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Volumn 12, Issue 7, 2011, Pages 4705-4721

Epigenetics: New questions on the response to hypoxia

Author keywords

Chromatin; HIF; Histone; Jumonji; Oxygen; Stress

Indexed keywords

HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 7; HISTONE DEMETHYLASE; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; SIRTUIN 1; CHROMATIN; HISTONE;

EID: 79960785531     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12074705     Document Type: Review
Times cited : (63)

References (97)
  • 1
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: The central role of the HIF hydroxylase pathway
    • Kaelin, W.G., Jr.; Ratcliffe, P.J. Oxygen sensing by metazoans: The central role of the HIF hydroxylase pathway. Mol. Cell 2008, 30, 393-402.
    • (2008) Mol. Cell , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 2
    • 85047682984 scopus 로고    scopus 로고
    • Regulation of oxygen homeostasis by hypoxia-inducible factor 1
    • Semenza, G.L., Regulation of oxygen homeostasis by hypoxia-inducible factor 1. Physiology (Bethesda) 2009, 24, 97-106.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 97-106
    • Semenza, G.L.1
  • 3
    • 78649364332 scopus 로고    scopus 로고
    • Hypoxia-inducible factors and the response to hypoxic stress
    • Majmundar, A.J.; Wong, W.J.; Simon, M.C. Hypoxia-inducible factors and the response to hypoxic stress. Mol. Cell 2010, 40, 294-309.
    • (2010) Mol. Cell , vol.40 , pp. 294-309
    • Majmundar, A.J.1    Wong, W.J.2    Simon, M.C.3
  • 4
    • 0029074024 scopus 로고
    • Development of retinal vasculature is mediated by hypoxia-induced vascular endothelial growth factor (VEGF) expression by neuroglia
    • Stone, J.; Itin, A.; Alon, T.; Pe'er, J.; Gnessin, H.; Chan-Ling, T.; Keshet, E. Development of retinal vasculature is mediated by hypoxia-induced vascular endothelial growth factor (VEGF) expression by neuroglia. J. Neurosci. 1995, 15, 4738-4747.
    • (1995) J. Neurosci , vol.15 , pp. 4738-4747
    • Stone, J.1    Itin, A.2    Alon, T.3    Pe'er, J.4    Gnessin, H.5    Chan-Ling, T.6    Keshet, E.7
  • 5
    • 0032882169 scopus 로고    scopus 로고
    • Hypoxic microenvironment within an embryo induces apoptosis and is essential for proper morphological development
    • Chen, E.Y.; Fujinaga, M.; Giaccia, A.J. Hypoxic microenvironment within an embryo induces apoptosis and is essential for proper morphological development. Teratology 1999, 60, 215-225.
    • (1999) Teratology , vol.60 , pp. 215-225
    • Chen, E.Y.1    Fujinaga, M.2    Giaccia, A.J.3
  • 6
    • 58149167063 scopus 로고    scopus 로고
    • Essential role of developmentally activated hypoxia-inducible factor 1alpha for cardiac morphogenesis and function
    • Krishnan, J.; Ahuja, P.; Bodenmann, S.; Knapik, D.; Perriard, E.; Krek, W.; Perriard, J.C. Essential role of developmentally activated hypoxia-inducible factor 1alpha for cardiac morphogenesis and function. Circ. Res. 2008, 103, 1139-1146.
    • (2008) Circ. Res , vol.103 , pp. 1139-1146
    • Krishnan, J.1    Ahuja, P.2    Bodenmann, S.3    Knapik, D.4    Perriard, E.5    Krek, W.6    Perriard, J.C.7
  • 7
    • 71649094085 scopus 로고    scopus 로고
    • The role of hypoxia in development of the Mammalian embryo
    • Dunwoodie, S.L. The role of hypoxia in development of the Mammalian embryo. Dev. Cell 2009, 17, 755-773.
    • (2009) Dev. Cell , vol.17 , pp. 755-773
    • Dunwoodie, S.L.1
  • 8
    • 33645452371 scopus 로고    scopus 로고
    • Chronic hypoxia and tubulointerstitial injury: A final common pathway to end-stage renal failure
    • Nangaku, M. Chronic hypoxia and tubulointerstitial injury: A final common pathway to end-stage renal failure. J. Am. Soc. Nephrol. 2006, 17, 17-25.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 17-25
    • Nangaku, M.1
  • 9
    • 72449163624 scopus 로고    scopus 로고
    • Hypoxia inducible factor 1 as a therapeutic target in ischemic stroke
    • Shi, H. Hypoxia inducible factor 1 as a therapeutic target in ischemic stroke. Curr. Med. Chem. 2009, 16, 4593-4600.
    • (2009) Curr. Med. Chem , vol.16 , pp. 4593-4600
    • Shi, H.1
  • 10
    • 78650373860 scopus 로고    scopus 로고
    • Hypoxia and hypoxia-inducible factors: Master regulators of metastasis
    • Lu, X.; Kang, Y. Hypoxia and hypoxia-inducible factors: Master regulators of metastasis. Clin. Cancer Res. 2010, 16, 5928-5935.
    • (2010) Clin. Cancer Res , vol.16 , pp. 5928-5935
    • Lu, X.1    Kang, Y.2
  • 11
    • 76049100577 scopus 로고    scopus 로고
    • HIF-1: Upstream and downstream of cancer metabolism
    • Semenza, G.L. HIF-1: Upstream and downstream of cancer metabolism. Curr. Opin. Genet. Dev. 2010, 20, 51-56.
    • (2010) Curr. Opin. Genet. Dev , vol.20 , pp. 51-56
    • Semenza, G.L.1
  • 12
    • 0027461553 scopus 로고
    • Inducible operation of the erythropoietin 3' enhancer in multiple cell lines: Evidence for a widespread oxygen-sensing mechanism
    • Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J. Inducible operation of the erythropoietin 3' enhancer in multiple cell lines: Evidence for a widespread oxygen-sensing mechanism. Proc. Natl. Acad. Sci. USA 1993, 90, 2423-2427.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2423-2427
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 13
    • 0027210562 scopus 로고
    • General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia
    • Wang, G.L.; Semenza, G.L. General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia. Proc. Natl. Acad. Sci. USA 1993, 90, 4304-4308.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 14
    • 0035812772 scopus 로고    scopus 로고
    • HIF-1, O(2), and the 3 PHDs: How animal cells signal hypoxia to the nucleus
    • Semenza, G.L. HIF-1, O(2), and the 3 PHDs: How animal cells signal hypoxia to the nucleus. Cell 2001, 107, 1-3.
    • (2001) Cell , vol.107 , pp. 1-3
    • Semenza, G.L.1
  • 15
    • 0242330181 scopus 로고    scopus 로고
    • Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor
    • R.K. Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor. Genes. Dev. 2003, 17, 2614-2623.
    • (2003) Genes. Dev , vol.17 , pp. 2614-2623
  • 16
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R.K.; McKnight, S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 2001, 294, 1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 22
    • 40649114443 scopus 로고    scopus 로고
    • Hypoxia induces a novel signature of chromatin modifications and global repression of transcription
    • Johnson, A.B.; Denko, N.; Barton, M.C. Hypoxia induces a novel signature of chromatin modifications and global repression of transcription. Mutat. Res. 2008, 640, 174-179.
    • (2008) Mutat. Res , vol.640 , pp. 174-179
    • Johnson, A.B.1    Denko, N.2    Barton, M.C.3
  • 23
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg, R.D.; Lorch, Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 1999, 98, 285-294.
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 24
    • 0035313769 scopus 로고    scopus 로고
    • Nucleosomes and the chromatin fiber
    • Hayes, J.J.; Hansen, J.C. Nucleosomes and the chromatin fiber. Curr. Opin. Genet. Dev. 2001, 11, 124-129.
    • (2001) Curr. Opin. Genet. Dev , vol.11 , pp. 124-129
    • Hayes, J.J.1    Hansen, J.C.2
  • 25
    • 0037072601 scopus 로고    scopus 로고
    • Molecular biology. Chromatin higher order folding--wrapping up transcription
    • Horn, P.J.; Peterson, C.L. Molecular biology. Chromatin higher order folding--wrapping up transcription. Science 2002, 297, 1824-1827.
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J.1    Peterson, C.L.2
  • 26
    • 18744421874 scopus 로고    scopus 로고
    • Chromatin higher order structure: Opening up chromatin for transcription
    • Nemeth, A.; Langst, G. Chromatin higher order structure: Opening up chromatin for transcription. Brief. Funct. Genomic Proteomic 2004, 2, 334-343.
    • (2004) Brief. Funct. Genomic Proteomic , vol.2 , pp. 334-343
    • Nemeth, A.1    Langst, G.2
  • 27
    • 33847106524 scopus 로고    scopus 로고
    • Higher-order structures of chromatin: The elusive 30 nm fiber
    • Tremethick, D.J. Higher-order structures of chromatin: The elusive 30 nm fiber. Cell 2007, 128, 651-654.
    • (2007) Cell , vol.128 , pp. 651-654
    • Tremethick, D.J.1
  • 28
  • 29
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T.; Allis, C.D. Translating the histone code. Science 2001, 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 30
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson, C.L.; Laniel, M.A. Histones and histone modifications. Curr. Biol. 2004, 14, R546-R551.
    • (2004) Curr. Biol , vol.14
    • Peterson, C.L.1    Laniel, M.A.2
  • 31
    • 77956153243 scopus 로고    scopus 로고
    • The language of histone crosstalk
    • Lee, J.S.; Smith, E.; Shilatifard, A. The language of histone crosstalk. Cell 2010, 142, 682-685.
    • (2010) Cell , vol.142 , pp. 682-685
    • Lee, J.S.1    Smith, E.2    Shilatifard, A.3
  • 32
    • 0029157378 scopus 로고
    • Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions
    • Eisen, J.A.; Sweder, K.S.; Hanawalt, P.C. Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions. Nucleic Acids Res. 1995, 23, 2715-2723.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2715-2723
    • Eisen, J.A.1    Sweder, K.S.2    Hanawalt, P.C.3
  • 33
    • 0032742874 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodelling: SWI/SNF and Co. are on the job
    • Muchardt, C.; Yaniv, M. ATP-dependent chromatin remodelling: SWI/SNF and Co. are on the job. J. Mol. Biol. 1999, 293, 187-198.
    • (1999) J. Mol. Biol , vol.293 , pp. 187-198
    • Muchardt, C.1    Yaniv, M.2
  • 35
    • 34147161066 scopus 로고    scopus 로고
    • Hypoxia-induced and stress-specific changes in chromatin structure and function
    • Johnson, A.B.; Barton, M.C. Hypoxia-induced and stress-specific changes in chromatin structure and function. Mutat. Res. 2007, 618, 149-162.
    • (2007) Mutat. Res , vol.618 , pp. 149-162
    • Johnson, A.B.1    Barton, M.C.2
  • 37
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema, M.; Hirota, K.; Mimura, J.; Abe, H.; Yodoi, J.; Sogawa, K.; Poellinger, L.; Fujii-Kuriyama, Y. Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 1999, 18, 1905-1914.
    • (1999) EMBO J , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 38
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero, P.; Okamoto, K.; Coumailleau, P.; O'Brien, S.; Tanaka, H.; Poellinger, L. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell Biol. 2000, 20, 402-415.
    • (2000) Mol. Cell Biol , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 39
    • 0037064141 scopus 로고    scopus 로고
    • Functional analysis of hypoxia-inducible factor-1 alpha-mediated transactivation. Identification of amino acid residues critical for transcriptional activation and/or interaction with CREB-binding protein
    • Ruas, J.L.; Poellinger, L.; Pereira, T. Functional analysis of hypoxia-inducible factor-1 alpha-mediated transactivation. Identification of amino acid residues critical for transcriptional activation and/or interaction with CREB-binding protein. J. Biol. Chem. 2002, 277, 38723-38730.
    • (2002) J. Biol. Chem , vol.277 , pp. 38723-38730
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 40
    • 14044257943 scopus 로고    scopus 로고
    • Role of CBP in regulating HIF-1-mediated activation of transcription
    • Ruas, J.L.; Poellinger, L.; Pereira, T. Role of CBP in regulating HIF-1-mediated activation of transcription. J. Cell Sci. 2005, 118, 301-311.
    • (2005) J. Cell Sci , vol.118 , pp. 301-311
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 41
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity
    • Kato, H.; Tamamizu-Kato, S.; Shibasaki, F. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. J. Biol. Chem. 2004, 279, 41966-41974.
    • (2004) J. Biol. Chem , vol.279 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 42
    • 57749177692 scopus 로고    scopus 로고
    • Transcriptional activation of hypoxia-inducible factor-1alpha by HDAC4 and HDAC5 involves differential recruitment of p300 and FIH-1
    • Seo, H.W.; Kim, E.J.; Na, H.; Lee, M.O. Transcriptional activation of hypoxia-inducible factor-1alpha by HDAC4 and HDAC5 involves differential recruitment of p300 and FIH-1. FEBS Lett. 2009, 583, 55-60.
    • (2009) FEBS Lett , vol.583 , pp. 55-60
    • Seo, H.W.1    Kim, E.J.2    Na, H.3    Lee, M.O.4
  • 43
    • 8744302175 scopus 로고    scopus 로고
    • Roles of Brahma and Brahma/SWI2-related gene 1 in hypoxic induction of the erythropoietin gene
    • Wang, F.; Zhang, R.; Beischlag, T.V.; Muchardt, C.; Yaniv, M.; Hankinson, O. Roles of Brahma and Brahma/SWI2-related gene 1 in hypoxic induction of the erythropoietin gene. J. Biol. Chem. 2004, 279, 46733-46741.
    • (2004) J. Biol. Chem , vol.279 , pp. 46733-46741
    • Wang, F.1    Zhang, R.2    Beischlag, T.V.3    Muchardt, C.4    Yaniv, M.5    Hankinson, O.6
  • 44
    • 79251566746 scopus 로고    scopus 로고
    • Physical and functional HAT/HDAC interplay regulates protein acetylation balance
    • Peserico, A.; Simone, C. Physical and functional HAT/HDAC interplay regulates protein acetylation balance. J. Biomed. Biotechnol. 2011, 2011, 371-832.
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 371-832
    • Peserico, A.1    Simone, C.2
  • 46
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak, M.; Ishii, H.; Sun, J.M.; Pazin, M.J.; Davie, J.R.; Peterson, C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311, 844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 47
    • 4143098311 scopus 로고    scopus 로고
    • CBP and p300: HATs for different occasions
    • Kalkhoven, E. CBP and p300: HATs for different occasions. Biochem. Pharmacol. 2004, 68, 1145-1155.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 1145-1155
    • Kalkhoven, E.1
  • 48
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J.; Kouzarides, T. The CBP co-activator is a histone acetyltransferase. Nature 1996, 384, 641-643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 49
    • 0029968939 scopus 로고    scopus 로고
    • Human p300 protein is a coactivator for the transcription factor MyoD
    • Yuan, W.; Condorelli, G.; Caruso, M.; Felsani, A.; Giordano, A. Human p300 protein is a coactivator for the transcription factor MyoD. J. Biol. Chem. 1996, 271, 9009-9013.
    • (1996) J. Biol. Chem , vol.271 , pp. 9009-9013
    • Yuan, W.1    Condorelli, G.2    Caruso, M.3    Felsani, A.4    Giordano, A.5
  • 52
    • 77449159578 scopus 로고    scopus 로고
    • Complex regulation of the transactivation function of hypoxia-inducible factor-1 alpha by direct interaction with two distinct domains of the CREB-binding protein/p300
    • Ruas, J.L.; Berchner-Pfannschmidt, U.; Malik, S.; Gradin, K.; Fandrey, J.; Roeder, R.G.; Pereira, T.; Poellinger, L. Complex regulation of the transactivation function of hypoxia-inducible factor-1 alpha by direct interaction with two distinct domains of the CREB-binding protein/p300. J. Biol. Chem. 2010, 285, 2601-2609.
    • (2010) J. Biol. Chem , vol.285 , pp. 2601-2609
    • Ruas, J.L.1    Berchner-Pfannschmidt, U.2    Malik, S.3    Gradin, K.4    Fandrey, J.5    Roeder, R.G.6    Pereira, T.7    Poellinger, L.8
  • 53
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando, D.; Peet, D.J.; Whelan, D.A.; Gorman, J.J.; Whitelaw, M.L. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 2002, 295, 858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 54
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon, P.C.; Hirota, K.; Semenza, G.L. FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 2001, 15, 2675-2686.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 55
    • 70449527373 scopus 로고    scopus 로고
    • Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing
    • Webb, J.D.; Coleman, M.L.; Pugh, C.W. Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing. Cell. Mol. Life Sci. 2009, 66, 3539-3554.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 3539-3554
    • Webb, J.D.1    Coleman, M.L.2    Pugh, C.W.3
  • 56
    • 0037470159 scopus 로고    scopus 로고
    • Identification of residues critical for regulation of protein stability and the transactivation function of the hypoxia-inducible factor-1alpha by the von Hippel-Lindau tumor suppressor gene product
    • Pereira, T.; Zheng, X.; Ruas, J.L.; Tanimoto, K.; Poellinger, L. Identification of residues critical for regulation of protein stability and the transactivation function of the hypoxia-inducible factor-1alpha by the von Hippel-Lindau tumor suppressor gene product. J. Biol. Chem. 2003, 278, 6816-6823.
    • (2003) J. Biol. Chem , vol.278 , pp. 6816-6823
    • Pereira, T.1    Zheng, X.2    Ruas, J.L.3    Tanimoto, K.4    Poellinger, L.5
  • 57
    • 40949132841 scopus 로고    scopus 로고
    • Turn me on: Regulating HIF transcriptional activity
    • Lisy, K.; Peet, D.J. Turn me on: Regulating HIF transcriptional activity. Cell Death Differ. 2008, 15, 642-649.
    • (2008) Cell Death Differ , vol.15 , pp. 642-649
    • Lisy, K.1    Peet, D.J.2
  • 58
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim, J.H.; Lee, Y.M.; Chun, Y.S.; Chen, J.; Kim, J.E.; Park, J.W. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol. Cell 2010, 38, 864-878.
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6
  • 59
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum, E.M.; Chen, R.; Alexander, M.S.; Zhang, Q.; Hogg, R.T.; Gerard, R.D.; Garcia, J.A. Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 2009, 324, 1289-1293.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 60
    • 0031835957 scopus 로고    scopus 로고
    • Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein
    • Ebert, B.L.; Bunn, H.F. Regulation of transcription by hypoxia requires a multiprotein complex that includes hypoxia-inducible factor 1, an adjacent transcription factor, and p300/CREB binding protein. Mol. Cell. Biol. 1998, 18, 4089-4096.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4089-4096
    • Ebert, B.L.1    Bunn, H.F.2
  • 62
    • 77956322192 scopus 로고    scopus 로고
    • Roles of coactivators in hypoxic induction of the erythropoietin gene
    • e10002
    • Wang, F.; Zhang, R.; Wu, X.; Hankinson, O. Roles of coactivators in hypoxic induction of the erythropoietin gene. PLoS One 2010, 5, e10002.
    • (2010) PLoS One , vol.5
    • Wang, F.1    Zhang, R.2    Wu, X.3    Hankinson, O.4
  • 64
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth
    • Krieg, A.J.; Rankin, E.B.; Chan, D.; Razorenova, O.; Fernandez, S.; Giaccia, A.J. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Mol. Cell. Biol. 2010, 30, 344-353.
    • (2010) Mol. Cell. Biol , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 65
    • 77952795537 scopus 로고    scopus 로고
    • Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase
    • Zhou, X.; Sun, H.; Chen, H.; Zavadil, J.; Kluz, T.; Arita, A.; Costa, M. Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase. Cancer Res. 2010, 70, 4214-4221.
    • (2010) Cancer Res , vol.70 , pp. 4214-4221
    • Zhou, X.1    Sun, H.2    Chen, H.3    Zavadil, J.4    Kluz, T.5    Arita, A.6    Costa, M.7
  • 66
    • 33645823895 scopus 로고    scopus 로고
    • Permissive effects of oxygen on cyclic AMP and interleukin-1 stimulation of surfactant protein A gene expression are mediated by epigenetic mechanisms
    • Islam, K.N.; Mendelson, C.R. Permissive effects of oxygen on cyclic AMP and interleukin-1 stimulation of surfactant protein A gene expression are mediated by epigenetic mechanisms. Mol. Cell. Biol. 2006, 26, 2901-2912.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2901-2912
    • Islam, K.N.1    Mendelson, C.R.2
  • 67
    • 33749494456 scopus 로고    scopus 로고
    • Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells
    • Chen, H.; Yan, Y.; Davidson, T.L.; Shinkai, Y.; Costa, M. Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells. Cancer Res. 2006, 66, 9009-9016.
    • (2006) Cancer Res , vol.66 , pp. 9009-9016
    • Chen, H.1    Yan, Y.2    Davidson, T.L.3    Shinkai, Y.4    Costa, M.5
  • 68
    • 78651086487 scopus 로고    scopus 로고
    • Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity
    • Tausendschon, M.; Dehne, N.; Brune, B. Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity. Cytokine 2011, 53, 256-262.
    • (2011) Cytokine , vol.53 , pp. 256-262
    • Tausendschon, M.1    Dehne, N.2    Brune, B.3
  • 69
    • 0037382681 scopus 로고    scopus 로고
    • Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
    • Yang, X.J.; Seto, E. Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression. Curr. Opin. Genet. Dev. 2003, 13, 143-153.
    • (2003) Curr. Opin. Genet. Dev , vol.13 , pp. 143-153
    • Yang, X.J.1    Seto, E.2
  • 70
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3 histone deacetylase complexes in development
    • Ahringer, J. NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 2000, 16, 351-356.
    • (2000) Trends Genet , vol.16 , pp. 351-356
    • Ahringer, J.1
  • 71
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G.; Guarente, L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 2004, 73, 417-435.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 72
    • 16244366803 scopus 로고    scopus 로고
    • Histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang, X.J.; Gregoire, S. Class II histone deacetylases: From sequence to function, regulation, and clinical implication. Mol. Cell. Biol. 2005, 25, 2873-2884.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2    Class, I.I.3
  • 73
    • 34547875013 scopus 로고    scopus 로고
    • NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs
    • Vaquero, A.; Sternglanz, R.; Reinberg, D. NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs. Oncogene 2007, 26, 5505-5520.
    • (2007) Oncogene , vol.26 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 74
    • 79251576774 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: The epigenetic therapeutics that repress hypoxia-inducible factors
    • Chen, S.; Sang, N. Histone deacetylase inhibitors: The epigenetic therapeutics that repress hypoxia-inducible factors. J. Biomed. Biotechnol. 2011, 2011, 197-946.
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 197-946
    • Chen, S.1    Sang, N.2
  • 75
    • 77951938407 scopus 로고    scopus 로고
    • Downregulation of a tumor suppressor RECK by hypoxia through recruitment of HDAC1 and HIF-1alpha to reverse HRE site in the promoter
    • Lee, K.J.; Lee, K.Y.; Lee, Y.M. Downregulation of a tumor suppressor RECK by hypoxia through recruitment of HDAC1 and HIF-1alpha to reverse HRE site in the promoter. Biochim. Biophys. Acta 2010, 1803, 608-616.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 608-616
    • Lee, K.J.1    Lee, K.Y.2    Lee, Y.M.3
  • 77
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath, D.M.; Kong, X.; Liang, D.; Lin, Z.; Chou, A.; Jiang, Y.; Fang, J.; Caro, J.; Sang, N. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J. Biol. Chem. 2006, 281, 13612-13619.
    • (2006) J. Biol. Chem , vol.281 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3    Lin, Z.4    Chou, A.5    Jiang, Y.6    Fang, J.7    Caro, J.8    Sang, N.9
  • 79
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target
    • Johnstone, R.W.; Licht, J.D. Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target? Cancer Cell 2003, 4, 13-18.
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 81
    • 63249087504 scopus 로고    scopus 로고
    • SWI/SNF regulates the cellular response to hypoxia
    • Kenneth, N.S.; Mudie, S.; van Uden, P.; Rocha, S. SWI/SNF regulates the cellular response to hypoxia. J. Biol. Chem. 2009, 284, 4123-4131.
    • (2009) J. Biol. Chem , vol.284 , pp. 4123-4131
    • Kenneth, N.S.1    Mudie, S.2    van Uden, P.3    Rocha, S.4
  • 82
    • 77954218952 scopus 로고    scopus 로고
    • Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription
    • Tang, L.; Nogales, E.; Ciferri, C., Structure and function of SWI/SNF chromatin remodeling complexes and mechanistic implications for transcription. Prog. Biophys. Mol. Biol. 2010, 102, 122-128.
    • (2010) Prog. Biophys. Mol. Biol , vol.102 , pp. 122-128
    • Tang, L.1    Nogales, E.2    Ciferri, C.3
  • 84
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose, R.J.; Kallin, E.M.; Zhang, Y. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 2006, 7, 715-727.
    • (2006) Nat. Rev. Genet , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 85
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: Emerging roles in development, physiology and disease
    • Shi, Y. Histone lysine demethylases: Emerging roles in development, physiology and disease. Nat. Rev. Genet. 2007, 8, 829-833.
    • (2007) Nat. Rev. Genet , vol.8 , pp. 829-833
    • Shi, Y.1
  • 86
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi, Y.; Whetstine, J.R. Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 2007, 25, 1-14.
    • (2007) Mol. Cell , vol.25 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 87
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • Loenarz, C.; Schofield, C.J. Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 2008, 4, 152-156.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 88
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S.L., The complex language of chromatin regulation during transcription. Nature 2007, 447, 407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 89
    • 63449103705 scopus 로고    scopus 로고
    • Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis
    • Xia, X.; Lemieux, M.E.; Li, W.; Carroll, J.S.; Brown, M.; Liu, X.S.; Kung, A.L. Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis. Proc. Natl. Acad. Sci. USA 2009, 106, 4260-4265.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4260-4265
    • Xia, X.1    Lemieux, M.E.2    Li, W.3    Carroll, J.S.4    Brown, M.5    Liu, X.S.6    Kung, A.L.7
  • 91
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer, S.; Kristensen, M.M.; Jensen, K.S.; Johansen, J.V.; Staller, P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 2008, 283, 36542-36552.
    • (2008) J. Biol. Chem , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 96
    • 77954661616 scopus 로고    scopus 로고
    • Epigenetics the epicenter of the hypoxic response
    • Watson, J.A.; Watson, C.J.; McCann, A.; Baugh, J. Epigenetics the epicenter of the hypoxic response. Epigenetics 2010, 5, 293-296.
    • (2010) Epigenetics , vol.5 , pp. 293-296
    • Watson, J.A.1    Watson, C.J.2    McCann, A.3    Baugh, J.4
  • 97
    • 75349114759 scopus 로고    scopus 로고
    • Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia
    • doi: 10.1186/gb-2009-10-10-r113
    • Xia, X.; Kung, A.L. Preferential binding of HIF-1 to transcriptionally active loci determines cell-type specific response to hypoxia. Genome Biol 2009, 10, doi: 10.1186/gb-2009-10-10-r113.
    • (2009) Genome Biol , vol.10
    • Xia, X.1    Kung, A.L.2


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