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Drug Evaluation

Vorinostat: a new oral histone deacetylase inhibitor approved for cutaneous T-cell lymphoma

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Pages 1111-1120 | Published online: 26 Jun 2007

Bibliography

  • GIARDI M, HEALD PW, WILSON LD: The pathogenesis of mycosis fungoides. N. Engl. J. Med. (2004) 350:1978-1988.
  • KAZAKOV DV, BURG G, KEMPF W: Clinicopathological spectrum of mycosis fungoides. J. Eur. Acad. Dermatol. Venereol. (2004) 18:397-415.
  • PICARDO DA, QUERFELD C, GUITART J et al.: Cutaneous T-cell lymphoma: a paradigm for biological therapies. Leukemia Lymphoma (2004) 45(9):1755-1765.
  • JACKOW CM, MCHAM JB, FRISS A et al.: HLA-DR5 and DQB1*03 class II alleles are associated with cutaneous T-cell lymphoma. J. Invest. Dermatol. (1996) 107:373-376.
  • KIM EJ, HESS S, RICHARDSON SK et al.: Immunopathogenesis and therapy of cutaneous T cell lymphoma. J. Clin. Invest. (2005) 115:798-812.
  • BERGER CL, HANLON D, KANADA D et al.: The growth of cutaneous T-cell lymphoma is stimulated by immature dendritic cells. Blood (2002) 99:2929-2939.
  • VEGA F, LUTHRA R, MEDEIROS LJ et al.: Clonal heterogeneity in mycosis fungoides and its relationship to clinical course. Blood (2002) 100:3369-3373.
  • ROOK AH, GOTTLIEB SL, WOLFE JT et al.: Pathogenesis of cutaneous T-cell lymphoma: implications for the use of recombinant cytokines and photopheresis. Clin. Exp. Immunol. (1997) 107(Suppl. 1):16-20.
  • DUVIC M, TALPUR R, NI Xet al.: Phase II trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL). Blood (2007) 109(1):31-39.
  • ZHANG C, RICHON V, NI Xet al.: Selective induction of apoptosis by histone deacetylase inhibitor SAHA in cutaneous T-cell lymphoma cells: relevance to mechanism of therapeutic action. J. Invest. Dermatol. (2005) 125(5):1045-1052.
  • KELLY W, O’CONNOR A, KRUG LM et al.: Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer. J. Clin. Oncol. (2005) 23(17):3923-3931.
  • DUVIC M, ZHANG C: Clinical and laboratory experience of vorinostat (suberoylanilide hydroxamic acid) in the treatment of cutaneous T-cell lymphoma. Br. J. Cancer (2006) 95(Suppl. 1):S13-S19.
  • HEIDER U, KAISER M, STERZ J et al.: Histone deacetylase inhibitors reduce VEGF production and induce growth suppression and apoptosis in human mantle cell lymphoma. Eur. J. Haematol. (2006) 76:42-50.
  • DE RUIJTER AJ, VAN GENNIP AH, CARON HN et al.: Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem. J. (2003) 370(Part 3):737-749.
  • GREGORETTI IV, LEE YM, GOODSON HV: Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. (2004) 338:17-31.
  • LEDENT V, VERVOORT M: Comparative genomics of class 4 histone deacetylases indicates a complex evolutionary history. BMC Biol. (2006) 4:24.
  • BLANDER G, GUARENTE L: The Sir2 family of protein deacetylases. Ann. Rev. Biochem. (2004) 73:417-435.
  • GREGORETTI IV, LEE YM, GOODSON HV: Molecular evolution of histone deacetylase family: functional implications of phylogenetic analysis. J. Mol. Biol. (2004) 338:17-31.
  • FURUMAI R, MATSUYAMA A, KOBASHI N et al.: FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res. (2002) 62:4916-4921.
  • KELLY WK, MARKS PA: Drug insight: histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide development of the new targeted anticancer agent suberoylanilide hydroxamic acid. Nat. Clin. Paract. Oncol. (2005) 2:150-157.
  • O’CONNOR OA: Developing new drugs for the treatment of lymphoma. Eur. J. Haematol. Suppl. (2005) (66):150-158.
  • BUTLER L, AGUS B, SCHER HI et al.: Suberoylanilide hydroxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo. Cancer Res. (2000) 60(18):5165-5170.
  • BUTLER L, ZHOU MX: The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc. Natl. Acad. Sci. USA (2002) 99(18):11700-11705.
  • MARCHION DC, BICAKU E, DAUD AI et al.: Sequence-specific potentiation of topoisomerase II inhibitors by the histone deacetylase inhibitor suberoylanilide hydroxamic acid. J. Cell Biochem. (2004) 92(2):223-237.
  • ALMENARA J, ROSATO R, GRANT S: Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA). Leukemia (2002) 16(7):1331-1343.
  • NIMMANAPALLI R, FUINO L, STOBAUGH C et al.: Cotreatment with the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) enhances imatinib-induced apoptosis of Bcr-Abl-positive human acute leukemia cells. Blood (2003) 101(8):3236-3239.
  • HE LZ, TOLENTINO T, GRAYSON P et al.: Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia. J. Clin. Invest. (2001) 108(9):1321-1330.
  • SAKAJIRI S, KUMAGAI T, KAWAMATA N et al.: Histone deacetylase inhibitors profoundly decrease proliferation of human lymphoid cancer cell lines. Exp. Hematol. (2005) 33(1):53-61.
  • KELLY W, K V, RICHON M, O’CONNOR O et al.: Phase I clinical trial of histone deacetylase inhibitor: suberoylanilide hydroxamic acid administered intravenously. Clin. Cancer Res. (2003) 9(10 Part 1):3578-3588.
  • O’CONNOR O, HEANEY L, SCHWARTZ L et al.: Clinical experience with intravenous and oral formulations of the novel histone deacetylase inhibitor suberoylanilide hydroxamic acid in patients with advanced hematologic malignancies. J. Clin. Oncol. (2006) 24(1):166-173.
  • GARCIA-MANERO G, YANG H, SANCHEZ-GONZALEZ B et al.: Final results of a Phase I study of the histone deacetylase inhibitor vorinostat (suberoylanilide hydroxamic acid, SAHA) in patients with leukemia and myelodysplastic syndrome. Blood. (2005) 106:785a (Abstract).
  • BUTLER L, LIAPIS MV, BOURALEXIS S et al.: The histone deacetylase inhibitor, suberoylanilide hydroxamic acid, overcomes resistance of human breast cancer cells to Apo2L/TRAIL. Int. J. Cancer (2006) 119(4):944-954.
  • VONDERHEID E, BERNENGO G, BURG G et al.: Update on erythrodermic cutaneous T-cell lymphoma: report of the International Society for Cutaneous Lymphomas. J. Am. Acad. Dermatol. (2002) 46(1):95-106.
  • LAKSHMIKANTHAN V, KADDOUR-DJEBBAR I, LEWIS RW, KUMAR MV: SAHA-sensitized prostate cancer cells to TNFalpha-related apoptosis-inducing ligand (TRAIL): mechanisms leading to synergistic apoptosis. Int. J. Cancer (2006) 119(1):221-8.
  • VRANA JA, DECKER RH, JOHNSON CR et al.: Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53. Oncogene (1999) 18:7016-7025.
  • DESAI D, DAS A: Chemopreventive efficacy of suberoylanilide hydroxamic acid (SAHA) against 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in female A/J mice. Anticancer Res. (2003) 23(1A):499-503.
  • MORADEI O, MAROUN CR, PAQUIN I, VAISBURG A: Histone deacetylase inhibitors: latest developments, trends, and prospects. Curr. Med. Chem. Anticancer Agents (2005) 5:529-560.
  • MARKS P, RIFKIND RA, RICHON VM et al.: Histone deacetylases and cancer: causes and therapies. Nat. Rev. Cancer (2001) 1:194-202.
  • MARKS PA, DOKMANOVIC M: Histone deacetylase inhibitors: discovery and development as anticancer agents. Expert Opin. Investig. Drugs (2005) 14(12):1497-1511.
  • BUTLER LM, AGUS DB, SCHER HI et al.: Suberoylanilide hydoxamic acid, an inhibitor of histone deacetylase, suppresses the growth of prostate cancer cells in vitro and in vivo. Cancer Res. (2000) 60:5165-5170.
  • RICHON VM, EMILIANI S, VERDIN E et al.: A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc. Natl. Acad. Sci. USA (1998) 95:3003-3007.
  • RICHON VM, SANDHOFF TW, RIFKIND RA, MARKS PA: Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. USA (2000) 97:10014-10019.
  • GUI CY, NGO L, XU WS, RICHON VM, MARKS PA: Histone deacetylase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc. Natl. Acad. Sci. USA (2004) 101:1241-1246.
  • ROSATO RR, ALMENARA JA, DAI Y, GRANT S: Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol. Cancer Ther. (2003) 2:1273-1284.
  • SHAO Y, GAO Z, MARKS PA, JIANG X: Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc. Natl. Acad. Sci. USA (2004) 101:18030-18035.
  • GUO F, SIGUA C, TAO J et al.: Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells. Cancer Res. (2004) 64:2580-2589.
  • UNGERSTEDT JS, SOWA Y, XU WS et al.: Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc. Natl. Acad. Sci. USA (2005) 102:673-678.
  • PIEKARZ RL, ROBEY RW, ZHAN Z et al.: T-cell lymphoma as a model for the use of histone deacetylase inhibitors in cancer therapy: impact of depsipeptide on molecular markers, therapeutic targets, and mechanisms of resistance. Blood (2004) 103(12):4636-4643.
  • MARKS PA, JIANG X: Histone deacetylase inhibitors in programmed cell death and cancer therapy. Cell Cycle (2005) 4:549-551.
  • MEI S, HO AD, MAHLKNECHT U: Role of histone deacetylase inhibitors in the treatment of cancer. Int. J. Oncol. (2004) 25:1509-1519.
  • SOMECH R, IZRAELI S, SIMON J: Histone deacetylase inhibitors – a new tool to treat cancer. Cancer Treat. Rev. (2004) 30:461-472.
  • SOMMER VH, CLEMMENSEN OJ, NIELSEN O et al.: In vivo activation of STAT3 in cutaneous T-cell lymphoma. Evidence for an antiapoptotic function of STAT3. Leukemia (2004) 18:1288-1295.
  • TURKSON J: STAT proteins as novel targets for cancer drug discovery. Expert Opin. Ther. Targets (2004) 8:409-422.
  • MITCHELL TJ, JOHN S: Signal transducer and activator of transcription (STAT) signaling and T-cell lymphomas. Immunology (2005) 114:301-312.
  • DUVIC M, KIMYH, KUZEL TM et al.: Vorinostat (suberoylanilide hydroxamic acid, (SAHA) provides prolonged clinical benefit to advanced ctcl patients: updated results of Phase IIb multicenter clinical trial. Blood (2006) 108(11):112a (Abstract 399).
  • OLSEN E: Vorinostat (suberoylanilide hydroxamic acid, SAHA) is clinically active in advanced cutaneous T-cell lymphoma (CTCL): results of Phase IIB trial. ASCO Annual Meeting Proceedings (2006) 24(Suppl., Part 1):7500.
  • MANN BS, JOHNSON JR, HE K et al.: Vorinostat for treatment of cutaneous manifestations of advanced primary cutaneous T-cell lymphoma. Clin. Cancer Res. (2007) 13:2318-2322.
  • DUVIC M, HYMES K, HEALD P et al.: Bexarotene is effective and safe for treatment of refractory advanced-stage cutaneous T-cell lymphoma: Multinational Phase II-III trial results. J. Clin. Oncol. (2001) 19:2456-2471.
  • BOLDEN JE, PEART MJ, JOHNSTONE RW: Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. (2006) 5:769-784.

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