Journal Menu
- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Annual Issues
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 197946, 14 pages
doi:10.1155/2011/197946
Review Article
Histone Deacetylase Inhibitors: The Epigenetic Therapeutics That Repress Hypoxia-Inducible Factors
Department of Biology and Graduate Program of Biological Sciences, College of Arts & Sciences, Drexel University, 3141 Chestnut Street, Stratton Hall 318, Philadelphia, PA 19104, USA
Received 20 July 2010; Accepted 25 September 2010
Academic Editor: Minoru Yoshida
Copyright © 2011 Shuyang Chen and Nianli Sang. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- D. L. Schwartz, J. A. Bankson, R. Lemos Jr. et al., “Radiosensitization and stromal imaging response correlates for the HIF-1 inhibitor PX-478 given with or without chemotherapy in pancreatic cancer,” Molecular Cancer Therapeutics, vol. 9, no. 7, pp. 2057–2067, 2010. View at Publisher · View at Google Scholar · View at PubMed
- G. L. Semenza, “Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics,” Oncogene, vol. 29, no. 5, pp. 625–634, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. Daponte, M. Ioannou, I. Mylonis et al., “Prognostic significance of hypoxia-inducible factor 1 alpha(HIF-1alpha) expression in serous ovarian cancer: an immunohistochemical study,” BMC Cancer, vol. 8, article no. 335, 2008. View at Publisher · View at Google Scholar · View at PubMed
- C. Gómez-Raposo, M. Mendiola, J. Barriuso, E. Casado, D. Hardisson, and A. Redondo, “Angiogenesis and ovarian cancer,” Clinical & Translational Oncology, vol. 11, no. 9, pp. 564–571, 2009.
- H. Jiang and Y. Feng, “Hypoxia-inducible factor 1α (HIF-1α) correlated with tumor growth and apoptosis in ovarian cancer,” International Journal of Gynecological Cancer, vol. 16, supplement 1, pp. 405–412, 2006. View at Publisher · View at Google Scholar · View at PubMed
- J. M. Brown and W. R. Wilson, “Exploiting tumour hypoxia in cancer treatment,” Nature Reviews Cancer, vol. 4, no. 6, pp. 437–447, 2004. View at Scopus
- A. Giaccia, B. G. Siim, and R. S. Johnson, “HIF-1 as a target for drug development,” Nature Reviews Drug Discovery, vol. 2, no. 10, pp. 803–811, 2003. View at Scopus
- G. Powis and L. Kirkpatrick, “Hypoxia inducible factor-1α as a cancer drug target,” Molecular Cancer Therapeutics, vol. 3, no. 5, pp. 647–654, 2004. View at Scopus
- G. L. Semenza, “Targeting HIF-1 for cancer therapy,” Nature Reviews Cancer, vol. 3, no. 10, pp. 721–732, 2003. View at Scopus
- S. J. Welsh and G. Powis, “Hypoxia inducible factor as a cancer drug target,” Current Cancer Drug Targets, vol. 3, no. 6, pp. 391–405, 2003. View at Publisher · View at Google Scholar · View at Scopus
- D. Kong, E. J. Park, A. G. Stephen et al., “Echinomycin, a small-molecule inhibitor of hypoxia-inducible factor-1 DNA-binding activity,” Cancer Research, vol. 65, no. 19, pp. 9047–9055, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Tan, R. G. De Noronha, A. J. Roecker et al., “Identification of a novel small-molecule inhibitor of the hypoxia-inducible factor 1 pathway,” Cancer Research, vol. 65, no. 2, pp. 605–612, 2005. View at Scopus
- S. Welsh, R. Williams, L. Kirkpatrick, G. Paine-Murrieta, and G. Powis, “Antitumor activity and pharmacodynamic properties of PX-478, an inhibitor of hypoxia-inducible factor-1α,” Molecular Cancer Therapeutics, vol. 3, no. 3, pp. 233–244, 2004. View at Scopus
- D. C. Drummond, C. O. Noble, D. B. Kirpotin, Z. Guo, G. K. Scott, and C. C. Benz, “Clinical development of histone deacetylase inhibitors as anticancer agents,” Annual Review of Pharmacology and Toxicology, vol. 45, pp. 495–528, 2005. View at Publisher · View at Google Scholar · View at PubMed
- R. W. Johnstone and J. D. Licht, “Histone deacetylase inhibitors in cancer therapy: is transcription the primary target?” Cancer Cell, vol. 4, no. 1, pp. 13–18, 2003. View at Publisher · View at Google Scholar · View at Scopus
- P. A. Marks, V. M. Richon, R. Breslow, and R. A. Rifkind, “Histone deacetylase inhibitors as new cancer drugs,” Current Opinion in Oncology, vol. 13, no. 6, pp. 477–483, 2001. View at Publisher · View at Google Scholar · View at Scopus
- D. M. Fath, X. Kong, D. Liang et al., “Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-α,” Journal of Biological Chemistry, vol. 281, no. 19, pp. 13612–13619, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X. Kong, Z. Lin, D. Liang, D. Fath, N. Sang, and J. Caro, “Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1α,” Molecular and Cellular Biology, vol. 26, no. 6, pp. 2019–2028, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. Ahringer, “NuRD and SIN3: histone deacetylase complexes in development,” Trends in Genetics, vol. 16, no. 8, pp. 351–356, 2000. View at Publisher · View at Google Scholar · View at Scopus
- X.-J. Yang and S. Grégoire, “Class II histone deacetylases: from sequence to function, regulation, and clinical implication,” Molecular and Cellular Biology, vol. 25, no. 8, pp. 2873–2884, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- X.-J. Yang and E. Seto, “Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression,” Current Opinion in Genetics and Development, vol. 13, no. 2, pp. 143–153, 2003. View at Publisher · View at Google Scholar · View at Scopus
- C. Choudhary, C. Kumar, F. Gnad et al., “Lysine acetylation targets protein complexes and co-regulates major cellular functions,” Science, vol. 325, no. 5942, pp. 834–840, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. Bali, M. Pranpat, J. Bradner et al., “Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors,” Journal of Biological Chemistry, vol. 280, no. 29, pp. 26729–26734, 2005. View at Publisher · View at Google Scholar · View at PubMed
- P. A. Marks and M. Dokmanovic, “Histone deacetylase inhibitors: discovery and development as anticancer agents,” Expert Opinion on Investigational Drugs, vol. 14, no. 12, pp. 1497–1511, 2005. View at Publisher · View at Google Scholar · View at PubMed
- G. Blander and L. Guarente, “The Sir2 family of protein deacetylases,” Annual Review of Biochemistry, vol. 73, pp. 417–435, 2004. View at Publisher · View at Google Scholar · View at PubMed
- M. Goodson, B. A. Jonas, and M. A. Privalsky, “Corepressors: custom tailoring and alterations while you wait,” Nuclear Receptor Signal, vol. 3, article no. e003, 2005.
- M. G. Rosenfeld, V. V. Lunyak, and C. K. Glass, “Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response,” Genes and Development, vol. 20, no. 11, pp. 1405–1428, 2006. View at Publisher · View at Google Scholar · View at PubMed
- J. Joseph, G. Mudduluru, S. Antony, S. Vashistha, P. Ajitkumar, and K. Somasundaram, “Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB,” Oncogene, vol. 23, no. 37, pp. 6304–6315, 2004. View at Publisher · View at Google Scholar · View at PubMed
- A. Rascle, J. A. Johnston, and B. Amati, “Deacetylase activity is required for recruitment of the basal transcription machinery and transactivation by STAT5,” Molecular and Cellular Biology, vol. 23, no. 12, pp. 4162–4173, 2003. View at Publisher · View at Google Scholar
- T. Ikenoue, K. Inoki, B. Zhao, and K.-L. Guan, “PTEN acetylation modulates its interaction with PDZ domain,” Cancer Research, vol. 68, no. 17, pp. 6908–6912, 2008. View at Publisher · View at Google Scholar · View at PubMed
- P.-O. Hasselgren, “Ubiquitination, phosphorylation, and acetylation—triple threat in muscle wasting,” Journal of Cellular Physiology, vol. 213, no. 3, pp. 679–689, 2007. View at Publisher · View at Google Scholar · View at PubMed
- B. Chen and C. L. Cepko, “HDAC4 regulates neuronal survival in normal and diseased retinas,” Science, vol. 323, no. 5911, pp. 256–259, 2009. View at Publisher · View at Google Scholar · View at PubMed
- E. A. Miska, E. Langley, D. Wolf, C. Karlsson, J. Pines, and T. Kouzarides, “Differential localization of HDAC4 orchestrates muscle differentiation,” Nucleic Acids Research, vol. 29, no. 16, pp. 3439–3447, 2001.
- R. B. Vega, K. Matsuda, J. Oh et al., “Histone deacetylase 4 controls chondrocyte hypertrophy during skeletogenesis,” Cell, vol. 119, no. 4, pp. 555–566, 2004. View at Publisher · View at Google Scholar · View at PubMed
- A. H. Wang, N. R. Bertos, M. Vezmar et al., “HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor,” Molecular and Cellular Biology, vol. 19, no. 11, pp. 7816–7827, 1999.
- E. Y. Huang, J. Zhang, E. A. Miska, M. G. Guenther, T. Kouzarides, and M. A. Lazar, “Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway,” Genes and Development, vol. 14, no. 1, pp. 45–54, 2000.
- R. B. Vega, B. C. Harrison, E. Meadows et al., “Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5,” Molecular and Cellular Biology, vol. 24, no. 19, pp. 8374–8385, 2004. View at Publisher · View at Google Scholar · View at PubMed
- C. Lemercier, A. Verdel, B. Galloo, S. Curtet, M.-P. Brocard, and S. Khochbin, “mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity,” Journal of Biological Chemistry, vol. 275, no. 20, pp. 15594–15599, 2000. View at Publisher · View at Google Scholar · View at PubMed
- J. J. Kovacs, P. J. M. Murphy, S. Gaillard et al., “HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor,” Molecular Cell, vol. 18, no. 5, pp. 601–607, 2005. View at Publisher · View at Google Scholar · View at PubMed
- S. J. Haggarty, K. M. Koeller, J. C. Wong, C. M. Grozinger, and S. L. Schreiber, “Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 8, pp. 4389–4394, 2003. View at Publisher · View at Google Scholar · View at PubMed
- C. Hubbert, A. Guardiola, R. Shao et al., “HDAC6 is a microtubule-associated deacetylase,” Nature, vol. 417, no. 6887, pp. 455–458, 2002. View at Publisher · View at Google Scholar · View at PubMed
- A. Matsuyama, T. Shimazu, Y. Sumida et al., “In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation,” EMBO Journal, vol. 21, no. 24, pp. 6820–6831, 2002. View at Publisher · View at Google Scholar
- Y. Zhang, N. Li, C. Caron et al., “HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo,” EMBO Journal, vol. 22, no. 5, pp. 1168–1179, 2003. View at Publisher · View at Google Scholar · View at PubMed
- A. Rodriguez-Gonzalez, T. Lin, A. K. Ikeda, T. Simms-Waldrip, C. Fu, and K. M. Sakamoto, “Role of the aggresome pathway in cancer: targeting histone deacetylase 6-dependent protein degradation,” Cancer Research, vol. 68, no. 8, pp. 2557–2560, 2008. View at Publisher · View at Google Scholar · View at PubMed
- Y. Nakamura, M. Ogura, D. Tanaka, and N. Inagaki, “Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5,” Biochemical and Biophysical Research Communications, vol. 366, no. 1, pp. 174–179, 2008. View at Publisher · View at Google Scholar · View at PubMed
- G.-G. Liou, J. C. Tanny, R. G. Kruger, T. Walz, and D. Moazed, “Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation,” Cell, vol. 121, no. 4, pp. 515–527, 2005. View at Publisher · View at Google Scholar · View at PubMed
- T. Inoue, M. Hiratsuka, M. Osaki, and M. Oshimura, “The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation,” Cell Cycle, vol. 6, no. 9, pp. 1011–1018, 2007.
- B. J. North, B. L. Marshall, M. T. Borra, J. M. Denu, and E. Verdin, “The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase,” Molecular Cell, vol. 11, no. 2, pp. 437–444, 2003. View at Publisher · View at Google Scholar
- A. Vaquero, R. Sternglanz, and D. Reinberg, “NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs,” Oncogene, vol. 26, no. 37, pp. 5505–5520, 2007. View at Publisher · View at Google Scholar · View at PubMed
- S. Kume, T. Uzu, K. Horiike et al., “Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney,” Journal of Clinical Investigation, vol. 120, no. 4, pp. 1043–1055, 2010. View at Publisher · View at Google Scholar · View at PubMed
- T. Araki, Y. Sasaki, and J. Milbrandt, “Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration,” Science, vol. 305, no. 5686, pp. 1010–1013, 2004. View at Publisher · View at Google Scholar · View at PubMed
- M. Fainzilber and J. L. Twiss, “Tracking in the wlds—the hunting of the SIRT and the luring of the draper,” Neuron, vol. 50, no. 6, pp. 819–821, 2006. View at Publisher · View at Google Scholar · View at PubMed
- A. Villagra, F. Cheng, H-W. Wang, et al., “The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance,” Nature Immunology, vol. 10, pp. 92–100, 2008.
- X.-J. Yang and E. Seto, “HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention,” Oncogene, vol. 26, no. 37, pp. 5310–5318, 2007. View at Publisher · View at Google Scholar · View at PubMed
- Y.-Y. Lin, J.-Y. Lu, J. Zhang et al., “Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis,” Cell, vol. 136, no. 6, pp. 1073–1084, 2009. View at Publisher · View at Google Scholar · View at PubMed
- S. C. Kim, R. Sprung, Y. Chen et al., “Substrate and functional diversity of lysine acetylation revealed by a proteomics survey,” Molecular Cell, vol. 23, no. 4, pp. 607–618, 2006. View at Publisher · View at Google Scholar · View at PubMed
- I. V. Gregoretti, Y.-M. Lee, and H. V. Goodson, “Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis,” Journal of Molecular Biology, vol. 338, no. 1, pp. 17–31, 2004. View at Publisher · View at Google Scholar · View at PubMed
- A. J. M. De Ruijter, A. H. Van Gennip, H. N. Caron, S. Kemp, and A. B. P. Van Kuilenburg, “Histone deacetylases (HDACs): characterization of the classical HDAC family,” Biochemical Journal, vol. 370, no. 3, pp. 737–749, 2003. View at Publisher · View at Google Scholar · View at PubMed
- A. R. Guardiola and T.-P. Yao, “Molecular cloning and characterization of a novel histone deacetylase HDAC10,” Journal of Biological Chemistry, vol. 277, no. 5, pp. 3350–3356, 2002. View at Publisher · View at Google Scholar · View at PubMed
- H.-Y. Kao, C.-H. Lee, A. Komarov, C. C. Han, and R. M. Evans, “Isolation and characterization of mammalian HDAC10, a novel histone deacetylase,” Journal of Biological Chemistry, vol. 277, no. 1, pp. 187–193, 2002. View at Publisher · View at Google Scholar · View at PubMed
- L. Gao, M. A. Cueto, F. Asselbergs, and P. Atadja, “Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family,” Journal of Biological Chemistry, vol. 277, no. 28, pp. 25748–25755, 2002. View at Publisher · View at Google Scholar · View at PubMed
- J. E. Bolden, M. J. Peart, and R. W. Johnstone, “Anticancer activities of histone deacetylase inhibitors,” Nature Reviews Drug Discovery, vol. 5, no. 9, pp. 769–784, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- P. A. Marks and R. Breslow, “Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug,” Nature Biotechnology, vol. 25, no. 1, pp. 84–90, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. J. Greshock, D. M. Johns, Y. Noguchi, and R. M. Williams, “Improved total synthesis of the potent HDAC inhibitor FK228 (FR-901228),” Organic Letters, vol. 10, no. 4, pp. 613–616, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. F. Taghiyev, N. V. Guseva, M. T. Sturm, O. W. Rokhlin, and M. B. Cohen, “Trichostatin a (TSA) sensitizes the human prostatic cancer cell line DU145 to death receptor ligands treatment,” Cancer Biology and Therapy, vol. 4, no. 4, pp. 382–390, 2005. View at Scopus
- D. M. Vigushin, S. Ali, P. E. Pace et al., “Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo,” Clinical Cancer Research, vol. 7, no. 4, pp. 971–976, 2001. View at Scopus
- D. M. Lucas, L. Alinari, D. A. West et al., “The novel deacetylase inhibitor AR-42 demonstrates pre-clinical activity in B-cell malignancies in vitro and in vivo,” PLoS One, vol. 5, no. 6, article no. e10941, 2010. View at Publisher · View at Google Scholar · View at PubMed
- C.-J. Lai, R. Bao, X. Tao et al., “CUDC-101, a multitargeted inhibitor of histone deacetylase, epidermal growth factor receptor, and human epidermal growth factor receptor 2, exerts potent anticancer activity,” Cancer Research, vol. 70, no. 9, pp. 3647–3656, 2010. View at Publisher · View at Google Scholar · View at PubMed
- G. L. Semenza, “Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1,” Annual Review of Cell and Developmental Biology, vol. 15, pp. 551–578, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- G. L. Semenza, “Expression of hypoxia-inducible factor 1: mechanisms and consequences,” Biochemical Pharmacology, vol. 59, no. 1, pp. 47–53, 2000. View at Publisher · View at Google Scholar · View at Scopus
- C.-J. Hu, A. Sataur, L. Wang, H. Chen, and M. C. Simon, “The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1α and HIF-2α,” Molecular Biology of the Cell, vol. 18, no. 11, pp. 4528–4542, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C.-J. Hu, L.-Y. Wang, L. A. Chodosh, B. Keith, and M. C. Simon, “Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation,” Molecular and Cellular Biology, vol. 23, no. 24, pp. 9361–9374, 2003. View at Publisher · View at Google Scholar · View at Scopus
- V. A. Carroll and M. Ashcroft, “Role of hypoxia-inducible factor (HIF)-1α versus HIF-2α in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: implications for targeting the HIF pathway,” Cancer Research, vol. 66, no. 12, pp. 6264–6270, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. G. Kaelin Jr., “The von Hippel-Lindau tumor suppressor protein and clear cell renal carcinoma,” Clinical Cancer Research, vol. 13, no. 2, pp. 680s–684s, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Liao and R. S. Johnson, “Hypoxia: a key regulator of angiogenesis in cancer,” Cancer and Metastasis Reviews, vol. 26, no. 2, pp. 281–290, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Bos, P. J. Van Diest, J. S. De Jong, P. Van Der Groep, P. Van Der Valk, and E. Van Der Wall, “Hypoxia-inducible factor-1α is associated with angiogenesis, and expression of bFGF, PDGF-BB, and EGFR in invasive breast cancer,” Histopathology, vol. 46, no. 1, pp. 31–36, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Calvani, A. Rapisarda, B. Uranchimeg, R. H. Shoemaker, and G. Melillo, “Hypoxic induction of an HIF-1α-dependent bFGF autocrine loop drives angiogenesis in human endothelial cells,” Blood, vol. 107, no. 7, pp. 2705–2712, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. G. Kaelin Jr., “The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing,” Biochemical and Biophysical Research Communications, vol. 338, no. 1, pp. 627–628, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- D. Lando, J. J. Gorman, M. L. Whitelaw, and D. J. Peet, “Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation,” European Journal of Biochemistry, vol. 270, no. 5, pp. 781–790, 2003. View at Publisher · View at Google Scholar · View at Scopus
- G. L. Semenza, “Hydroxylation of HIF-1: oxygen sensing at the molecular level,” Physiology, vol. 19, no. 4, pp. 176–182, 2004. View at Scopus
- L. E. Huang, J. Gu, M. Schau, and H. F. Bunn, “Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 14, pp. 7987–7992, 1998. View at Scopus
- S. Salceda and J. Caro, “Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes,” Journal of Biological Chemistry, vol. 272, no. 36, pp. 22642–22647, 1997. View at Publisher · View at Google Scholar
- Z. Arany, L. E. Huang, R. Eckner et al., “An essential role for p300/CBP in the cellular response to hypoxia,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 23, pp. 12969–12973, 1996. View at Publisher · View at Google Scholar · View at Scopus
- P. Carrero, K. Okamoto, P. Coumailleau, S. A. O'Brien, H. Tanaka, and L. Poellinger, “Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia, inducible factor 1α,” Molecular and Cellular Biology, vol. 20, no. 1, pp. 402–415, 2000. View at Scopus
- D. Lando, D. J. Peet, D. A. Whelan, J. J. Gorman, and M. L. Whitelaw, “Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch,” Science, vol. 295, no. 5556, pp. 858–861, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Sang, J. Fang, V. Srinivas, I. Leshchinsky, and J. Caro, “Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1α is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP,” Molecular and Cellular Biology, vol. 22, no. 9, pp. 2984–2992, 2002. View at Publisher · View at Google Scholar · View at Scopus
- R. Paddenberg, A. Goldenberg, P. Faulhammer, R. C. Braun-Dullaeus, and W. Kummer, “Mitochondrial complex II is essential for hypoxia-induced ROS generation and vasoconstriction in the pulmonary vasculature,” Advances in Experimental Medicine and Biology, vol. 536, pp. 163–169, 2002. View at Scopus
- R. D. Guzy, B. Hoyos, E. Robin et al., “Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing,” Cell Metabolism, vol. 1, no. 6, pp. 401–408, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. Meng, S. Chen, T. Lao, D. Liang, and N. Sang, “Nitrogen anabolism underlies the importance of glutaminolysis in proliferating cells,” Cell Cycle, vol. 9, no. 19, pp. 3921–3932, 2010.
- G. L. Semenza, “Intratumoral hypoxia, radiation resistance, and HIF-1,” Cancer Cell, vol. 5, no. 5, pp. 405–406, 2004. View at Publisher · View at Google Scholar · View at Scopus
- G. L. Semenza, “Development of novel therapeutic strategies that target HIF-1,” Expert Opinion on Therapeutic Targets, vol. 10, no. 2, pp. 267–280, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Zhong, K. Chiles, D. Feldser et al., “Modulation of hypoxia-inducible factor 1α expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics,” Cancer Research, vol. 60, no. 6, pp. 1541–1545, 2000. View at Scopus
- P. Vaupel, M. Höckel, and A. Mayer, “Detection and characterization of tumor hypoxia using pO2 histography,” Antioxidants and Redox Signaling, vol. 9, no. 8, pp. 1221–1235, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. E. Ryan, J. Lo, and R. S. Johnson, “HIF-1α is required for solid tumor formation and embryonic vascularization,” EMBO Journal, vol. 17, no. 11, pp. 3005–3015, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. E. Ryan, M. Poloni, W. McNulty et al., “Hypoxia-inducible factor-1α is a positive factor in solid tumor growth,” Cancer Research, vol. 60, no. 15, pp. 4010–4015, 2000. View at Scopus
- K. Hirota and G. L. Semenza, “Regulation of angiogenesis by hypoxia-inducible factor 1,” Critical Reviews in Oncology/Hematology, vol. 59, no. 1, pp. 15–26, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Bouzin and O. Feron, “Targeting tumor stroma and exploiting mature tumor vasculature to improve anti-cancer drug delivery,” Drug Resistance Updates, vol. 10, no. 3, pp. 109–120, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- A. H. Licht, F. Müller-Holtkamp, I. Flamme, and G. Breier, “Inhibition of hypoxia-inducible factor activity in endothelial cells disrupts embryonic cardiovascular development,” Blood, vol. 107, no. 2, pp. 584–590, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. Löfstedt, E. Fredlund, L. Holmquist-Mengelbier et al., “Hypoxia inducible factor-2α in cancer,” Cell Cycle, vol. 6, no. 8, pp. 919–926, 2007. View at Scopus
- W. G. An, M. Kanekal, M. C. Simon, E. Maltepe, M. V. Blagosklonny, and L. M. Neckers, “Stabilization of wild-type p53 by hypoxia-inducible factor 1alpha,” Nature, vol. 392, no. 6674, pp. 405–408, 1998. View at Scopus
- M. V. Blagosklonny, W. G. An, L. Y. Romanova, J. Trepel, T. Fojo, and L. Neckers, “p53 inhibits hypoxia-inducible factor-stimulated transcription,” Journal of Biological Chemistry, vol. 273, no. 20, pp. 11995–11998, 1998. View at Publisher · View at Google Scholar · View at Scopus
- J. S. Isaacs, Y. J. Jung, D. R. Mole et al., “HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: novel role of fumarate in regulation of HIF stability,” Cancer Cell, vol. 8, no. 2, pp. 143–153, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Ravi, B. Mookerjee, Z. M. Bhujwalla et al., “Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1α,” Genes and Development, vol. 14, no. 1, pp. 34–44, 2000. View at Scopus
- N. Sang, D. P. Stiehl, J. Bohensky, I. Leshchinsky, V. Srinivas, and J. Caro, “MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300,” Journal of Biological Chemistry, vol. 278, no. 16, pp. 14013–14019, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. A. Selak, S. M. Armour, E. D. MacKenzie et al., “Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase,” Cancer Cell, vol. 7, no. 1, pp. 77–85, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Zundel, C. Schindler, D. Haas-Kogan et al., “Loss of PTEN facilitates HIF-1-mediated gene expression,” Genes and Development, vol. 14, no. 4, pp. 391–396, 2000. View at Scopus
- L. Neckers and K. Neckers, “Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics—an update,” Expert Opinion on Emerging Drugs, vol. 10, no. 1, pp. 137–149, 2005. View at Publisher · View at Google Scholar · View at Scopus
- Y. Miyata, “Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents,” Current Pharmaceutical Design, vol. 11, no. 9, pp. 1131–1138, 2005. View at Publisher · View at Google Scholar · View at Scopus
- M. Bazzaro, M. K. Lee, A. Zoso et al., “Ubiquitin-proteasome system stress sensitizes ovarian cancer to proteasome inhibitor-induced apoptosis,” Cancer Research, vol. 66, no. 7, pp. 3754–3763, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. Ishii, S. Waxman, and D. Germain, “Targeting the ubiquitin-proteasome pathway in cancer therapy,” Anti-Cancer Agents in Medicinal Chemistry, vol. 7, no. 3, pp. 359–365, 2007. View at Publisher · View at Google Scholar · View at Scopus
- C. A. P. Joazeiro, K. C. Anderson, and T. Hunter, “Proteasome inhibitor drugs on the rise,” Cancer Research, vol. 66, no. 16, pp. 7840–7842, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. B. Sunwoo, Z. Chen, G. Dong et al., “Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-κB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma,” Clinical Cancer Research, vol. 7, no. 5, pp. 1419–1428, 2001. View at Scopus
- D. Escuin, E. R. Kline, and P. Giannakakou, “Both microtubule-stabilizing and microtubule-destabilizing drugs inhibit hypoxia-inducible factor-1α accumulation and activity by disrupting microtubule function,” Cancer Research, vol. 65, no. 19, pp. 9021–9028, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. J. Mabjeesh, D. Escuin, T. M. LaVallee et al., “2ME2 inhibits tumor growth and angiogenesis by disrupting microtubules and dysregulating HIF,” Cancer Cell, vol. 3, no. 4, pp. 363–375, 2003. View at Publisher · View at Google Scholar · View at Scopus
- E. W. Newcomb, Y. Lukyanov, T. Schnee, M. A. Ali, L. Lan, and D. Zagzag, “Noscapine inhibits hypoxia-mediated HIF-1alpha expression andangiogenesis in vitro: a novel function for an old drug,” International Journal of Oncology, vol. 28, no. 5, pp. 1121–1130, 2006. View at Scopus
- D. Z. Qian, S. K. Kachhap, S. J. Collis et al., “Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1α,” Cancer Research, vol. 66, no. 17, pp. 8814–8821, 2006. View at Publisher · View at Google Scholar · View at PubMed
- H. Kato, S. Tamamizu-Kato, and F. Shibasaki, “Histone deacetylase 7 associates with hypoxia-inducible factor 1α and increases transcriptional activity,” Journal of Biological Chemistry, vol. 279, no. 40, pp. 41966–41974, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. S. Kim, H. J. Kwon, Y. M. Lee et al., “Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes,” Nature Medicine, vol. 7, no. 4, pp. 437–443, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. Maltepe, G. W. Krampitz, K. M. Okazaki et al., “Hypoxia-inducible factor-dependent histone deacetylase activity determines stem cell fate in the placenta,” Development, vol. 132, no. 15, pp. 3393–3403, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- Y. M. Lee, S.-H. Kim, H.-S. Kim et al., “Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1α activity,” Biochemical and Biophysical Research Communications, vol. 300, no. 1, pp. 241–246, 2003. View at Publisher · View at Google Scholar · View at Scopus
- Y. Sasakawa, Y. Naoe, T. Noto et al., “Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors,” Biochemical Pharmacology, vol. 66, no. 6, pp. 897–906, 2003. View at Publisher · View at Google Scholar · View at Scopus
- D. Zgouras, A. Wächtershäuser, D. Frings, and J. Stein, “Butyrate impairs intestinal tumor cell-induced angiogenesis by inhibiting HIF- 1α nuclear translocation,” Biochemical and Biophysical Research Communications, vol. 300, no. 4, pp. 832–838, 2003. View at Publisher · View at Google Scholar · View at Scopus
- T. Inoue, M. Hiratsuka, M. Osaki, and M. Oshimura, “The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation,” Cell Cycle, vol. 6, no. 9, pp. 1011–1018, 2007. View at Scopus
- J.-W. Jeong, M.-K. Bae, M.-Y. Ahn et al., “Regulation and destabilization of HIF-1α by ARD1-mediated acetylation,” Cell, vol. 111, no. 5, pp. 709–720, 2002. View at Publisher · View at Google Scholar · View at Scopus
- Y. Li, Z. Yuan, B. Liu et al., “Prevention of hypoxia-induced neuronal apoptosis through histone deacetylase inhibition,” Journal of Trauma, vol. 64, no. 4, pp. 863–870, 2008. View at Publisher · View at Google Scholar · View at PubMed
- H. Manabe, Y. Nasu, T. Komiyama et al., “Inhibition of histone deacetylase down-regulates the expression of hypoxia-induced vascular endothelial growth factor by rheumatoid synovial fibroblasts,” Inflammation Research, vol. 57, no. 1, pp. 4–10, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. H. Kim, K. W. Kim, and J. W. Jeong, “Inhibition of hypoxia-induced angiogenesis by sodium butyrate, a histone deacetylase inhibitor, through hypoxia-inducible factor-1alpha suppression,” Oncology Report, vol. 17, no. 4, pp. 793–797, 2007.
- Z. N. Demidenko, A. M. Rapisarda, M. Garayoa, P. Giannakakou, G. Melillo, and M. V. Blagosklonny, “Accumulation of hypoxia-inducible factor-1α is limited by transcription-dependent depletion,” Oncogene, vol. 24, no. 30, pp. 4829–4838, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. H. Kasper, F. Boussouar, K. Boyd et al., “Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression,” EMBO Journal, vol. 24, no. 22, pp. 3846–3858, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- L. H. Kasper and P. K. Brindle, “Mammalian gene expression program resiliency: the roles of multiple coactivator mechanisms in hypoxia-responsive transcription,” Cell Cycle, vol. 5, no. 2, pp. 142–146, 2006. View at Scopus
- D. P. Stiehl, D. M. Fath, D. Liang, Y. Jiang, and N. Sang, “Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation,” Cancer Research, vol. 67, no. 5, pp. 2256–2264, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- M. L. Hansson, A. E. Popko-Ścibor, M. Saint Just Ribeiro et al., “The transcriptional coactivator MAML1 regulates p300 autoacetylation and HAT activity,” Nucleic Acids Research, vol. 37, no. 9, pp. 2996–3006, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. C. Black, A. Mosley, T. Kitada, M. Washburn, and M. Carey, “The SIRT2 deacetylase regulates autoacetylation of p300,” Molecular Cell, vol. 32, no. 3, pp. 449–455, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Simone, P. Stiegler, S.-V. Forcales et al., “Deacetylase recruitment by the C/H3 domain of the acetyltransferase p300,” Oncogene, vol. 23, no. 12, pp. 2177–2187, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- H. Xiao, T. Hasegawa, and K.-I. Isobe, “p300 Collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor,” Journal of Biological Chemistry, vol. 275, no. 2, pp. 1371–1376, 2000. View at Publisher · View at Google Scholar · View at Scopus
- J. L. Ruas, U. Berchner-Pfannschmidt, S. Malik et al., “Complex regulation of the transactivation function of hypoxia-inducible factor-1αby direct interaction with two distinct domains of the creb-binding protein/p300,” Journal of Biological Chemistry, vol. 285, no. 4, pp. 2601–2609, 2010. View at Publisher · View at Google Scholar · View at PubMed
- D. Liang, X. Kong, and N. Sang, “Effects of histone deacetylase inhibitors on HIF-1,” Cell Cycle, vol. 5, no. 21, pp. 2430–2435, 2006. View at Scopus
- K. Sadoul, C. Boyault, M. Pabion, and S. Khochbin, “Regulation of protein turnover by acetyltransferases and deacetylases,” Biochimie, vol. 90, no. 2, pp. 306–312, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Caron, C. Boyault, and S. Khochbin, “Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability,” BioEssays, vol. 27, no. 4, pp. 408–415, 2005.
- T. Arnesen, X. Kong, R. Evjenth et al., “Interaction between HIF-1α (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1α,” FEBS Letters, vol. 579, no. 28, pp. 6428–6432, 2005. View at Publisher · View at Google Scholar · View at PubMed
- R. Bilton, N. Mazure, E. Trottier et al., “Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1α and is not induced by hypoxia or HIF,” Journal of Biological Chemistry, vol. 280, no. 35, pp. 31132–31140, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. S. Fisher, S. Des Etages, L. Hayes, K. Crimin, and B. Li, “Analysis of ARD1 function in hypoxia response using retroviral RNA interference,” Journal of Biological Chemistry, vol. 280, no. 18, pp. 17749–17757, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- T. A. Murray-Rust, N. J. Oldham, K. S. Hewitson, and C. J. Schofield, “Purified recombinant hARD1 does not catalyse acetylation of Lys 532 of HIF-1α fragments in vitro,” FEBS Letters, vol. 580, no. 8, pp. 1911–1918, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S.-H. Kim, J. A. Park, J. H. Kim et al., “Characterization of ARD1 variants in mammalian cells,” Biochemical and Biophysical Research Communications, vol. 340, no. 2, pp. 422–427, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- N. Sanchez-Puig and A. R. Fersht, “Characterization of the native and fibrillar conformation of the human nalpha-acetyltransferase ard1,” Protein Science, vol. 15, no. 8, pp. 1968–1976, 2006.
- J. H. Seo, J.-H. Cha, J.-H. Park et al., “Arrest defective 1 autoacetylation is a critical step in its ability to stimulate cancer cell proliferation,” Cancer Research, vol. 70, no. 11, pp. 4422–4432, 2010. View at Publisher · View at Google Scholar · View at PubMed
- C.-C. Chang, M.-T. Lin, B.-R. Lin et al., “Effect of connective tissue growth factor on hypoxia-inducible factor 1α degradation and tumor angiogenesis,” Journal of the National Cancer Institute, vol. 98, no. 14, pp. 984–995, 2006. View at Publisher · View at Google Scholar · View at PubMed
- S. Lin, S.-C. Tsai, C.-C. Lee, B.-W. Wang, J.-Y. Liou, and K.-G. Shyu, “Berberine inhibits HIF-1α expression via enhanced proteolysis,” Molecular Pharmacology, vol. 66, no. 3, pp. 612–619, 2004. View at Scopus
- G. Xenaki, T. Ontikatze, R. Rajendran et al., “PCAF is an HIF-1α cofactor that regulates p53 transcriptional activity in hypoxia,” Oncogene, vol. 27, no. 44, pp. 5785–5796, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- E. M. Dioum, R. Chen, M. S. Alexander et al., “Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1,” Science, vol. 324, no. 5932, pp. 1289–1293, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- W. Luo, J. Zhong, R. Chang, H. Hu, A. Pandey, and G. L. Semenza, “Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but not HIF-2α,” Journal of Biological Chemistry, vol. 285, no. 6, pp. 3651–3663, 2010. View at Publisher · View at Google Scholar · View at PubMed
- G.-C. Zeng, H. L. Ozer, and R. Hand, “Further characterization of the phenotype of ts20, a DNA(ts) mutant of BALB/3T3 cells,” Experimental Cell Research, vol. 160, no. 1, pp. 184–196, 1985. View at Scopus
- J. Buchner, “Hsp90 and Co.—a holding for folding,” Trends in Biochemical Sciences, vol. 24, no. 4, pp. 136–141, 1999. View at Publisher · View at Google Scholar · View at Scopus
- G. Chiosis, E. C. Lopes, and D. Solit, “Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents,” Current Opinion in Investigational Drugs, vol. 7, no. 6, pp. 534–541, 2006. View at Scopus
- M. P. Goetz, D. O. Toft, M. M. Ames, and C. Erlichman, “The Hsp90 chaperone complex as a novel target for cancer therapy,” Annals of Oncology, vol. 14, no. 8, pp. 1169–1176, 2003. View at Publisher · View at Google Scholar · View at Scopus
- J. Ai, Y. Wang, J. A. Dar et al., “HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer,” Molecular Endocrinology, vol. 23, no. 12, pp. 1963–1972, 2009. View at Publisher · View at Google Scholar · View at PubMed
- V. D. Kekatpure, A. J. Dannenberg, and K. Subbaramaiah, “HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling,” Journal of Biological Chemistry, vol. 284, no. 12, pp. 7436–7445, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. Basak, D. Pookot, E. J. Noonan, and R. Dahiya, “Genistein down-regulates androgen receptor by modulating HDAC6-Hsp90 chaperone function,” Molecular Cancer Therapeutics, vol. 7, no. 10, pp. 3195–3202, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- R. Rao, W. Fiskus, Y. Yang et al., “HDAC6 inhibition enhances 17-AAG mediated abrogation of hsp90 chaperone function in human leukemia cells,” Blood, vol. 112, no. 5, pp. 1886–1893, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- J. J. Kovacs, P. J. M. Murphy, S. Gaillard et al., “HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor,” Molecular Cell, vol. 18, no. 5, pp. 601–607, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. W. L'Hernault and J. L. Rosenbaum, “Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine,” Biochemistry, vol. 24, no. 2, pp. 473–478, 1985.
- H. Maruta, K. Greer, and J. L. Rosenbaum, “The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules,” Journal of Cell Biology, vol. 103, no. 2, pp. 571–579, 1986. View at Scopus
- A. D.-A. Tran, T. P. Marmo, A. A. Salam et al., “HDAC6 deacetylation of tubulin modulates dynamics of cellular adhesions,” Journal of Cell Science, vol. 120, no. 8, pp. 1469–1479, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Boyault, K. Sadoul, M. Pabion, and S. Khochbin, “HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination,” Oncogene, vol. 26, no. 37, pp. 5468–5476, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- S. L. Thomas, D. Zhong, W. Zhou et al., “EF24, a novel curcumin analog, disrupts the microtubule cytoskeleton and inhibits HIF-1,” Cell Cycle, vol. 7, no. 15, pp. 2409–2417, 2008. View at Scopus
- J. H. Lim, Y. M. Lee, Y. S. Chun, J. Chen, J. E. Kim, and J. W. Park, “Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha,” Molecular cell, vol. 38, no. 6, pp. 864–878, 2010.
- S. Zhao, W. Xu, W. Jiang et al., “Regulation of cellular metabolism by protein lysine acetylation,” Science, vol. 327, no. 5968, pp. 1000–1004, 2010. View at Publisher · View at Google Scholar · View at PubMed
- A. Granger, I. Abdullah, F. Huebner et al., “Histone deacetylase inhibition reduces myocardial ischemia-reperfusion injury in mice,” FASEB Journal, vol. 22, no. 10, pp. 3549–3560, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- C. Colussi, B. Illi, J. Rosati et al., “Histone deacetylase inhibitors: keeping momentum for neuromuscular and cardiovascular diseases treatment,” Pharmacological Research, vol. 62, no. 1, pp. 3–10, 2010. View at Publisher · View at Google Scholar · View at PubMed
- C. Colussi, R. Berni, J. Rosati et al., “The histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces cardiac arrhythmias in dystrophic mice,” Cardiovascular Research, vol. 87, no. 1, pp. 73–82, 2010. View at Publisher · View at Google Scholar · View at PubMed