol. Cell 29, 435-442
    • (2010) Mol. Cell , vol.29 , pp. 435-442
    • Loboda, A.1    Jozkowicz, A.2    Dulak, J.3
  • 27
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang, Y., Rao, R., Shen, J., Tang, Y., Fiskus, W., Nechtman, J., Atadja, P., and Bhalla, K. (2008) Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res. 68, 4833-4842
    • (2008) Cancer Res. , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3    Tang, Y.4    Fiskus, W.5    Nechtman, J.6    Atadja, P.7    Bhalla, K.8
  • 30
    • 0032866999 scopus 로고    scopus 로고
    • The Sp-family of transcription factors
    • Suske, G. (1999) The Sp-family of transcription factors. Gene 238, 291-300
    • (1999) Gene , vol.238 , pp. 291-300
    • Suske, G.1
  • 31
    • 77956611413 scopus 로고    scopus 로고
    • The role of Sp1 and Sp3 in normal and cancer cell biology
    • Li, L., and Davie, J. R. (2010) The role of Sp1 and Sp3 in normal and cancer cell biology. Ann. Anat. 192, 275-283
    • (2010) Ann. Anat. , vol.192 , pp. 275-283
    • Li, L.1    Davie, J.R.2
  • 33
    • 0027416220 scopus 로고
    • Regulation of thymidylate synthase in human colon cancer cells treated with 5-fluorouracil and interferon-gamma
    • Chu, E., Koeller, D. M., Johnston, P. G., Zinn, S., and Allegra, C. J. (1993) Regulation of thymidylate synthase in human colon cancer cells treated with 5-fluorouracil and interferon-gamma. Mol. Pharmacol. 43, 527-533
    • (1993) Mol. Pharmacol. , vol.43 , pp. 527-533
    • Chu, E.1    Koeller, D.M.2    Johnston, P.G.3    Zinn, S.4    Allegra, C.J.5
  • 37
    • 71049179047 scopus 로고    scopus 로고
    • Expression levels of histone deacetylases determine the cell fate of hematopoietic progenitors
    • Wada, T., Kikuchi, J., Nishimura, N., Shimizu, R., Kitamura, T., and Furukawa, Y. (2009) Expression levels of histone deacetylases determine the cell fate of hematopoietic progenitors. J. Biol. Chem. 284, 30673-30683
    • (2009) J. Biol. Chem. , vol.284 , pp. 30673-30683
    • Wada, T.1    Kikuchi, J.2    Nishimura, N.3    Shimizu, R.4    Kitamura, T.5    Furukawa, Y.6
  • 38
    • 84870023777 scopus 로고    scopus 로고
    • Acetylation of histone deacetylase 1 regulates NuRD corepressor complex activity
    • Yang, T., Jian, W., Luo, Y., Fu, X., Noguchi, C., Bungert, J., Huang, S., and Qiu, Y. (2012) Acetylation of histone deacetylase 1 regulates NuRD corepressor complex activity. J. Biol. Chem.287, 40279-40291
    • (2012) J. Biol. Chem. , vol.287 , pp. 40279-40291
    • Yang, T.1    Jian, W.2    Luo, Y.3    Fu, X.4    Noguchi, C.5    Bungert, J.6    Huang, S.7    Qiu, Y.8
  • 39
    • 0025986514 scopus 로고
    • Transcription from a TATAless promoter requires a multisubunit TFIID complex
    • Pugh, B. F., and Tjian, R. (1991) Transcription from a TATAless promoter requires a multisubunit TFIID complex. Genes Dev. 5, 1935-1945
    • (1991) Genes Dev. , vol.5 , pp. 1935-1945
    • Pugh, B.F.1    Tjian, R.2
  • 40
    • 0032582671 scopus 로고    scopus 로고
    • Cloning and characterization of the mouse histone deacetylase-2 gene
    • Zeng, Y., Tang, C. M., Yao, Y. L., Yang, W. M., and Seto, E. (1998) Cloning and characterization of the mouse histone deacetylase-2 gene. J. Biol. Chem. 273, 28921-28930
    • (1998) J. Biol. Chem. , vol.273 , pp. 28921-28930
    • Zeng, Y.1    Tang, C.M.2    Yao, Y.L.3    Yang, W.M.4    Seto, E.5
  • 41
    • 84876336093 scopus 로고    scopus 로고
    • Transcription factor Sp3 represses expression of p21CIP(1) via inhibition of productive elongation by RNA polymerase II
    • Valin, A., Ouyang, J., and Gill, G. (2013) Transcription factor Sp3 represses expression of p21CIP(1) via inhibition of productive elongation by RNA polymerase II. Mol. Cell. Biol. 33, 1582-1593
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1582-1593
    • Valin, A.1    Ouyang, J.2    Gill, G.3
  • 42
    • 0033529096 scopus 로고    scopus 로고
    • Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation
    • Billon, N., Carlisi, D., Datto, M. B., van Grunsven, L. A., Watt, A., Wang, X. F., and Rudkin, B. B. (1999) Cooperation of Sp1 and p300 in the induction of the CDK inhibitor p21WAF1/CIP1 during NGF-mediated neuronal differentiation. Oncogene 18, 2872-2882
    • (1999) Oncogene , vol.18 , pp. 2872-2882
    • Billon, N.1    Carlisi, D.2    Datto, M.B.3    Van Grunsven, L.A.4    Watt, A.5    Wang, X.F.6    Rudkin, B.B.7
  • 44
    • 0033964512 scopus 로고    scopus 로고
    • P300 collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor
    • Xiao, H., Hasegawa, T., and Isobe, K. (2000) p300 collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor. J. Biol. Chem. 275, 1371-1376
    • (2000) J. Biol. Chem. , vol.275 , pp. 1371-1376
    • Xiao, H.1    Hasegawa, T.2    Isobe, K.3
  • 45
    • 77957917520 scopus 로고    scopus 로고
    • Sp1 acetylation is associated with loss of DNA binding at promoters associated with cell cycle arrest and cell death in a colon cell line
    • Waby, J. S., Chirakkal, H., Yu, C., Griffiths, G. J., Benson, R. S., Bingle, C. D., and Corfe, B. M. (2010) Sp1 acetylation is associated with loss of DNA binding at promoters associated with cell cycle arrest and cell death in a colon cell line. Mol. Cancer 9, 275
    • (2010) Mol. Cancer , vol.9 , pp. 275
    • Waby, J.S.1    Chirakkal, H.2    Yu, C.3    Griffiths, G.J.4    Benson, R.S.5    Bingle, C.D.6    Corfe, B.M.7
  • 46
    • 33644511058 scopus 로고    scopus 로고
    • Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription
    • Hung, J. J., Wang, Y. T., and Chang, W. C. (2006) Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription. Mol. Cell. Biol. 26, 1770-1785
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1770-1785
    • Hung, J.J.1    Wang, Y.T.2    Chang, W.C.3
  • 48
    • 41549159879 scopus 로고    scopus 로고
    • Class i histone deacetylase expression has independent prognostic impact in human colorectal cancer: Specific role of class i histone deacetylases in vitro and in vivo
    • Weichert, W., Roske, A., Niesporek, S., Noske, A., Buckendahl, A. C., Dietel, M., Gekeler, V., Boehm, M., Beckers, T., and Denkert, C. (2008) Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo. Clin. Cancer Res. 14, 1669-1677
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1669-1677
    • Weichert, W.1    Roske, A.2    Niesporek, S.3    Noske, A.4    Buckendahl, A.C.5    Dietel, M.6    Gekeler, V.7    Boehm, M.8    Beckers, T.9    Denkert, C.10
  • 49
    • 75749143069 scopus 로고    scopus 로고
    • A novel histone deacetylase inhibitor Chidamide induces apoptosis of human colon cancer cells
    • Liu, L., Chen, B., Qin, S., Li, S., He, X., Qiu, S., Zhao, W., and Zhao, H. (2010) A novel histone deacetylase inhibitor Chidamide induces apoptosis of human colon cancer cells. Biochem. Biophys. Res. Commun. 392, 190-195
    • (2010) Biochem. Biophys. Res. Commun. , vol.392 , pp. 190-195
    • Liu, L.1    Chen, B.2    Qin, S.3    Li, S.4    He, X.5    Qiu, S.6    Zhao, W.7    Zhao, H.8
  • 50
    • 84861565976 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor trichostatin A induces cell cycle arrest and apoptosis in colorectal cancer cells via p53-dependent and-independent pathways
    • Meng, J., Zhang, H. H., Zhou, C. X., Li, C., Zhang, F., and Mei, Q. B. (2012) The histone deacetylase inhibitor trichostatin A induces cell cycle arrest and apoptosis in colorectal cancer cells via p53-dependent and-independent pathways. Oncol. Rep. 28, 384-388
    • (2012) Oncol. Rep. , vol.28 , pp. 384-388
    • Meng, J.1    Zhang, H.H.2    Zhou, C.X.3    Li, C.4    Zhang, F.5    Mei, Q.B.6
  • 51
    • 70449367075 scopus 로고    scopus 로고
    • Efficacy of MS-275, a selective inhibitor of class i histone deacetylases, in human colon cancer models
    • Bracker, T. U., Sommer, A., Fichtner, I., Faus, H., Haendler, B., and Hess-Stumpp, H. (2009) Efficacy of MS-275, a selective inhibitor of class I histone deacetylases, in human colon cancer models. Int. J. Oncol. 35, 909-920
    • (2009) Int. J. Oncol. , vol.35 , pp. 909-920
    • Bracker, T.U.1    Sommer, A.2    Fichtner, I.3    Faus, H.4    Haendler, B.5    Hess-Stumpp, H.6
  • 53
    • 85027952442 scopus 로고    scopus 로고
    • Synergistic induction of apoptosis and chemosensitization of human colorectal cancer cells by histone deacetylase inhibitor, scriptaid, and proteasome inhibitors: Potential mechanisms of action
    • Abaza, M. S., Bahman, A. M., Al-Attiyah, R. J., and Kollamparambil, A. M. (2012) Synergistic induction of apoptosis and chemosensitization of human colorectal cancer cells by histone deacetylase inhibitor, scriptaid, and proteasome inhibitors: potential mechanisms of action. Tumour Biol. 33, 1951-1972
    • (2012) Tumour Biol. , vol.33 , pp. 1951-1972
    • Abaza, M.S.1    Bahman, A.M.2    Al-Attiyah, R.J.3    Kollamparambil, A.M.4
  • 55
    • 48749097600 scopus 로고    scopus 로고
    • Expression patterns of SP1 and SP3 during mouse spermatogenesis: SP1 down-regulation correlates with two successive promoter changes and translationally compromised transcripts
    • Ma, W., Horvath, G. C., Kistler, M. K., and Kistler, W. S. (2008) Expression patterns of SP1 and SP3 during mouse spermatogenesis: SP1 down-regulation correlates with two successive promoter changes and translationally compromised transcripts. Biol. Reprod. 79, 289-300
    • (2008) Biol. Reprod. , vol.79 , pp. 289-300
    • Ma, W.1    Horvath, G.C.2    Kistler, M.K.3    Kistler, W.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.