Next generation histone deacetylase inhibitors: the answer to the search for optimized epigenetic therapies?

Bibliography

• Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 1999;9(1):40-8
   PubMed Web of Science ®Google Scholar
• Biancotto C, Frige G, Minucci S. Histone modification therapy of cancer. Adv Genet 2010;6:341-86
   Google Scholar
• Kouzarides T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J 2000;19(6):1176-9
   PubMed Web of Science ®Google Scholar
• Choudhary C, Kumar C, Gnad F, Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009;325(5942):834-40
   PubMed Web of Science ®Google Scholar
• Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006;6(1):38-51
   PubMed Web of Science ®Google Scholar
• Mercurio C, Minucci S, Pelicci PG. Histone deacetylases and epigenetic therapies of hematological malignancies. Pharmacol Res 2010;62(1):18-34
   PubMed Web of Science ®Google Scholar
• Tan J, Cang S, Ma Y, Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents. J Hematol Oncol 2010;3:5
   PubMed Web of Science ®Google Scholar
• Copeland A, Buglio D, Younes A. Histone deacetylase inhibitors in lymphoma. Curr Opin Oncol 2010;22(5):431-6
   PubMed Web of Science ®Google Scholar
• Prince HM, Bishton MJ, Harrison SJ. Clinical studies of histone deacetylase inhibitors. Clin Cancer Res 2009;15(12):3958-69
   PubMed Web of Science ®Google Scholar
• Lane AA, Chabner BA. Histone deacetylase inhibitors in cancer therapy. J Clin Oncol 2009;27(32):5459-68
   PubMed Web of Science ®Google Scholar
• Glaser KB. HDAC inhibitors: clinical update and mechanism-based potential. Biochem Pharmacol 2007;74(5):659-71
   PubMed Web of Science ®Google Scholar
• Marks PA. Discovery and development of SAHA as an anticancer agent. Oncogene 2007;26(9):1351-6
   PubMed Web of Science ®Google Scholar
• Piekarz RL, Frye R, Turner M, Phase II multi-institutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma. J Clin Oncol 2009:5410-17
   PubMed Web of Science ®Google Scholar
• Gottlicher M. Valproic acid: an old drug newly discovered as inhibitor of histone deacetylases. Ann Hematol 2004;83(Suppl 1):S91-2
   PubMedGoogle Scholar
• Duenas-Gonzalez A, Candelaria M, Perez-Plascencia C, Valproic acid as epigenetic cancer drug: preclinical, clinical and transcriptional effects on solid tumors. Cancer Treat Rev 2008;34(3):206-22
   PubMed Web of Science ®Google Scholar
• Blaheta RA, Cinatl J Jr. Anti-tumor mechanisms of valproate: a novel role for an old drug. Med Res Rev 2002;22(5):492-511
   PubMed Web of Science ®Google Scholar
• Graham JS, Kaye SB, Brown R. The promises and pitfalls of epigenetic therapies in solid tumours. Eur J Cancer 2009;45(7):1129-36
   PubMed Web of Science ®Google Scholar
• Marsoni S, Damia G, Camboni G. A work in progress: the clinical development of histone deacetylase inhibitors. Epigenetics 2008;3(3):164-71
   PubMed Web of Science ®Google Scholar
• Botrugno OA, Santoro F, Minucci S. Histone deacetylase inhibitors as a new weapon in the arsenal of differentiation therapies of cancer. Cancer Lett 2009;280(2):134-44
   PubMed Web of Science ®Google Scholar
• Carew JS, Giles FJ, Nawrocki ST. Histone deacetylase inhibitors: Mechanisms of cell death and promise in combination cancer therapy. Cancer Lett 2008;269(1):7-17
   PubMed Web of Science ®Google Scholar
• Nolan L, Johnson PW, Ganesan A, Will histone deacetylase inhibitors require combination with other agents to fulfil their therapeutic potential? Br J Cancer 2008;99(5):689-94
   PubMed Web of Science ®Google Scholar
• Mahboobi S, Dove S, Sellmer A, Design of chimeric histone deacetylase- and tyrosine kinase-inhibitors: a series of imatinib hybrides as potent inhibitors of wild-type and mutant BCR-ABL, PDGF-Rbeta, and histone deacetylases. J Med Chem 2009;52(8):2265-79
   PubMed Web of Science ®Google Scholar
• Cai X, Zhai HX, Wang J, Discovery of 7-(4-(3-ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanam ide (CUDc-101) as a potent multi-acting HDAC, EGFR, and HER2 inhibitor for the treatment of cancer. J Med Chem 2010;53(5):2000-9
   PubMed Web of Science ®Google Scholar
• Lai CJ, Bao R, Tao X, CUDC-101, a multitargeted inhibitor of histone deacetylase, epidermal growth factor receptor, and human epidermal growth factor receptor 2, exerts potent anticancer activity. Cancer Res 2010;70(9):3647-56
   PubMed Web of Science ®Google Scholar
• Shimizu T, Tolcher AW, LoRusso P, 364 The first-in-human, first-in-class study of CUDC-101, a multi-targeted inhibitor of HDAC, EGFR, and HER2: a Phase I study in patients with advanced cancer. Eur J Cancer Suppl 2010;8(7):115
   Web of Science ®Google Scholar
• Andersen JB, Factor VM, Marquardt JU, An integrated genomic and epigenomic approach predicts therapeutic response to zebularine in human liver cancer. Sci Transl Med 2010;2(54): 54ra77
   Web of Science ®Google Scholar
• Altucci L, Minucci S. Epigenetic therapies in haematological malignancies: searching for true targets. Eur J Cancer 2009;45(7):1137-45
   PubMed Web of Science ®Google Scholar
• Gargiulo G, Minucci S. Epigenomic profiling of cancer cells. Int J Biochem Cell Biol 2009;41(1):127-35
   PubMed Web of Science ®Google Scholar
• Bradner JE, West N, Grachan ML, Chemical phylogenetics of histone deacetylases. Nat Chem Biol 2010;6(3):238-43
   PubMed Web of Science ®Google Scholar
• Elaut G, Rogiers V, Vanhaecke T. The pharmaceutical potential of histone deacetylase inhibitors. Curr Pharm Des 2007;13(25):2584-620
   PubMed Web of Science ®Google Scholar
• Ryan QC, Headlee D, Acharya M, Phase I and pharmacokinetic study of MS-275, a histone deacetylase inhibitor, in patients with advanced and refractory solid tumors or lymphoma. J Clin Oncol 2005;23(17):3912-22
   PubMed Web of Science ®Google Scholar
• Saito A, Yamashita T, Mariko Y, A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. Proc Natl Acad Sci USA 1999;96(8):4592-7
   PubMed Web of Science ®Google Scholar
• Wang H, Dymock BW. New patented histone deacetylase inhibitors. Expert Opin Ther Pat 2009;19(12):1727-57
   PubMed Web of Science ®Google Scholar
• Yeo P, Xin L, Goh E, Development and validation of high-performance liquid chromatography-tandem mass spectrometry assay for 6-(3-benzoyl-ureido)-hexanoic acid hydroxyamide, a novel HDAC inhibitor, in mouse plasma for pharmacokinetic studies. Biomed Chromatogr 2007;21(2):184-9
   PubMed Web of Science ®Google Scholar
• Sangthongpitag K, Wang H, Yeo P, ADME and PK/PD attributes of SB939, a potent orally active HDAC inhibitor Eur J Cancer Suppl 2006;4(12):53
   Web of Science ®Google Scholar
• Novotny-Diermayr V, Sangthongpitag K, Hu CY, SB939, a novel potent and orally active histone deacetylase inhibitor with high tumor exposure and efficacy in mouse models of colorectal cancer. Mol Cancer Ther 2010;9(3):642-52
   PubMed Web of Science ®Google Scholar
• Yong W, Goh B, Toh H, Phase I study of SB939 three times weekly for 3 weeks every 4 weeks in patients with advanced solid malignancies. J Clin Oncol 2009;27(15): abstract 2560
   PubMedGoogle Scholar
• Mandl-Weber S, Meinel FG, Jankowsky R, The novel inhibitor of histone deacetylase resminostat (RAS2410) inhibits proliferation and induces apoptosis in multiple myeloma (MM) cells. Br J Haematol 2010;149(4):518-28
   PubMed Web of Science ®Google Scholar
• Brunetto AT, Ang JE, Lal R, A first-in-human phase I study of 4SC-201, an oral histone deacetylase (HDAC) inhibitor, in patients with advanced solid tumors [abstr 3530]. J Clin Oncol 2009;27:15s
   Web of Science ®Google Scholar
• Hauns B, Mais A, Jankowsky R, Centralised analysis of phase I ECG dataset of resminostat, a new oral histone deacetylase inhibitor (HDACi). Eur J Cancer Suppl 2010;8(7):172
   Web of Science ®Google Scholar
• Bitzer M, Horger M, Ebert M, First clinical data of resminostat, a novel oral histone deacetylase (HDAC) inhibitor, in patients with hepatocellular carcinoma (HCC) – the SHELTER Study. ‘Viszeralmedizin 2010’ Symposium; organized by the German Gastroenterology (DGVS) and Visceral Surgery Associations (DGAV). Stuttgart, Germany; 2010. p. P432
   Google Scholar
• Arts J, King P, Marien A, JNJ-26481585, a novel ‘second-generation’ oral histone deacetylase inhibitor, shows broad-spectrum preclinical antitumoral activity. Clin Cancer Res 2009;15(22):6841-51
   PubMed Web of Science ®Google Scholar
• Hickson I, King P, Marien A, Preclinical assessment of the HDAC inhibitor JNJ-26481585: potent in vivo activity across a broad spectrum of human tumor xenografts. AACR Meeting Abstracts 2010;2010:5441
   Google Scholar
• Postel-Vinay S, Kristeleit R, Fong P, Preliminary results of an open-label phase I pharmacokinetic/pharmacodynamic study of JNJ26481585: early evidence of antitumor activity. J Clin Oncol 2009;27(20 Suppl 15S ):e13504
   Google Scholar
• Donald A, Belfield A, Day F, The discovery and Anti-Tumor Activity CHR-3996 – A Novel, Orally Available Inhibitor of Class 1 Histone Deacetylases. EFMC-ISMC (European Federation for Medicinal Chemistry) 2010, XXIst International Symposium on Medicinal Chemistry. Brussels 2010:PC 365
   Google Scholar
• Banerji U, van Doorn L, Papadatos-Pastos D, A phase I pharmacokinetic (PK) and pharmacodynamic (PD) study of CHR-3996, a class 1 selective histone deacetylase inhibitor (HDACi), in patients with advanced solid tumors. J Clin Oncol 2010;28(15 Suppl):2552
   Google Scholar
• Lu Q, Wang DS, Chen CS, Structure-based optimization of phenylbutyrate-derived histone deacetylase inhibitors. J Med Chem 2005;48(17):5530-5
   PubMed Web of Science ®Google Scholar
• Lucas DM, Alinari L, West DA, The novel deacetylase inhibitor AR-42 demonstrates pre-clinical activity in B-cell malignancies in vitro and in vivo. PLoS One 2010;5(6):e10941
   PubMed Web of Science ®Google Scholar
• Kulp SK, Chen CS, Wang DS, Antitumor effects of a novel phenylbutyrate-based histone deacetylase inhibitor, (S)-HDAC-42, in prostate cancer. Clin Cancer Res 2006;12(17):5199-206
   PubMed Web of Science ®Google Scholar
• Cheng H, Liu Z, Kulp SK, Preclinical pharmacokinetic studies with s-HDAC-42 (NSC 736012), an inhibitor of histone deacetylase, by LC-MS/MS. Proc Am Assoc Cancer Res 2006;47: abstract 3091
   Google Scholar
• Cheng H, Jones W, Wei X, Preclinical pharmacokinetics studies of R- and S- enantiomers of the histone deacetylase inhibitor, HDAC-42 (NSC 731438), in the rat. Proc Am Assoc Cancer Res 2006;47: abstract 686
   Google Scholar
• Oh ET, Park MT, Choi BH, Novel histone deacetylase inhibitor CG200745 induces clonogenic cell death by modulating acetylation of p53 in cancer cells. Invest New Drugs 2010 published online 27 October 2010, doi:10.1007/s10637-010-9568-2
   Google Scholar
• Hyun Y-L, Kim HJ, Kim YE, Preclinical studies of CG200745, novel histone deacetylase inhibitor discovered using structure-based drug discovery technologies. AACR Meeting Abstracts 2009 2009;2009:4561
   Google Scholar
• Lee CS, Kang SK, Seo HS, DMPK and early tox study of a novel HDAC inhibitor, CG200745. AACR Meeting Abstracts 2008 2008;2008:2617
   Google Scholar
• Liu L, Chen B, Qin S, A novel histone deacetylase inhibitor Chidamide induces apoptosis of human colon cancer cells. Biochem Biophys Res Commun 2010;392(2):190-5
   PubMed Web of Science ®Google Scholar
• Dong M, Ning Z, Newman MJ, Phase I study of chidamide (CS055/HBI-8000), a novel histone deacetylase inhibitor, in patients with advanced solid tumors and lymphomas [abstract 3529]. J Clin Oncol 2009;27:15s
   Web of Science ®Google Scholar
• Prince HM, Bishton MJ, Johnstone RW. Panobinostat (LBH589): a potent pan-deacetylase inhibitor with promising activity against hematologic and solid tumors. Future Oncol 2009;5(5):601-12
   PubMed Web of Science ®Google Scholar
• Atadja P. Development of the pan-DAC inhibitor panobinostat (LBH589): successes and challenges. Cancer Lett 2009;280(2):233-41
   PubMed Web of Science ®Google Scholar
• Marks PA, Breslow R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat Biotechnol 2007;25(1):84-90
   PubMed Web of Science ®Google Scholar
• Lahm A, Paolini C, Pallaoro M, Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases. Proc Natl Acad Sci USA 2007;104(44):17335-40
   PubMed Web of Science ®Google Scholar
• Finnin MS, Donigian JR, Cohen A, Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 1999;401(6749):188-93
   PubMed Web of Science ®Google Scholar
• Cronin CN, Hilgers M, Knuth ME, Crystallization of histone deacetylase 2. US7507552; 2009
   Google Scholar
• Bottomley MJ, Lo Surdo P, Di Giovine P, Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain. J Biol Chem 2008;283(39):26694-704
   PubMed Web of Science ®Google Scholar
• Schuetz A, Min J, Allali-Hassani A, Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity. J Biol Chem 2008;283(17):11355-63
   PubMed Web of Science ®Google Scholar
• Somoza JR, Skene RJ, Katz BA, Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 2004;12(7):1325-34
   PubMed Web of Science ®Google Scholar
• Vannini A, Volpari C, Filocamo G, Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc Natl Acad Sci USA 2004;101(42):15064-9
   PubMed Web of Science ®Google Scholar
• Balasubramanian S, Steggerda S, Sirisawad M, The Histone Deacetylase-8 (HDAC8) Selective Inhibitor PCI-34051 Decreases Interleukin-1 Beta Secretion in vitro and Reduces Inflammation in vivo 50th ASH Annual Meeting and Exposition; 2009; San Francisco: American Society of Hematology; 2009; abstract 2581
   Google Scholar
• Moradei O, Paquin I, Leit S, Inhibitors of histone deacetylase. WO2005030704; 2005
   Google Scholar
• Wilson KJ, Witter DJ, Grimm JB, Phenylglycine and phenylalanine derivatives as potent and selective HDAC1 inhibitors (SHI-1). Bioorg Med Chem Lett 2008;18(6):1859-63
   PubMed Web of Science ®Google Scholar
• Witter DJ, Harrington P, Wilson KJ, Optimization of biaryl Selective HDAC1&2 Inhibitors (SHI-1:2). Bioorg Med Chem Lett 2008;18(2):726-31
   PubMed Web of Science ®Google Scholar
• Methot JL, Chakravarty PK, Chenard M, Exploration of the internal cavity of histone deacetylase (HDAC) with selective HDAC1/HDAC2 inhibitors (SHI-1:2). Bioorg Med Chem Lett 2008;18(3):973-8
   PubMed Web of Science ®Google Scholar
• Bressi JC, Jennings AJ, Skene R, Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides. Bioorg Med Chem Lett 2010;20(10):3142-5
   PubMed Web of Science ®Google Scholar
• Tessier P, Smil DV, Wahhab A, Diphenylmethylene hydroxamic acids as selective class IIa histone deacetylase inhibitors. Bioorg Med Chem Lett 2009;19(19):5684-8
   PubMed Web of Science ®Google Scholar
• Itoh Y, Suzuki T, Miyata N. Isoform-selective histone deacetylase inhibitors. Curr Pharm Des 2008;14(6):529-44
   PubMed Web of Science ®Google Scholar
• Butler KV, Kozikowski AP. Chemical origins of isoform selectivity in histone deacetylase inhibitors. Curr Pharm Des 2008;14(6):505-28
   PubMed Web of Science ®Google Scholar
• Salisbury CM, Cravatt BF. Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc Natl Acad Sci USA 2007;104(4):1171-6
   PubMed Web of Science ®Google Scholar
• Bantscheff M, Eberhard D, Abraham Y, Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat Biotechnol 2007;25(9):1035-44
   PubMed Web of Science ®Google Scholar
• Filippakopoulos P, Qi J, Picaud S, Selective inhibition of BET bromodomains. Nature 2010;468(7327):1067-73
   PubMed Web of Science ®Google Scholar
• Zhang B, Strauss AC, Chu S, Effective targeting of quiescent chronic myelogenous leukemia stem cells by histone deacetylase inhibitors in combination with imatinib mesylate. Cancer Cell 2010;17(5):427-42
   PubMed Web of Science ®Google Scholar
• Yu Y, Zeng P, Xiong J, Epigenetic drugs can stimulate metastasis through enhanced expression of the pro-metastatic Ezrin gene. PLoS One 2010;5(9):e12710
   PubMed Web of Science ®Google Scholar
• Wang Y, Zhang H, Chen Y, LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell 2009;138(4):660-72
   PubMed Web of Science ®Google Scholar
• Bandyopadhyay D, Mishra A, Medrano EE. Overexpression of histone deacetylase 1 confers resistance to sodium butyrate-mediated apoptosis in melanoma cells through a p53-mediated pathway. Cancer Res 2004;64(21):7706-10
   PubMed Web of Science ®Google Scholar
• Fantin VR, Loboda A, Paweletz CP, Constitutive activation of signal transducers and activators of transcription predicts vorinostat resistance in cutaneous T-cell lymphoma. Cancer Res 2008;68(10):3785-94
   PubMed Web of Science ®Google Scholar
• Stimson L, La Thangue NB. Biomarkers for predicting clinical responses to HDAC inhibitors. Cancer Lett 2009;280(2):177-83
   PubMed Web of Science ®Google Scholar
• Scott GK, Marx C, Berger CE, Destabilization of ERBB2 transcripts by targeting 3′ untranslated region messenger RNA associated HuR and histone deacetylase-6. Mol Cancer Res 2008;6(7):1250-8
   PubMed Web of Science ®Google Scholar