메뉴 건너뛰기




Volumn 20, Issue 34, 2014, Pages 5438-5442

Teratogenic activity of HDAC inhibitors

Author keywords

Congenital malformations; HDAC inhibitors; Mechanisms; Teratogenesis

Indexed keywords

APICIDIN; BORIC ACID; BUTYRIC ACID; ENTINOSTAT; HISTONE DEACETYLASE INHIBITOR; RETINOIC ACID; SALICYLIC ACID; TERATOGENIC AGENT; TRICHOSTATIN A; VALPROIC ACID;

EID: 84925844825     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612820666140205144900     Document Type: Article
Times cited : (22)

References (83)
  • 1
    • 33644872992 scopus 로고    scopus 로고
    • Chromatin control and acne-drug discovery: Realizing the promise
    • [1] Inche AG, La Thangue NB. Chromatin control and acne-drug discovery: realizing the promise. Drug Discov Today 2006; 11: 97-109
    • (2006) Drug Discov Today , vol.11 , pp. 97-109
    • Inche, A.G.1    La Thangue, N.B.2
  • 2
  • 3
    • 0344407016 scopus 로고    scopus 로고
    • Histone deacetylases: Unique players in shaping the epigenetic histone code
    • [3] Thiagalingam S. Histone deacetylases: unique players in shaping the epigenetic histone code. Ann. NY Acad Sc 2003; 983: 84-100.
    • (2003) Ann. NY Acad Sc , vol.983 , pp. 84-100
    • Thiagalingam, S.1
  • 4
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of nonhistone proteins
    • [4] Glozak MA, Sengupta N, Zhang X, Seto E. Acetylation and deacetylation of nonhistone proteins. Gene 2005; 363: 15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 5
    • 18444414332 scopus 로고    scopus 로고
    • Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression
    • [5] Lagger G, O’Carroll D, Rembold M, et al. Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression. EMBO J 2002; 21: 2672-81.
    • (2002) EMBO J , vol.21 , pp. 2672-2681
    • Lagger, G.1    O’Carroll, D.2    Rembold, M.3
  • 6
    • 16244366803 scopus 로고    scopus 로고
    • Class II Histone Deacetylases: From Sequence to Function, Regulation, and Clinical Implication
    • [6] Xiang-Jiao Yang, Serge Grégoire. Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication. Mol Cellular Biol 2005; 25: 2873-84.
    • (2005) Mol Cellular Biol , vol.25 , pp. 2873-2884
    • Yang, X.-J.1    Grégoire, S.2
  • 7
    • 84855471028 scopus 로고    scopus 로고
    • Modulation of antigen-presenting cells by HDAC inhibitors: Implications in autoimmunity and cancer
    • [7] Karrune V Woan, Eva Sahakian, Eduardo M Sotomayor, Edward Seto and Alejandro Villagra Modulation of antigen-presenting cells by HDAC inhibitors: implications in autoimmunity and cancer. Immunol Cell Biol 2012; 90: 55-65
    • (2012) Immunol Cell Biol , vol.90 , pp. 55-65
    • Woan, K.V.1    Sahakian, E.2    Sotomayor, E.M.3    Seto, E.4    Villagra, A.5
  • 8
    • 8344261349 scopus 로고    scopus 로고
    • Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis
    • [8] Vega RB, Matsuda K, Oh J, et al. Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis. Cell 2004; 119: 555-66.
    • (2004) Cell , vol.119 , pp. 555-566
    • Vega, R.B.1    Matsuda, K.2    Oh, J.3
  • 9
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • [9] Zhang CL, McKinsey TA, Chang S, et al. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell 2002; 110: 479-88.
    • (2002) Cell , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3
  • 10
    • 6944252151 scopus 로고    scopus 로고
    • Histone deacetylase 1 (HDAC-1) required for the normal formation of craniofacial cartilage and pectoral fins of the zebrafish
    • [10] Coverdale LE, Gaytry D, Cristofre M. Histone deacetylase 1 (HDAC-1) required for the normal formation of craniofacial cartilage and pectoral fins of the zebrafish. Dev Dynamics 2004; 231: 647-54.
    • (2004) Dev Dynamics , vol.231 , pp. 647-654
    • Coverdale, L.E.1    Gaytry, D.2    Cristofre, M.3
  • 11
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • [11] Xu WS, Parmigiani RB, Marks PA. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007, 26: 5541-2.
    • (2007) Oncogene , vol.26 , pp. 5541-5542
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 12
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer terapy: Is transcription the primary target?
    • [12] Johnston RW, Licht JD. Histone deacetylase inhibitors in cancer terapy: is transcription the primary target? Cancer Cell 2003; 4: 13-8
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnston, R.W.1    Licht, J.D.2
  • 13
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor ms-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21cip1/waf1 1
    • [13] Rosato RR, Almenara JA, Grant S. The histone deacetylase inhibitor ms-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21cip1/waf1 1. Cancer Res 2003; 63: 3637-45.
    • (2003) Cancer Res , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 15
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • [15] Shao Y, Gao Z, Marks PA, et al. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 2004; 101: 18030-5.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3
  • 16
    • 77955643796 scopus 로고    scopus 로고
    • The clinical development of histone deacetylase inhibitors as targeted anticancer drugs
    • [16] Marks PA. The clinical development of histone deacetylase inhibitors as targeted anticancer drugs. Expert Opin Investig Drugs 2010; 19: 1049-166.
    • (2010) Expert Opin Investig Drugs , vol.19 , pp. 1049-1166
    • Marks, P.A.1
  • 17
    • 84855471990 scopus 로고    scopus 로고
    • HDAC inhibitors in cancer biology: Emerging mechanisms and clinical applications
    • [17] Khan M, La Thangue NB. HDAC inhibitors in cancer biology: emerging mechanisms and clinical applications. Immunol Cell Biol 2012; 90: 85-94.
    • (2012) Immunol Cell Biol , vol.90 , pp. 85-94
    • Khan, M.1    La Thangue, N.B.2
  • 18
    • 0019965961 scopus 로고
    • Maternal valproic acid and congenital neural tube defects
    • [18] Robert E, Guibaud P. Maternal valproic acid and congenital neural tube defects. Lancet 1982; 2: 937.
    • (1982) Lancet , vol.2 , pp. 937
    • Robert, E.1    Guibaud, P.2
  • 21
    • 0029760579 scopus 로고    scopus 로고
    • Teratogenic effects of sodium valproate in mice and rats at midgestation and at term
    • [21] Menegola E, Broccia ML, Nau H, et al. Teratogenic effects of sodium valproate in mice and rats at midgestation and at term. Terat Carcin Mutag 1996; 16: 97-108
    • (1996) Terat Carcin Mutag , vol.16 , pp. 97-108
    • Menegola, E.1    Broccia, M.L.2    Nau, H.3
  • 22
    • 1542357630 scopus 로고    scopus 로고
    • Amidic modification of valproic acid reduces skeletal teratogenicity in mice
    • [22] Okada A, Kurihara H, Aoki Y, Bialer M, Fijiwara M. Amidic modification of valproic acid reduces skeletal teratogenicity in mice. Birth Defects Res B 2004; 71: 47-53
    • (2004) Birth Defects Res B , vol.71 , pp. 47-53
    • Okada, A.1    Kurihara, H.2    Aoki, Y.3    Bialer, M.4    Fijiwara, M.5
  • 23
    • 0026556607 scopus 로고
    • Valproic acid induced spina bifida: A mouse model
    • [23] Ehlers K, Surje H, Merker HJ, Nau H. Valproic acid induced spina bifida: a mouse model. Teratology 1992; 45: 145-54
    • (1992) Teratology , vol.45 , pp. 145-154
    • Ehlers, K.1    Surje, H.2    Merker, H.J.3    Nau, H.4
  • 24
    • 77957183374 scopus 로고
    • Evaluation of valproic acid developmental toxicity and pharmacokinetics in Sprague-Dawley rats
    • [24] Binkerd PE, Rowland JM, Nau H, Hendrickx AG. Evaluation of valproic acid developmental toxicity and pharmacokinetics in Sprague-Dawley rats. Fund Appl Toxicol 1988, 11: 485-93.
    • (1988) Fund Appl Toxicol , vol.11 , pp. 485-493
    • Binkerd, P.E.1    Rowland, J.M.2    Nau, H.3    Hendrickx, A.G.4
  • 25
    • 0023697903 scopus 로고
    • Valproic acid developmental toxicity and pharmacokinetics in the rhesus monkey: An interspecies comparison
    • [25] Hendrickx AG, Nau H, Binkerd P, et al. Valproic acid developmental toxicity and pharmacokinetics in the rhesus monkey: an interspecies comparison. Teratology 1988; 38: 329-45.
    • (1988) Teratology , vol.38 , pp. 329-345
    • Hendrickx, A.G.1    Nau, H.2    Binkerd, P.3
  • 26
    • 0019832773 scopus 로고
    • Teratogenicity of valproic acid: In vivo and in vitro investigations
    • [26] Kao J, Brown N, Schmid B, Goulding E, Fabro S. Teratogenicity of valproic acid: in vivo and in vitro investigations. Terat Carcin Mutag 1981; 1: 367-82.
    • (1981) Terat Carcin Mutag , vol.1 , pp. 367-382
    • Kao, J.1    Brown, N.2    Schmid, B.3    Goulding, E.4    Fabro, S.5
  • 27
    • 0023030926 scopus 로고
    • Teratogenesis of calcium valproate in rabbits
    • [27] Petrere JA, Anderson JA, Sakowski R, et al. Teratogenesis of calcium valproate in rabbits. Teratology 1986; 34: 263-9.
    • (1986) Teratology , vol.34 , pp. 263-269
    • Petrere, J.A.1    Erson, J.A.2    Sakowski, R.3
  • 28
    • 0023273582 scopus 로고
    • Teratogenicity and developmental toxicity of valproic acid in rats
    • [28] Vorhees CV. Teratogenicity and developmental toxicity of valproic acid in rats. Teratology 1987; 35: 195-202.
    • (1987) Teratology , vol.35 , pp. 195-202
    • Vorhees, C.V.1
  • 29
    • 0031886987 scopus 로고    scopus 로고
    • Stage dependent skeletal malformations induced by valproic acid in rats
    • [29] Menegola E, Broccia ML, Prati M, Giavini E. Stage dependent skeletal malformations induced by valproic acid in rats. Int J Dev Biol 1998; 42: 99-102.
    • (1998) Int J Dev Biol , vol.42 , pp. 99-102
    • Menegola, E.1    Broccia, M.L.2    Prati, M.3    Giavini, E.4
  • 30
    • 0034780879 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor trichostatin A influences the development of Drosophila melanogaster
    • [30] Pile LA, Lee FW, Wassarman DA. The histone deacetylase inhibitor trichostatin A influences the development of Drosophila melanogaster. Cell Mol Life Sci 2001; 58: 1715-1718.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1715-1718
    • Pile, L.A.1    Lee, F.W.2    Wassarman, D.A.3
  • 31
    • 0027414742 scopus 로고
    • Accumulation of multiacetylated forms of histones by trichostatin A and its developmental consequences in early starfish embryos
    • [31] Ikegami S, Ooe Y, Shimizu T, et al. Accumulation of multiacetylated forms of histones by trichostatin A and its developmental consequences in early starfish embryos. Roux’s Arch Dev Biol 1993; 202: 144-151.
    • (1993) Roux’s Arch Dev Biol , vol.202 , pp. 144-151
    • Ikegami, S.1    Ooe, Y.2    Shimizu, T.3
  • 32
    • 0031761928 scopus 로고    scopus 로고
    • Histone deacetylase mRNA temporally and spatially regulated in its expression in sea urchin embryos
    • [32] Nemer M. Histone deacetylase mRNA temporally and spatially regulated in its expression in sea urchin embryos. Dev Growth Differ 1998; 40: 583-90.
    • (1998) Dev Growth Differ , vol.40 , pp. 583-590
    • Nemer, M.1
  • 33
    • 0027971019 scopus 로고
    • Histone acetylation influences both gene expression and development of Xenopus laevis
    • [33] Almouzni G, Khochbin S, Dimitrov S, et al. Histone acetylation influences both gene expression and development of Xenopus laevis. Dev Biol 1994; 165: 654-69.
    • (1994) Dev Biol , vol.165 , pp. 654-669
    • Almouzni, G.1    Khochbin, S.2    Dimitrov, S.3
  • 34
    • 0034795328 scopus 로고    scopus 로고
    • Involvement of histone deacetylase at two distinct steps in gene regulation during intestinal development in Xenopus laevis
    • [34] Sachs LM, Amano T, Rouse N, et al. Involvement of histone deacetylase at two distinct steps in gene regulation during intestinal development in Xenopus laevis. Dev Dyn 2001; 222: 280-91.
    • (2001) Dev Dyn , vol.222 , pp. 280-291
    • Sachs, L.M.1    Amano, T.2    Rouse, N.3
  • 35
    • 0035650655 scopus 로고    scopus 로고
    • An essential role of histone deacetylase in postembryonic organ transformations in Xenopus laevis
    • [35] Sachs LM, Amano T, Shi YB. An essential role of histone deacetylase in postembryonic organ transformations in Xenopus laevis. Int J Mol Med 2001; 8: 595-601.
    • (2001) Int J Mol Med , vol.8 , pp. 595-601
    • Sachs, L.M.1    Amano, T.2    Shi, Y.B.3
  • 36
    • 21744448183 scopus 로고    scopus 로고
    • Association of valproate induced teratogenesis with histone deacetylase inhibition in vivo
    • [36] Gurvich N, Berman MG, Wittner BS, et al. Association of valproate induced teratogenesis with histone deacetylase inhibition in vivo. FASEB J 2005; 19: 1166-8.
    • (2005) FASEB J , vol.19 , pp. 1166-1168
    • Gurvich, N.1    Berman, M.G.2    Wittner, B.S.3
  • 37
    • 0035866388 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity
    • [37] Nervi C, Borello U, Fazi F, et al. Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity. Cancer Res 2001; 61: 1247-9.
    • (2001) Cancer Res , vol.61 , pp. 1247-1249
    • Nervi, C.1    Borello, U.2    Fazi, F.3
  • 38
    • 27644527117 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity on specific embryonic tissues as a new mechanism for teratogenicity
    • [38] Menegola E, Di Renzo F, Broccia ML, et al. Inhibition of histone deacetylase activity on specific embryonic tissues as a new mechanism for teratogenicity. Birth Defects Res B Dev Reprod Toxicol 2005; 74: 392-8.
    • (2005) Birth Defects Res B Dev Reprod Toxicol , vol.74 , pp. 392-398
    • Menegola, E.1    Di Renzo, F.2    Broccia, M.L.3
  • 39
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • [39] Phiel CJ, Zhang F, Huang EY, Guenther MG, Lazar MA, Klein PS. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J Biol Chem 2001; 276: 36734-41.
    • (2001) J Biol Chem , vol.276 , pp. 36734-36741
    • Phiel, C.J.1    Zhang, F.2    Huang, E.Y.3    Guenther, M.G.4    Lazar, M.A.5    Klein, P.S.6
  • 40
    • 34547851651 scopus 로고    scopus 로고
    • Relationship between embryonic histonic hyperacetylation and axial skeletal defects in mouse exposed to the three HDAC inhibitors apicidin, MS-275, and sodium butyrate
    • [40] Di Renzo F, Broccia ML, Giavini E, Menegola E. Relationship between embryonic histonic hyperacetylation and axial skeletal defects in mouse exposed to the three HDAC inhibitors apicidin, MS-275, and sodium butyrate. Toxicol Sci 2007; 98, 582-8.
    • (2007) Toxicol Sci , vol.98 , pp. 582-588
    • Di Renzo, F.1    Broccia, M.L.2    Giavini, E.3    Menegola, E.4
  • 41
    • 16244367785 scopus 로고    scopus 로고
    • Vertebral malformations induced by sodium salicylate correlate with shifts in expression domains of Hox genes
    • [41] Wéry N, Foulon O, Blacker A, Picard JJ, Gofflot F. Vertebral malformations induced by sodium salicylate correlate with shifts in expression domains of Hox genes. Reprod Toxicol 2005; 20: 39-45.
    • (2005) Reprod Toxicol , vol.20 , pp. 39-45
    • Wéry, N.1    Foulon, O.2    Blacker, A.3    Picard, J.J.4    Gofflot, F.5
  • 42
    • 16244363907 scopus 로고    scopus 로고
    • Defects in cervical vertebrae in boric acid-exposed rat embryos are associated with anterior shifts of hox gene expression domains
    • [42] Wéry N, Narotsky MG, Pacico N, Kavlock RJ, Picard JJ, Gofflot F. Defects in cervical vertebrae in boric acid-exposed rat embryos are associated with anterior shifts of hox gene expression domains. Birth Defects Res A 2003; 67: 59-67.
    • (2003) Birth Defects Res A , vol.67 , pp. 59-67
    • Wéry, N.1    Narotsky, M.G.2    Pacico, N.3    Kavlock, R.J.4    Picard, J.J.5    Gofflot, F.6
  • 43
    • 33947714264 scopus 로고    scopus 로고
    • Boric acid inhibits embryonic histone deacetylases: A suggested mechanism to explain boric acid-related teratogenicity
    • [43] Di Renzo F, Cappelletti G, Broccia ML, Giavini E, Menegola E. Boric acid inhibits embryonic histone deacetylases: A suggested mechanism to explain boric acid-related teratogenicity. Toxicol ApplPharmacol 2007; 220: 178-85.
    • (2007) Toxicol Applpharmacol , vol.220 , pp. 178-185
    • Di Renzo, F.1    Cappelletti, G.2    Broccia, M.L.3    Giavini, E.4    Menegola, E.5
  • 44
    • 47849119313 scopus 로고    scopus 로고
    • The inhibition of embryonic histone deacetylases as the possible mechanism accounting for axial skeletal malformations induced by sodium salicylate
    • [44] Di Renzo F, Cappelletti G, Broccia ML, Giavini E, Menegola E. The inhibition of embryonic histone deacetylases as the possible mechanism accounting for axial skeletal malformations induced by sodium salicylate. Toxicol Sci 2008; 104: 397-404
    • (2008) Toxicol Sci , vol.104 , pp. 397-404
    • Di Renzo, F.1    Cappelletti, G.2    Broccia, M.L.3    Giavini, E.4    Menegola, E.5
  • 45
    • 33645305408 scopus 로고    scopus 로고
    • Cellular changes in boric acid-treated DU-145 prostate cancer cells
    • [45] Barranco WT, Eckhert CD. Cellular changes in boric acid-treated DU-145 prostate cancer cells. Br J Cancer 2006; 94, 884-90.
    • (2006) Br J Cancer , vol.94 , pp. 884-890
    • Barranco, W.T.1    Eckhert, C.D.2
  • 46
    • 0034892506 scopus 로고    scopus 로고
    • Salicylic acid: A link between aspirin, diet and the prevention of colorectal cancer
    • [46] Paterson JR, Lawrence JR.: Salicylic acid: A link between aspirin, diet and the prevention of colorectal cancer. Q J Med 2001; 94: 445-8.
    • (2001) Q J Med , vol.94 , pp. 445-448
    • Paterson, J.R.1    Lawrence, J.R.2
  • 47
    • 34247639408 scopus 로고    scopus 로고
    • A large cohort study of long term daily use of adult-strength aspirin and cancer incidence
    • [47] Jacobs EJ, Thun MJ, Bain EB, et al. A large cohort study of long term daily use of adult-strength aspirin and cancer incidence. J Natl Cancer Inst 2007; 99: 608-15.
    • (2007) J Natl Cancer Inst , vol.99 , pp. 608-615
    • Jacobs, E.J.1    Thun, M.J.2    Bain, E.B.3
  • 48
    • 78650021238 scopus 로고    scopus 로고
    • Intrauterine exposure to carbamazepine and specific congenital malformations: Systemic review and case-control study
    • [48] Jentik J, Dolk H, Loane MA, et al. Intrauterine exposure to carbamazepine and specific congenital malformations: systemic review and case-control study. B Med J 2010, 341: c6581
    • (2010) B Med J , vol.341
    • Jentik, J.1    Dolk, H.2    Loane, M.A.3
  • 49
    • 50549083309 scopus 로고    scopus 로고
    • Topiramate in pregnancy. Preliminary experience from the UK epilepsy and pregnancy register
    • [49] Hunt S, Russell A, Smithson H, et al. Topiramate in pregnancy. Preliminary experience from the UK epilepsy and pregnancy register. Neurology 2008; 71: 272-6.
    • (2008) Neurology , vol.71 , pp. 272-276
    • Hunt, S.1    Russell, A.2    Smithson, H.3
  • 50
    • 84873669013 scopus 로고    scopus 로고
    • Levetiracetam in pregnancy: Results from the UK and Irelend epilepsy and pregnancy registers
    • [50] Mawhinney E, Craig J, Morrow J, et al. Levetiracetam in pregnancy: results from the UK and Irelend epilepsy and pregnancy registers. Neurology 2013, 80: 400-5.
    • (2013) Neurology , vol.80 , pp. 400-405
    • Mawhinney, E.1    Craig, J.2    Morrow, J.3
  • 51
    • 3042859183 scopus 로고    scopus 로고
    • The activity of antiepileptic drugs as histone deacetylase inhibitors
    • [51] Eyal S, Yagen B, Sobol E, Altschuler Y, Shmuel M, Bialer M. The activity of antiepileptic drugs as histone deacetylase inhibitors. Epilepsia 2004; 45: 737-44.
    • (2004) Epilepsia , vol.45 , pp. 737-744
    • Eyal, S.1    Yagen, B.2    Sobol, E.3    Altschuler, Y.4    Shmuel, M.5    Bialer, M.6
  • 52
    • 17844403222 scopus 로고    scopus 로고
    • Carbamazepine is an inhibitor of histone deacetylases
    • [52] Beutler AS, Li S, Nicol R, Walsh MJ. Carbamazepine is an inhibitor of histone deacetylases. Life Sciences 2005; 76: 3107-15
    • (2005) Life Sciences , vol.76 , pp. 3107-3115
    • Beutler, A.S.1    Li, S.2    Nicol, R.3    Walsh, M.J.4
  • 53
    • 77949453165 scopus 로고    scopus 로고
    • Sodium valproateinduced congenital cardiac abnormalities in mice are associated with the inhibition of histone deacetylase
    • [53] Wu G, Nan C, Rollo JC, Huang X, Tian J. Sodium valproateinduced congenital cardiac abnormalities in mice are associated with the inhibition of histone deacetylase. J Biomed Sci 2010; 17: 16-23.
    • (2010) J Biomed Sci , vol.17 , pp. 16-23
    • Wu, G.1    Nan, C.2    Rollo, J.C.3    Huang, X.4    Tian, J.5
  • 54
    • 73449110127 scopus 로고    scopus 로고
    • VPA-related axial skeletal defects and apoptosis: A proposed event cascade
    • [54] Di Renzo F, Broccia ML, Giavini E, Menegola E. VPA-related axial skeletal defects and apoptosis: a proposed event cascade. Reprod Toxicol 2010; 29: 106-12.
    • (2010) Reprod Toxicol , vol.29 , pp. 106-112
    • Di Renzo, F.1    Broccia, M.L.2    Giavini, E.3    Menegola, E.4
  • 55
    • 28644440158 scopus 로고    scopus 로고
    • Dokmanovic MHistone deacetylase inhibitors: Discovery and development as anticancer agents
    • [55] Marks PA. Dokmanovic MHistone deacetylase inhibitors: discovery and development as anticancer agents. Expert Opin Investig Drugs 2005; 14: 1497-511.
    • (2005) Expert Opin Investig Drugs , vol.14 , pp. 1497-1511
    • Marks, P.A.1
  • 56
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • [56] Bolden JE, Peart MJ, Johnstone RW. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 2006; 5: 769-84
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 57
    • 0037052687 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in Pglycoprotein-expressing cells
    • [57] Ruefli AA, Bernhard D, Tainton KM, Kofler R, Smyth MJ, Johnstone RW. Suberoylanilide hydroxamic acid (SAHA) overcomes multidrug resistance and induces cell death in Pglycoprotein-expressing cells. Int J Cancer 2002; 99: 292-8
    • (2002) Int J Cancer , vol.99 , pp. 292-298
    • Ruefli, A.A.1    Bernhard, D.2    Tainton, K.M.3    Kofler, R.4    Smyth, M.J.5    Johnstone, R.W.6
  • 58
    • 33750288048 scopus 로고    scopus 로고
    • Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
    • [58] Xu W, Ngo L, Perez G, Dokmanovic M, Marks PA. Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor. Proc Natl Acad Sci USA 2006, 103: 15540-5.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15540-15545
    • Xu, W.1    Ngo, L.2    Perez, G.3    Dokmanovic, M.4    Marks, P.A.5
  • 59
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules-from biology to health and disease
    • [59] Lillig CH, Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid Redox Signal 2007; 9: 25-47.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 60
    • 84866486549 scopus 로고    scopus 로고
    • Oxidative stress, thiols, and redox profiles
    • [60] Harris C and Hansen JC. Oxidative stress, thiols, and redox profiles. Methods Mol Biol 2012; 889: 325-46.
    • (2012) Methods Mol Biol , vol.889 , pp. 325-346
    • Harris, C.1    Hansen, J.C.2
  • 61
    • 76749126263 scopus 로고    scopus 로고
    • Ascorbic acid reverses valproic acid-induced inhibition of hoxa2 and maintains glutathione homeostasis inmouseembryos in culture
    • [61] Zhang B, Wang X, Nazarali AJ. Ascorbic acid reverses valproic acid-induced inhibition of hoxa2 and maintains glutathione homeostasis inmouseembryos in culture. Cell Mol Neurobiol 2010; 30: 137-48.
    • (2010) Cell Mol Neurobiol , vol.30 , pp. 137-148
    • Zhang, B.1    Wang, X.2    Nazarali, A.J.3
  • 62
    • 0034644938 scopus 로고    scopus 로고
    • Vitamin E decreases valproic acid induced neural tube defects in mice
    • [62] Al Deeb S, Al Moutaery K, Arshaduddin M, Tariq M. Vitamin E decreases valproic acid induced neural tube defects in mice. Neuroscience Lett 2000; 292: 179-82.
    • (2000) Neuroscience Lett , vol.292 , pp. 179-182
    • Al Deeb, S.1    Al Moutaery, K.2    Arshaduddin, M.3    Tariq, M.4
  • 63
    • 81555195488 scopus 로고    scopus 로고
    • Valproic acid increases formation of reactive oxygen species and induces apoptosis in postimplantation embryos: A role for oxidative stress in valproic acid-induced neural tube defects
    • [63] Tung EW, Winn LM. Valproic acid increases formation of reactive oxygen species and induces apoptosis in postimplantation embryos: a role for oxidative stress in valproic acid-induced neural tube defects. Mol Pharmacol 2011; 80: 979-87.
    • (2011) Mol Pharmacol , vol.80 , pp. 979-987
    • Tung, E.W.1    Winn, L.M.2
  • 64
    • 28844466046 scopus 로고    scopus 로고
    • Valproic acid monotherapy induces DNA oxidative damage
    • [64] Schulpis KH, Lazaropoulou C, Regoutas S, et al. Valproic acid monotherapy induces DNA oxidative damage. Toxicology 2006; 217: 228-32.
    • (2006) Toxicology , vol.217 , pp. 228-232
    • Schulpis, K.H.1    Lazaropoulou, C.2    Regoutas, S.3
  • 65
    • 77953228720 scopus 로고    scopus 로고
    • Effects of valproate, carbamazepine, and levetiracetam on the antioxidant and oxidant systems in epileptic patients and their clinical importance
    • [65] Varoglu AO, Yildirim A, Aygul R, Gundogdu OL, Sahin YN. Effects of valproate, carbamazepine, and levetiracetam on the antioxidant and oxidant systems in epileptic patients and their clinical importance. Clinical Neuropharmacol 2010; 33: 155-7.
    • (2010) Clinical Neuropharmacol , vol.33 , pp. 155-157
    • Varoglu, A.O.1    Yildirim, A.2    Aygul, R.3    Gundogdu, O.L.4    Sahin, Y.N.5
  • 66
    • 0042346416 scopus 로고    scopus 로고
    • Valproate induces replicationindependent active DNA demethylation
    • [66] Detich N, Bovenzi V, Szyf M. Valproate induces replicationindependent active DNA demethylation. J Biol Chem 2003; 278: 27586-92.
    • (2003) J Biol Chem , vol.278 , pp. 27586-27592
    • Detich, N.1    Bovenzi, V.2    Szyf, M.3
  • 67
    • 34047170360 scopus 로고    scopus 로고
    • Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes
    • [67] Milutinovic S, D’Alessio AC, Detich N, Szyf M. Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes. Carcinogenesis 2007; 28: 560-71.
    • (2007) Carcinogenesis , vol.28 , pp. 560-571
    • Milutinovic, S.1    D’Alessio, A.C.2    Detich, N.3    Szyf, M.4
  • 68
    • 33947368681 scopus 로고    scopus 로고
    • N, Histone deacetylase inhibitor trichostatin A induces global and gene-specific DNA demethylation in human cancer cell lines
    • [68] Ou JN, Torrisani J, Unterberger A, et al N, Histone deacetylase inhibitor trichostatin A induces global and gene-specific DNA demethylation in human cancer cell lines. Biochem Pharmacol 2007; 73: 1297-307.
    • (2007) Biochem Pharmacol , vol.73 , pp. 1297-1307
    • Ou, J.N.1    Torrisani, J.2    Unterberger, A.3
  • 69
    • 0022396998 scopus 로고
    • Cell cycle-dependent regulation of eukaryotic DNA methylase level
    • [69] Szyf M, Kaplan F, Mann V, Giloh H, Kedar E, Razin A. Cell cycle-dependent regulation of eukaryotic DNA methylase level. J Biol Chem 1985; 260: 8653-6.
    • (1985) J Biol Chem , vol.260 , pp. 8653-8656
    • Szyf, M.1    Kaplan, F.2    Mann, V.3    Giloh, H.4    Kedar, E.5    Razin, A.6
  • 70
    • 0042917464 scopus 로고    scopus 로고
    • Effects of vitamin B12 and folate deficiencies on DNA methylation and carcinogenesis in rat liver
    • [70] Brunaud L, Alberto JM, Ayav A, et al. Effects of vitamin B12 and folate deficiencies on DNA methylation and carcinogenesis in rat liver. Clin Chem Lab Med 2003; 41: 1012-9.
    • (2003) Clin Chem Lab Med , vol.41 , pp. 1012-1019
    • Brunaud, L.1    Alberto, J.M.2    Ayav, A.3
  • 71
    • 34447342598 scopus 로고    scopus 로고
    • Reduction in neural-tube defects after folic acid fortification in Canada
    • [71] De Wals P, Tairou F, Van Allen MI, et al. Reduction in neural-tube defects after folic acid fortification in Canada. N E J Med 2007; 357: 135-42.
    • (2007) N E J Med , vol.357 , pp. 135-142
    • De Wals, P.1    Tairou, F.2    Van Allen, M.I.3
  • 72
    • 0036057549 scopus 로고    scopus 로고
    • Incidence of open neural tube defects in Nova Scotia after folic acid fortification
    • [72] Persaud VL, Van den Hof MC, Dube JM, Zimmer P. Incidence of open neural tube defects in Nova Scotia after folic acid fortification. Can Med Ass J 2002; 167: 241-5.
    • (2002) Can Med Ass J , vol.167 , pp. 241-245
    • Persaud, V.L.1    Van Den Hof, M.C.2    Dube, J.M.3    Zimmer, P.4
  • 73
    • 0033150223 scopus 로고    scopus 로고
    • Failure of periconceptional folic acid to prevent a neural tube defect in the offspring of a mother taking sodium valproate
    • [73] Craig J, Morrison P, Morrow J, Patterson V. Failure of periconceptional folic acid to prevent a neural tube defect in the offspring of a mother taking sodium valproate. Seizure 1999; 8: 253-4.
    • (1999) Seizure , vol.8 , pp. 253-254
    • Craig, J.1    Morrison, P.2    Morrow, J.3    Patterson, V.4
  • 74
    • 0037974463 scopus 로고    scopus 로고
    • Clinical care of pregnant women with epilepsy: Neural tube defects and folic acid supplementation
    • [74] Yerby MS. Clinical care of pregnant women with epilepsy: neural tube defects and folic acid supplementation. Epilepsia 2003; 44(Suppl. 3): 33-40.
    • (2003) Epilepsia , vol.44 , Issue.3 , pp. 33-40
    • Yerby, M.S.1
  • 75
    • 67349202446 scopus 로고    scopus 로고
    • Spontaneous abortion and the prophylactic effect of folic acid supplementation in epileptic women undergoing antiepileptic therapy
    • [75] Pittschieler S, Brezinka C, Jahn B, Trinka E, et al. Spontaneous abortion and the prophylactic effect of folic acid supplementation in epileptic women undergoing antiepileptic therapy. J Neurol 2008; 255: 1926-31.
    • (2008) J Neurol , vol.255 , pp. 1926-1931
    • Pittschieler, S.1    Brezinka, C.2    Jahn, B.3    Trinka, E.4
  • 76
    • 0347060631 scopus 로고    scopus 로고
    • Amelioration of sodium valproate-induced neural tube defects in mouse fetuses by maternal folic acid supplementation during gestation
    • [76] Padmanabhan R, Shafiullah MM. Amelioration of sodium valproate-induced neural tube defects in mouse fetuses by maternal folic acid supplementation during gestation. Congenital Anomalies 2003; 43: 29-40.
    • (2003) Congenital Anomalies , vol.43 , pp. 29-40
    • Padmanabhan, R.1    Shafiullah, M.M.2
  • 77
    • 32544445967 scopus 로고    scopus 로고
    • Folic acid and pantothenic acid protection against valproic acid-induced neural tube defects in CD-1 mice
    • [77] Dawson JE, Raymond AM, Winn LM. Folic acid and pantothenic acid protection against valproic acid-induced neural tube defects in CD-1 mice. Toxicol App Pharmacol 2006; 211: 124-32.
    • (2006) Toxicol App Pharmacol , vol.211 , pp. 124-132
    • Dawson, J.E.1    Raymond, A.M.2    Winn, L.M.3
  • 78
    • 0029612799 scopus 로고
    • Effect of supplemental folic acid on valproic acid-induced embryotoxicity and tissue zinc levels in vivo
    • [78] Hansen DK, Grafton TF, Dial SL, Gehring TA, Siitonen PH. Effect of supplemental folic acid on valproic acid-induced embryotoxicity and tissue zinc levels in vivo. Teratology 1995; 52: 277-85.
    • (1995) Teratology , vol.52 , pp. 277-285
    • Hansen, D.K.1    Grafton, T.F.2    Dial, S.L.3    Gehring, T.A.4    Siitonen, P.H.5
  • 79
    • 84999352218 scopus 로고    scopus 로고
    • Folate, vitamin B12, inositol or pantothenic acid supplementation exacerbates the frequency of valproic acid induced neural tube defects
    • [79] Bennett GD, Ridge L, Finnell RH. Folate, vitamin B12, inositol or pantothenic acid supplementation exacerbates the frequency of valproic acid induced neural tube defects. Toxicologist 1998; 42: 262.
    • (1998) Toxicologist , vol.42 , pp. 262
    • Bennett, G.D.1    Ridge, L.2    Finnell, R.H.3
  • 80
    • 0025941823 scopus 로고
    • Homeotic transformations of murine vertebrae and concomitant alteration of hox codes induced by retinoic acid
    • [80] Kessel M, Gruss P. Homeotic transformations of murine vertebrae and concomitant alteration of hox codes induced by retinoic acid. Cell 1991, 67: 89-104.
    • (1991) Cell , vol.67 , pp. 89-104
    • Kessel, M.1    Gruss, P.2
  • 81
    • 0026772226 scopus 로고
    • Respecification of vertebral identities by retinoic acid
    • [81] Kessel M. Respecification of vertebral identities by retinoic acid. Development 1992, 115: 487-501.
    • (1992) Development , vol.115 , pp. 487-501
    • Kessel, M.1
  • 82
    • 84866542699 scopus 로고    scopus 로고
    • Valproic acid downregulates RBP4 and elicits hypervitaminosis A-teratogenesis. A kinetic analysis on retinol/retinoic acid homeostatic system
    • [82] Chuang CM, Chang CH, Wang HE, et al. Valproic acid downregulates RBP4 and elicits hypervitaminosis A-teratogenesis. A kinetic analysis on retinol/retinoic acid homeostatic system. PLOS ONE 2012, 7: e43692.
    • (2012) PLOS ONE , vol.7
    • Chuang, C.M.1    Chang, C.H.2    Wang, H.E.3
  • 83
    • 84865279633 scopus 로고    scopus 로고
    • Tang WWC, et al A paradoxical teratogenic mechanism for retinoic acid
    • [83] Lee LMY, Leung CY, Tang WWC, et al A paradoxical teratogenic mechanism for retinoic acid. PNAS 2012, 109: 13668-73.
    • (2012) PNAS , vol.109 , pp. 13668-13673
    • Lee, L.1    Leung, C.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.