메뉴 건너뛰기




Volumn 121, Issue 3, 2007, Pages 656-665

Histone deacetylase inhibitor, suberoylanilide hydroxamic acid (Vorinostat, SAHA) profoundly inhibits the growth of human pancreatic cancer cells

Author keywords

Histone deacetylase inhibitor; Pancreatic cancer; SAHA

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; 5 AZA 2' DEOXYCYTIDINE; BETA CATENIN; CCAAT ENHANCER BINDING PROTEIN ALPHA; CYCLIN B1; CYCLIN DEPENDENT KINASE INHIBITOR 1; CYTOKERATIN 7; HISTONE DEACETYLASE INHIBITOR; HISTONE H3; PROTEIN P53; RETINOIC ACID RECEPTOR ALPHA; UVOMORULIN; VORINOSTAT;

EID: 34250810709     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.22558     Document Type: Article
Times cited : (174)

References (61)
  • 2
    • 0034041801 scopus 로고    scopus 로고
    • Pancreatic cancer: A review of emerging therapies
    • Rosenberg L. Pancreatic cancer: a review of emerging therapies. Drugs 2000;59:1071-89.
    • (2000) Drugs , vol.59 , pp. 1071-1089
    • Rosenberg, L.1
  • 3
  • 5
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton VG, Imai BS, Yau P, Bradbury EM. Histone acetylation reduces nucleosome core particle linking number change. Cell 1989; 57:449-57.
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 6
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 1999;9:40-8.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 7
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell RP Jr., He LZ, Richon V, Calleja E, Pandolfi PP. Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J Natl Cancer Inst 1998;90:1621-5.
    • (1998) J Natl Cancer Inst , vol.90 , pp. 1621-1625
    • Warrell Jr., R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 8
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW. Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 2002;1:287-99.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 10
    • 12344330351 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors profoundly decrease proliferation of human lymphoid cancer cell lines
    • Sakajiri S, Kumagai T, Kawamata N, Saitoh T, Said JW, Koeffler HP. Histone deacetylase inhibitors profoundly decrease proliferation of human lymphoid cancer cell lines. Exp Hematol 2005;33:53-61.
    • (2005) Exp Hematol , vol.33 , pp. 53-61
    • Sakajiri, S.1    Kumagai, T.2    Kawamata, N.3    Saitoh, T.4    Said, J.W.5    Koeffler, H.P.6
  • 12
    • 10044225745 scopus 로고    scopus 로고
    • Human ovarian carcinoma cells: Histone deacetylase inhibitors exhibit antiproliferative activity and potently induce apoptosis
    • Takai N, Kawamata N, Gui D, Said JW, Miyakawa I, Koeffler HP. Human ovarian carcinoma cells: histone deacetylase inhibitors exhibit antiproliferative activity and potently induce apoptosis. Cancer 2004;101:2760-70.
    • (2004) Cancer , vol.101 , pp. 2760-2770
    • Takai, N.1    Kawamata, N.2    Gui, D.3    Said, J.W.4    Miyakawa, I.5    Koeffler, H.P.6
  • 14
    • 0032989027 scopus 로고    scopus 로고
    • Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu L, Kelso MJ, Hansen C, West ML, Fairlie DP, Parsons PG. Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br J Cancer 1999;80:1252-8.
    • (1999) Br J Cancer , vol.80 , pp. 1252-1258
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3    West, M.L.4    Fairlie, D.P.5    Parsons, P.G.6
  • 15
    • 0036906832 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From target to clinical trials
    • Kelly WK, O'Connor OA, Marks PA. Histone deacetylase inhibitors: from target to clinical trials. Expert Opin Investig Drugs 2002; 11:1695-713.
    • (2002) Expert Opin Investig Drugs , vol.11 , pp. 1695-1713
    • Kelly, W.K.1    O'Connor, O.A.2    Marks, P.A.3
  • 17
    • 0032146179 scopus 로고    scopus 로고
    • 19-nor-26,27-bishomo-vitamin D3 analogs: A unique class of potent inhibitors of proliferation of prostate, breast, and hematopoietic cancer cells
    • Kubota T, Koshizuka K, Koike M, Uskokovic M, Miyoshi I, Koeffler HP. 19-nor-26,27-bishomo-vitamin D3 analogs: a unique class of potent inhibitors of proliferation of prostate, breast, and hematopoietic cancer cells. Cancer Res 1998;58:3370-3375.
    • (1998) Cancer Res , vol.58 , pp. 3370-3375
    • Kubota, T.1    Koshizuka, K.2    Koike, M.3    Uskokovic, M.4    Miyoshi, I.5    Koeffler, H.P.6
  • 18
    • 0037704213 scopus 로고    scopus 로고
    • Vitamin D2 analog 19-nor-1,25-dihydroxyvitamin D2: Antitumor activity against leukemia, myeloma, and colon cancer cells
    • Kumagai T, O'Kelly J, Said JW, Koeffler HP. Vitamin D2 analog 19-nor-1,25-dihydroxyvitamin D2: antitumor activity against leukemia, myeloma, and colon cancer cells. J Natl Cancer Inst 2003;95:896-905.
    • (2003) J Natl Cancer Inst , vol.95 , pp. 896-905
    • Kumagai, T.1    O'Kelly, J.2    Said, J.W.3    Koeffler, H.P.4
  • 20
    • 9744254768 scopus 로고    scopus 로고
    • Evaluation of combination chemotherapy: Integration of nonlinear regression, curve shift, isobologram, and combination index analyses
    • Zhao L, Wientjes MG, Au JL. Evaluation of combination chemotherapy: integration of nonlinear regression, curve shift, isobologram, and combination index analyses. Clin Cancer Res 2004;10:7994-8004.
    • (2004) Clin Cancer Res , vol.10 , pp. 7994-8004
    • Zhao, L.1    Wientjes, M.G.2    Au, J.L.3
  • 21
    • 0028986091 scopus 로고
    • New pancreas cancers cell lines that represent distinct stages of ductal differentiation
    • Vila MR, Lloreta J, Schussler MH, Berrozpe G, Welt S, Real FX. New pancreas cancers cell lines that represent distinct stages of ductal differentiation. Lab Invest 1995;72:395-404.
    • (1995) Lab Invest , vol.72 , pp. 395-404
    • Vila, M.R.1    Lloreta, J.2    Schussler, M.H.3    Berrozpe, G.4    Welt, S.5    Real, F.X.6
  • 22
    • 0033119801 scopus 로고    scopus 로고
    • β-catenin regulates expression of cyclin D1 in colon carcinoma cells
    • Tetsu O, McCormick F. β-catenin regulates expression of cyclin D1 in colon carcinoma cells. Nature 1999;398:422-6.
    • (1999) Nature , vol.398 , pp. 422-426
    • Tetsu, O.1    McCormick, F.2
  • 26
    • 0041532109 scopus 로고    scopus 로고
    • Cell cycle blockade and differentiation of ovarian cancer cells by the histone deacetylase inhibitor trichostatin A are associated with changes in p21, Rb, and Id proteins
    • Strait KA, Dabbas B, Hammond EH, Wamick CT, Iistrup SJ, Ford CD. Cell cycle blockade and differentiation of ovarian cancer cells by the histone deacetylase inhibitor trichostatin A are associated with changes in p21, Rb, and Id proteins. Mol Cancer Ther 2002;1:1181-90.
    • (2002) Mol Cancer Ther , vol.1 , pp. 1181-1190
    • Strait, K.A.1    Dabbas, B.2    Hammond, E.H.3    Wamick, C.T.4    Iistrup, S.J.5    Ford, C.D.6
  • 27
    • 3042604470 scopus 로고    scopus 로고
    • Characterization of mutations and loss of heterozygosity of p53 and K-ras2 in pancreatic cancer cell lines by immobilized polymerase chain reaction
    • Butz J, Wickstrom E, Edwards J. Characterization of mutations and loss of heterozygosity of p53 and K-ras2 in pancreatic cancer cell lines by immobilized polymerase chain reaction. BMC Biotechnol 2003;3:11.
    • (2003) BMC Biotechnol , vol.3 , pp. 11
    • Butz, J.1    Wickstrom, E.2    Edwards, J.3
  • 29
    • 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, Isobe K. p300 collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor. J Biol Chem 2000;275:1371-6.
    • (2000) J Biol Chem , vol.275 , pp. 1371-1376
    • Xiao, H.1    Hasegawa, T.2    Isobe, K.3
  • 30
    • 0037126303 scopus 로고    scopus 로고
    • Myc suppression of the p21(Cip1) Cdk inhibitor influences the outcome of the p53 response to DNA damage
    • Seoane J, Le HV, Massague J. Myc suppression of the p21(Cip1) Cdk inhibitor influences the outcome of the p53 response to DNA damage. Nature 2002;419:729-34.
    • (2002) Nature , vol.419 , pp. 729-734
    • Seoane, J.1    Le, H.V.2    Massague, J.3
  • 31
    • 0031961995 scopus 로고    scopus 로고
    • Niculescu AB, III, Chen X, Smeets M, Hengst L, Prives C, Reed SI. Effects of p21(Cip1/Waf1) at both the G1/S and the G2/M cell cycle transitions: pRb is a critical determinant in blocking DNA replication and in preventing endoreduplication. Mol Cell Biol 1998;18:629-43. Erratum in: Mol Cell Biol 1998;18:1763.
    • Niculescu AB, III, Chen X, Smeets M, Hengst L, Prives C, Reed SI. Effects of p21(Cip1/Waf1) at both the G1/S and the G2/M cell cycle transitions: pRb is a critical determinant in blocking DNA replication and in preventing endoreduplication. Mol Cell Biol 1998;18:629-43. Erratum in: Mol Cell Biol 1998;18:1763.
  • 33
    • 0027731971 scopus 로고
    • Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit
    • Gu Y, Turck CW, Morgan DO. Inhibition of CDK2 activity in vivo by an associated 20K regulatory subunit. Nature 1993;366:707-10.
    • (1993) Nature , vol.366 , pp. 707-710
    • Gu, Y.1    Turck, C.W.2    Morgan, D.O.3
  • 34
    • 0028363519 scopus 로고
    • p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21
    • Toyoshima H, Hunter T. p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21. Cell 1994;78:67-74.
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 35
    • 0028988158 scopus 로고
    • Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution
    • Lee MH, Reynisdottir I, Massague J. Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. Genes Dev 1995;9:639-49.
    • (1995) Genes Dev , vol.9 , pp. 639-649
    • Lee, M.H.1    Reynisdottir, I.2    Massague, J.3
  • 36
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis P. Wnt signaling and cancer. Genes Dev 2000;14:1837-51.
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 37
    • 0031436939 scopus 로고    scopus 로고
    • Induction of a β-catenin-LEF-1 complex by wnt-1 and transforming mutants of β-catenin
    • Porfiri E, Rubinfeld B, Albert I, Hovanes K, Waterman M, Polakis P. Induction of a β-catenin-LEF-1 complex by wnt-1 and transforming mutants of β-catenin. Oncogene 1997;15:2833-9.
    • (1997) Oncogene , vol.15 , pp. 2833-2839
    • Porfiri, E.1    Rubinfeld, B.2    Albert, I.3    Hovanes, K.4    Waterman, M.5    Polakis, P.6
  • 40
    • 0033817339 scopus 로고    scopus 로고
    • β-catenin-histone deacetylase interactions regulate the transition of LEF1 from a transcriptional repressor to an activator
    • Billin AN, Thirlwell H, Ayer DE. β-catenin-histone deacetylase interactions regulate the transition of LEF1 from a transcriptional repressor to an activator. Mol Cell Biol 2000;20:6882-90.
    • (2000) Mol Cell Biol , vol.20 , pp. 6882-6890
    • Billin, A.N.1    Thirlwell, H.2    Ayer, D.E.3
  • 41
    • 0031029557 scopus 로고    scopus 로고
    • Absence of granulocyte colony-stimulating factor signaling and neutrophil development in CCAAT enhancer binding protein α-deficient mice
    • Zhang DE, Zhang P, Wang ND, Hetherington CJ, Darlington GJ, Tenen DG. Absence of granulocyte colony-stimulating factor signaling and neutrophil development in CCAAT enhancer binding protein α-deficient mice. Proc Natl Acad Sci USA 1997;94:569-74.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 569-574
    • Zhang, D.E.1    Zhang, P.2    Wang, N.D.3    Hetherington, C.J.4    Darlington, G.J.5    Tenen, D.G.6
  • 42
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi M. Morphogenetic roles of classic cadherins. Curr Opin Cell Biol 1995;7:619-27.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 43
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 1996;84:345-57.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 44
    • 0032510494 scopus 로고    scopus 로고
    • A causal role for E-cadherin in the transition from adenoma to carcinoma
    • Perl AK, Wilgenbus P, Dahl U, Semb H, Christofori G. A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature 1998;392:190-3.
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2    Dahl, U.3    Semb, H.4    Christofori, G.5
  • 45
    • 0033079605 scopus 로고    scopus 로고
    • The role of the cell-adhesion molecule E-cadherin as a tumour-suppressor gene
    • Christofori G, Semb H. The role of the cell-adhesion molecule E-cadherin as a tumour-suppressor gene. Trends Biochem Sci 1999;24:73-6.
    • (1999) Trends Biochem Sci , vol.24 , pp. 73-76
    • Christofori, G.1    Semb, H.2
  • 47
    • 0028804542 scopus 로고
    • E-cadherin expression in renal cell cancer and its significance in metastasis and survival
    • Katagiri A, Watanabe R, Tomita Y. E-cadherin expression in renal cell cancer and its significance in metastasis and survival. Br J Cancer 1995;71:376-9.
    • (1995) Br J Cancer , vol.71 , pp. 376-379
    • Katagiri, A.1    Watanabe, R.2    Tomita, Y.3
  • 48
    • 0035286576 scopus 로고    scopus 로고
    • The loss of E-cadherin, α- and β-catenin expression is associated with metastasis and poor prognosis in invasive breast cancer
    • Yoshida R, Kimura N, Harada Y, Ohuchi N. The loss of E-cadherin, α- and β-catenin expression is associated with metastasis and poor prognosis in invasive breast cancer. Int J Oncol 2001;18:513-20.
    • (2001) Int J Oncol , vol.18 , pp. 513-520
    • Yoshida, R.1    Kimura, N.2    Harada, Y.3    Ohuchi, N.4
  • 49
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon P. A decade of molecular biology of retinoic acid receptors. FASEB J 1996;10:940-54.
    • (1996) FASEB J , vol.10 , pp. 940-954
    • Chambon, P.1
  • 50
    • 0032528489 scopus 로고    scopus 로고
    • Impaired granulocytic differentiation in vitro in hematopoietic cells lacking retinoic acid receptors α1 and γ
    • Labrecque J, Allan D, Chambon P, Iscove NN, Lohnes D, Hoang T. Impaired granulocytic differentiation in vitro in hematopoietic cells lacking retinoic acid receptors α1 and γ. Blood 1998;92:607-15.
    • (1998) Blood , vol.92 , pp. 607-615
    • Labrecque, J.1    Allan, D.2    Chambon, P.3    Iscove, N.N.4    Lohnes, D.5    Hoang, T.6
  • 51
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves ahistone deacetylase complex
    • Nan X, Ng HH, Johnson CA, Laherty CD, Turner BM, Eisenman RN, Bird A. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves ahistone deacetylase complex. Nature 1998;393: 386-9.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 53
    • 0033601073 scopus 로고    scopus 로고
    • Methylation-induced repression-belts, braces, and chromatin
    • Bird AP, Wolffe AP. Methylation-induced repression-belts, braces, and chromatin. Cell 1999;99:451-4.
    • (1999) Cell , vol.99 , pp. 451-454
    • Bird, A.P.1    Wolffe, A.P.2
  • 54
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myohanen S, Herman JG, Baylin SB. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet 1999;21:103-7.
    • (1999) Nat Genet , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 55
    • 0034917318 scopus 로고    scopus 로고
    • Antineoplastic action of 5-aza-2′- deoxycytidine and histone deacetylase inhibitor and their effect on the expression of retinoic acid receptor β and estrogen receptor α genes in breast carcinoma cells
    • Bovenzi V, Momparler RL. Antineoplastic action of 5-aza-2′- deoxycytidine and histone deacetylase inhibitor and their effect on the expression of retinoic acid receptor β and estrogen receptor α genes in breast carcinoma cells. Cancer Chemother Pharmacol 2001;48:71-6.
    • (2001) Cancer Chemother Pharmacol , vol.48 , pp. 71-76
    • Bovenzi, V.1    Momparler, R.L.2
  • 56
    • 0024378078 scopus 로고
    • Specific protection of methylated CpGs in mammalian nuclei
    • Antequera F, Macleod D, Bird AP. Specific protection of methylated CpGs in mammalian nuclei. Cell 1989;58:509-17.
    • (1989) Cell , vol.58 , pp. 509-517
    • Antequera, F.1    Macleod, D.2    Bird, A.P.3
  • 58
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida M, Horinouchi S, Beppu T. Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 1995;17:423-30.
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 59
    • 0036746906 scopus 로고    scopus 로고
    • Antineoplastic action of 5-aza-2′-deoxycytidine and phenylbutyrate on human lung carcinoma cells
    • Boivin AJ, Momparler LF, Hurtubise A, Momparler RL. Antineoplastic action of 5-aza-2′-deoxycytidine and phenylbutyrate on human lung carcinoma cells. Anticancer Drugs 2002;13:869-74.
    • (2002) Anticancer Drugs , vol.13 , pp. 869-874
    • Boivin, A.J.1    Momparler, L.F.2    Hurtubise, A.3    Momparler, R.L.4
  • 60
  • 61
    • 0037400558 scopus 로고    scopus 로고
    • Preclinical evaluation of antineoplastic activity of inhibitors of DNA methylation (5-aza-2′-deoxycytidine) and histone deacetylation (trichostatin A, depsipeptide) in combination against myeloid leukemic cells
    • Shaker S, Bernstein M, Momparler LF, Momparler RL. Preclinical evaluation of antineoplastic activity of inhibitors of DNA methylation (5-aza-2′-deoxycytidine) and histone deacetylation (trichostatin A, depsipeptide) in combination against myeloid leukemic cells. Leuk Res 2003;27:437-44.
    • (2003) Leuk Res , vol.27 , pp. 437-444
    • Shaker, S.1    Bernstein, M.2    Momparler, L.F.3    Momparler, R.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.