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Volumn 21, Issue 11, 2011, Pages 760-768

Impact of UDP-gluconoryltransferase 2B17 genotype on vorinostat metabolism and clinical outcomes in Asian women with breast cancer

Author keywords

breast cancer; pharmacogenetics; UGT2B17; UGT2B17 2; vorinostat

Indexed keywords

EXEMESTANE; IBUPROFEN; VORINOSTAT;

EID: 80055016793     PISSN: 17446872     EISSN: 17446880     Source Type: Journal    
DOI: 10.1097/FPC.0b013e32834a8639     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 2642531973 scopus 로고    scopus 로고
    • Epigenetics in human disease and prospects for epigenetic therapy
    • Egger G, Liang G, Aparicio A, Jones PA. Epigenetics in human disease and prospects for epigenetic therapy. Nature 2004; 429:457-463.
    • (2004) Nature , vol.429 , pp. 457-463
    • Egger, G.1    Liang, G.2    Aparicio, A.3    Jones, P.A.4
  • 2
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB. The epigenomics of cancer. Cell 2007; 128:683-692.
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 4
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA, Baylin SB. The fundamental role of epigenetic events in cancer. Nat Rev Genet 2002; 3:415-428.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 5
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga MF, Ballestar E, Villar-Garea A, Boix-Chornet M, Espada J, Schotta G, et al. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 2005; 37:391-400.
    • (2005) Nat. Genet. , vol.37 , pp. 391-400
    • Fraga, M.F.1    Ballestar, E.2    Villar-Garea, A.3    Boix-Chornet, M.4    Espada, J.5    Schotta, G.6
  • 7
    • 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; 1:287-299.
    • (2002) Nat. Rev. Drug. Discov. , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 9
    • 21244464349 scopus 로고    scopus 로고
    • Phase I study of an oral histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced cancer
    • Kelly WK, O'Connor OA, Krug LM, Chiao JH, Heaney M, Curley T, et al. Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer. J Clin Oncol 2005; 23:3923-3931.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 3923-3931
    • Kelly, W.K.1    O'Connor, O.A.2    Krug, L.M.3    Chiao, J.H.4    Heaney, M.5    Curley, T.6
  • 10
    • 85047699941 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling
    • Deroanne CF, Bonjean K, Servotte S, Devy L, Colige A, Clausse N, et al. Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. Oncogene 2002; 21:427-436.
    • (2002) Oncogene , vol.21 , pp. 427-436
    • Deroanne, C.F.1    Bonjean, K.2    Servotte, S.3    Devy, L.4    Colige, A.5    Clausse, N.6
  • 11
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • USA
    • Richon VM, Emiliani S, Verdin E, Webb Y, Breslow R, Rifkind RA, et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc Natl Acad Sci USA 1998; 95:3003-3007.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3    Webb, Y.4    Breslow, R.5    Rifkind, R.A.6
  • 12
    • 1542588471 scopus 로고    scopus 로고
    • Second generation hybrid polar compounds are potent inducers of transformed cell differentiation
    • USA
    • Richon VM,Webb Y, Merger R, Sheppard T, Jursic B, Ngo L, et al. Second generation hybrid polar compounds are potent inducers of transformed cell differentiation. Proc Natl Acad Sci USA 1996; 93:5705-5708.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 5705-5708
    • Richon, V.M.1    Webb, Y.2    Merger, R.3    Sheppard, T.4    Jursic, B.5    Ngo, L.6
  • 13
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997; 389:349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 14
    • 0034297220 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment
    • Huang L, Pardee AB. Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment. Mol Med 2000; 6:849-866.
    • (2000) Mol. Med. , vol.6 , pp. 849-866
    • Huang, L.1    Pardee, A.B.2
  • 15
    • 0033367018 scopus 로고    scopus 로고
    • Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent suberanilohydroxamic acid SAHA
    • Cohen LA, Amin S, Marks PA, Rifkind RA, Desai D, Richon VM. Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent, suberanilohydroxamic acid (SAHA). Anticancer Res 1999; 19:4999-5005.
    • (1999) Anticancer Res. , vol.19 , pp. 4999-5005
    • Cohen, L.A.1    Amin, S.2    Marks, P.A.3    Rifkind, R.A.4    Desai, D.5    Richon, V.M.6
  • 16
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso-Sandoval T, Rosen N, Rifkind R, Marks PA, Richon VM. The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res 2001; 61:8492-8497.
    • (2001) Cancer Res. , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 18
    • 66149089601 scopus 로고    scopus 로고
    • Characterization of UGTs active against SAHA and association between SAHA glucuronidation activity phenotype with UGT genotype
    • Balliet RM, Chen G, Gallagher CJ, Dellinger RW, Sun D, Lazarus P. Characterization of UGTs active against SAHA and association between SAHA glucuronidation activity phenotype with UGT genotype. Cancer Res 2009; 69:2981-2989.
    • (2009) Cancer Res. , vol.69 , pp. 2981-2989
    • Balliet, R.M.1    Chen, G.2    Gallagher, C.J.3    Dellinger, R.W.4    Sun, D.5    Lazarus, P.6
  • 19
    • 58149242889 scopus 로고    scopus 로고
    • A phase II trial of vorinostat suberoylanilide hydroxamic acid in metastatic breast cancer: A california cancer consortium study
    • Luu TH, Morgan RJ, Leong L, Lim D, McNamara M, Portnow J, et al. A phase II trial of vorinostat (suberoylanilide hydroxamic acid) in metastatic breast cancer: a California Cancer Consortium Study. Clin Cancer Res 2008; 14:7138-7142.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 7138-7142
    • Luu, T.H.1    Morgan, R.J.2    Leong, L.3    Lim, D.4    McNamara, M.5    Portnow, J.6
  • 21
    • 32544455635 scopus 로고    scopus 로고
    • Large differences in testosterone excretion in Korean and Swedish men are strongly associated with a UDP-glucuronosyl transferase 2B17 polymorphism
    • Jakobsson J, Ekstrom L, Inotsume N, Garle M, Lorentzon M, Ohlsson C, et al. Large differences in testosterone excretion in Korean and Swedish men are strongly associated with a UDP-glucuronosyl transferase 2B17 polymorphism. J Clin Endocrinol Metab 2006; 91:687-693.
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 687-693
    • Jakobsson, J.1    Ekstrom, L.2    Inotsume, N.3    Garle, M.4    Lorentzon, M.5    Ohlsson, C.6
  • 22
    • 33748057111 scopus 로고    scopus 로고
    • Deletion polymorphism of UDP-glucuronosyltransferase 2B17 and risk of prostate cancer in African American and Caucasian men
    • Park J, Chen L, Ratnashinge L, Sellers TA, Tanner JP, Lee JH, et al. Deletion polymorphism of UDP-glucuronosyltransferase 2B17 and risk of prostate cancer in African American and Caucasian men. Cancer Epidemiol Biomarkers Prev 2006; 15:1473-1478.
    • (2006) Cancer Epidemiol. Biomarkers Prev. , vol.15 , pp. 1473-1478
    • Park, J.1    Chen, L.2    Ratnashinge, L.3    Sellers, T.A.4    Tanner, J.P.5    Lee, J.H.6
  • 24
    • 0024536437 scopus 로고
    • Optimal two-stage designs for phase II clinical trials
    • Simon R. Optimal two-stage designs for phase II clinical trials. Control Clin Trials 1989; 10:1-10.
    • (1989) Control. Clin. Trials , vol.10 , pp. 1-10
    • Simon, R.1
  • 25
    • 33947356688 scopus 로고    scopus 로고
    • Early stopping clinical trials of binomial response with an exact group sequential method
    • Zhao Z. Early stopping clinical trials of binomial response with an exact group sequential method. Stat Med 2007; 26:1724-1729.
    • (2007) Stat. Med. , vol.26 , pp. 1724-1729
    • Zhao, Z.1
  • 27
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M, Kijima M, Akita M, Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 1990; 265:17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 28
    • 73949140461 scopus 로고    scopus 로고
    • Carboplatin and Paclitaxel in combination with either vorinostat or placebo for first-line therapy of advanced non-small-cell lung cancer
    • Ramalingam SS, Maitland ML, Frankel P, Argiris AE, Koczywas M, Gitlitz B, et al. Carboplatin and Paclitaxel in combination with either vorinostat or placebo for first-line therapy of advanced non-small-cell lung cancer. J Clin Oncol 2010; 28:56-62.
    • (2010) J. Clin. Oncol. , vol.28 , pp. 56-62
    • Ramalingam, S.S.1    Maitland, M.L.2    Frankel, P.3    Argiris, A.E.4    Koczywas, M.5    Gitlitz, B.6
  • 29
    • 77957243014 scopus 로고    scopus 로고
    • Characterization of 17-dihydroexemestane glucuronidation: Potential role of the UGT2B17 deletion in exemestane pharmacogenetics
    • Sun D, Chen G, Dellinger RW, Sharma AK, Lazarus P. Characterization of 17-dihydroexemestane glucuronidation: potential role of the UGT2B17 deletion in exemestane pharmacogenetics. Pharmacogenet Genomics 2010; 20:575-585.
    • (2010) Pharmacogenet Genomics , vol.20 , pp. 575-585
    • Sun, D.1    Chen, G.2    Dellinger, R.W.3    Sharma, A.K.4    Lazarus, P.5
  • 31
    • 33748360764 scopus 로고    scopus 로고
    • Vorinostat a histone deacetylase inhibitor enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci
    • Munshi A, Tanaka T, Hobbs ML, Tucker SL, Richon VM, Meyn RE. Vorinostat a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol Cancer Ther 2006; 5:1967-1974.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1967-1974
    • Munshi, A.1    Tanaka, T.2    Hobbs, M.L.3    Tucker, S.L.4    Richon, V.M.5    Meyn, R.E.6
  • 32
    • 0038620379 scopus 로고    scopus 로고
    • Cotreatment with the histone deacetylase inhibitor suberoylanilide hydroxamic acid SAHA enhances imatiniβ-induced apoptosis of Bcr-Abl-positive human acute leukemia cells
    • Nimmanapalli R, Fuino L, Stobaugh C, Richon V, Bhalla K. Cotreatment with the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) enhances imatiniβ-induced apoptosis of Bcr-Abl-positive human acute leukemia cells. Blood 2003; 101:3236-3239.
    • (2003) Blood , vol.101 , pp. 3236-3239
    • Nimmanapalli, R.1    Fuino, L.2    Stobaugh, C.3    Richon, V.4    Bhalla, K.5
  • 33
    • 16544379283 scopus 로고    scopus 로고
    • Sequence-specific potentiation of topoisomerase II inhibitors by the histone deacetylase inhibitor suberoylanilide hydroxamic acid
    • Marchion DC, Bicaku E, Daud AI, Richon V, Sullivan DM, Munster PN. Sequence-specific potentiation of topoisomerase II inhibitors by the histone deacetylase inhibitor suberoylanilide hydroxamic acid. J Cell Biochem 2004; 92:223-237.
    • (2004) J. Cell. Biochem. , vol.92 , pp. 223-237
    • Marchion, D.C.1    Bicaku, E.2    Daud, A.I.3    Richon, V.4    Sullivan, D.M.5    Munster, P.N.6
  • 34
    • 41549151359 scopus 로고    scopus 로고
    • Response of preclinical medulloblastoma models to combination therapy with 13-cis retinoic acid and suberoylanilide hydroxamic acid SAHA
    • Spiller SE, Ditzler SH, Pullar BJ, Olson JM. Response of preclinical medulloblastoma models to combination therapy with 13-cis retinoic acid and suberoylanilide hydroxamic acid (SAHA). J Neurooncol 2008; 87:133-141.
    • (2008) J. Neurooncol. , vol.87 , pp. 133-141
    • Spiller, S.E.1    Ditzler, S.H.2    Pullar, B.J.3    Olson, J.M.4
  • 35
    • 76649088181 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor vorinostat to restore hormone sensitivity to the antiestrogen tamoxifen in patients with advanced breast cancer who progressed on prior hormone therapy
    • 15s (Suppl; abstr 1075
    • Munster PN, Lacevic M, Thomas S, Christian C, Ismail-Khan R, Melisko M, Rugo H. Phase II trial of the histone deacetylase inhibitor, vorinostat, to restore hormone sensitivity to the antiestrogen tamoxifen in patients with advanced breast cancer who progressed on prior hormone therapy. J Clin Oncol 2009; 27:15s (Suppl; abstr 1075).
    • (2009) J. Clin. Oncol. , vol.27
    • Munster, P.N.1    Lacevic, M.2    Thomas, S.3    Christian, C.4    Ismail-Khan, R.5    Melisko, M.6    Rugo, H.7
  • 36
    • 38949096781 scopus 로고    scopus 로고
    • Phase 1 study of the histone deacetylase inhibitor vorinostat suberoylanilide hydroxamic acid SAHA in patients with advanced leukemias and myelodysplastic syndromes
    • Garcia-Manero G,Yang H, Bueso-Ramos C, Ferrajoli A, Cortes J,WierdaWG, et al. Phase 1 study of the histone deacetylase inhibitor vorinostat [suberoylanilide hydroxamic acid (SAHA)] in patients with advanced leukemias and myelodysplastic syndromes. Blood 2008; 111:1060-1066.
    • (2008) Blood , vol.111 , pp. 1060-1066
    • Garcia-Manero, G.1    Yang, H.2    Bueso-Ramos, C.3    Ferrajoli, A.4    Cortes, J.5    Wierda, W.G.6
  • 37
    • 34249941680 scopus 로고    scopus 로고
    • Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma
    • USA
    • Lindemann RK, Newbold A,Whitecross KF, Cluse LA, Frew AJ, Ellis L, et al. Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma. Proc Natl Acad Sci USA 2007; 104:8071-8076.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 8071-8076
    • Lindemann, R.K.1    Newbold, A.2    Whitecross, K.F.3    Cluse, L.A.4    Frew, A.J.5    Ellis, L.6
  • 38
    • 36448988881 scopus 로고    scopus 로고
    • A functional genetic screen identifies retinoic acid signaling as a target of histone deacetylase inhibitors
    • USA
    • Epping MT, Wang L, Plumb JA, Lieb M, Gronemeyer H, Brown R, et al. A functional genetic screen identifies retinoic acid signaling as a target of histone deacetylase inhibitors. Proc Natl Acad Sci USA 2007; 104: 17777-17782.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 17777-17782
    • Epping, M.T.1    Wang, L.2    Plumb, J.A.3    Lieb, M.4    Gronemeyer, H.5    Brown, R.6
  • 39
    • 53449090857 scopus 로고    scopus 로고
    • Molecular and biologic characterization and drug sensitivity of pan-histone deacetylase inhibitor-resistant acute myeloid leukemia cells
    • Fiskus W, Rao R, Fernandez P, Herger B, Yang Y, Chen J, et al. Molecular and biologic characterization and drug sensitivity of pan-histone deacetylase inhibitor-resistant acute myeloid leukemia cells. Blood 2008; 112: 2896-2905.
    • (2008) Blood , vol.112 , pp. 2896-2905
    • Fiskus, W.1    Rao, R.2    Fernandez, P.3    Herger, B.4    Yang, Y.5    Chen, J.6
  • 40
    • 45549083112 scopus 로고    scopus 로고
    • Constitutive activation of signal transducers and activators of transcription predicts vorinostat resistance in cutaneous T-cell lymphoma
    • Fantin VR, Loboda A, Paweletz CP, Hendrickson RC, Pierce JW, Roth JA, et al. Constitutive activation of signal transducers and activators of transcription predicts vorinostat resistance in cutaneous T-cell lymphoma. Cancer Res 2008; 68:3785-3794.
    • (2008) Cancer Res. , vol.68 , pp. 3785-3794
    • Fantin, V.R.1    Loboda, A.2    Paweletz, C.P.3    Hendrickson, R.C.4    Pierce, J.W.5    Roth, J.A.6
  • 41
    • 67349157687 scopus 로고    scopus 로고
    • Biomarkers for predicting clinical responses to HDAC inhibitors
    • Stimson L, La Thangue NB. Biomarkers for predicting clinical responses to HDAC inhibitors. Cancer Lett 2009; 280:177-183.
    • (2009) Cancer Lett. , vol.280 , pp. 177-183
    • Stimson, L.1    La Thangue, N.B.2
  • 42
    • 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 AC, Dietel M, et al. 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 2008; 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
  • 43
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • Weichert W, Roske A, Gekeler V, Beckers T, Stephan C, Jung K, et al. Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. Br J Cancer 2008; 98:604-610.
    • (2008) Br. J. Cancer , vol.98 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6


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