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Volumn 108, Issue , 2015, Pages 1-7

Hypoxia-inducible factor-1alpha in hepatic fibrosis: A promising therapeutic target

Author keywords

Hepatic fibrosis; Hypoxia inducible factor 1alpha; Signaling pathways; Therapeutic target

Indexed keywords

HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; SUNITINIB; TOPOTECAN; VASCULOTROPIN; VASCULOTROPIN INHIBITOR; HIF1A PROTEIN, HUMAN;

EID: 84910045079     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.10.013     Document Type: Review
Times cited : (55)

References (86)
  • 1
    • 0037220482 scopus 로고    scopus 로고
    • Liver fibrosis - From bench to bedside
    • S.L. Friedman Liver fibrosis - from bench to bedside J. Hepatol. 38 Suppl. 1 2003 S38 S53
    • (2003) J. Hepatol. , vol.38 , Issue.SUPPL. 1 , pp. 38-S53
    • Friedman, S.L.1
  • 4
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: Role of the HIF system
    • C.W. Pugh, and P.J. Ratcliffe Regulation of angiogenesis by hypoxia: role of the HIF system Nat. Med. 9 2003 677 684
    • (2003) Nat. Med. , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 6
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • G.L. Semenza Hypoxia-inducible factors in physiology and medicine Cell 148 2012 399 408
    • (2012) Cell , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 7
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • G.L. Wang, and G.L. Semenza Purification and characterization of hypoxia-inducible factor 1 J. Biol. Chem. 270 1995 1230 1237
    • (1995) J. Biol. Chem. , vol.270 , pp. 1230-1237
    • Wang, G.L.1    Semenza, G.L.2
  • 8
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • B.H. Jiang, E. Rue, G.L. Wang, R. Roe, and G.L. Semenza Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1 J. Biol. Chem. 271 1996 17771 17778
    • (1996) J. Biol. Chem. , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 9
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • L.E. Huang, Z. Arany, D.M. Livingston, and H.F. Bunn Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit J. Biol. Chem. 271 1996 32253 32259
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 10
    • 0030914648 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor 1alpha: Posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor
    • P.J. Kallio, I. Pongratz, K. Gradin, J. McGuire, and L. Poellinger Activation of hypoxia-inducible factor 1alpha: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor Proc. Natl. Acad. Sci. U. S. A. 94 1997 5667 5672
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5667-5672
    • Kallio, P.J.1    Pongratz, I.2    Gradin, K.3    McGuire, J.4    Poellinger, L.5
  • 14
    • 0036846033 scopus 로고    scopus 로고
    • Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803
    • L.A. McNeill, K.S. Hewitson, T.D. Claridge, J.F. Seibel, L.E. Horsfall, and C.J. Schofield Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803 Biochem. J. 367 2002 571 575
    • (2002) Biochem. J. , vol.367 , pp. 571-575
    • McNeill, L.A.1    Hewitson, K.S.2    Claridge, T.D.3    Seibel, J.F.4    Horsfall, L.E.5    Schofield, C.J.6
  • 15
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • 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 295 2002 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
  • 16
    • 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
    • P.C. Mahon, K. Hirota, and G.L. Semenza FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity Genes. Dev. 15 2001 2675 2686
    • (2001) Genes. Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 18
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • G.L. Semenza, B.H. Jiang, S.W. Leung, R. Passantino, J.P. Concordet, P. Maire, and A. Giallongo Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia-inducible factor 1 J. Biol. Chem. 271 1996 32529 32537
    • (1996) J. Biol. Chem. , vol.271 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.H.2    Leung, S.W.3    Passantino, R.4    Concordet, J.P.5    Maire, P.6    Giallongo, A.7
  • 19
    • 1542344522 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 and oncogenic signalling
    • J.I. Bardos, and M. Ashcroft Hypoxia-inducible factor-1 and oncogenic signalling Bioessays 26 2004 262 269
    • (2004) Bioessays , vol.26 , pp. 262-269
    • Bardos, J.I.1    Ashcroft, M.2
  • 20
    • 78650792166 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha regulates the expression of genes in hypoxic hepatic stellate cells important for collagen deposition and angiogenesis
    • B.L. Copple, S. Bai, L.D. Burgoon, and J.O. Moon Hypoxia-inducible factor-1alpha regulates the expression of genes in hypoxic hepatic stellate cells important for collagen deposition and angiogenesis Liver Int. 31 2011 230 244
    • (2011) Liver Int. , vol.31 , pp. 230-244
    • Copple, B.L.1    Bai, S.2    Burgoon, L.D.3    Moon, J.O.4
  • 21
    • 84883827426 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha and MAPK co-regulate activation of hepatic stellate cells upon hypoxia stimulation
    • Y. Wang, Y. Huang, F. Guan, Y. Xiao, J. Deng, H. Chen, X. Chen, J. Li, H. Huang, and C. Shi Hypoxia-inducible factor-1alpha and MAPK co-regulate activation of hepatic stellate cells upon hypoxia stimulation PLoS One 8 2013 e74051
    • (2013) PLoS One , vol.8 , pp. 74051
    • Wang, Y.1    Huang, Y.2    Guan, F.3    Xiao, Y.4    Deng, J.5    Chen, H.6    Chen, X.7    Li, J.8    Huang, H.9    Shi, C.10
  • 22
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • G.L. Wang, B.H. Jiang, E.A. Rue, and G.L. Semenza Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension Proc. Natl. Acad. Sci. U. S. A. 92 1995 5510 5514
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 23
    • 0035478294 scopus 로고    scopus 로고
    • Transduction pathways involved in Hypoxia-Inducible Factor-1 phosphorylation and activation
    • E. Minet, G. Michel, D. Mottet, M. Raes, and C. Michiels Transduction pathways involved in Hypoxia-Inducible Factor-1 phosphorylation and activation Free Radic. Biol. Med. 31 2001 847 855
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 847-855
    • Minet, E.1    Michel, G.2    Mottet, D.3    Raes, M.4    Michiels, C.5
  • 24
    • 84891595627 scopus 로고    scopus 로고
    • Effects of PI3K inhibitor NVP-BKM120 on acquired resistance to gefitinib of human lung adenocarcinoma H1975 cells
    • Y.C. Liang, H.G. Wu, H.J. Xue, Q. Liu, L.L. Shi, T. Liu, and G. Wu Effects of PI3K inhibitor NVP-BKM120 on acquired resistance to gefitinib of human lung adenocarcinoma H1975 cells J. Huazhong Univ. Sci. Technol. Med. Sci. 33 2013 845 851
    • (2013) J. Huazhong Univ. Sci. Technol. Med. Sci. , vol.33 , pp. 845-851
    • Liang, Y.C.1    Wu, H.G.2    Xue, H.J.3    Liu, Q.4    Shi, L.L.5    Liu, T.6    Wu, G.7
  • 26
    • 84863429438 scopus 로고    scopus 로고
    • Nifedipine inhibits hypoxia induced transvascular leakage through down regulation of NFkB
    • K.S.S. S, Veeramohan, P. H, T. Mathew, S. S, and M. C Nifedipine inhibits hypoxia induced transvascular leakage through down regulation of NFkB Respir. Physiol. Neurobiol. 183 2012 26 34
    • (2012) Respir. Physiol. Neurobiol. , vol.183 , pp. 26-34
    • Veeramohan K.S, S.S.1    Mathew, P.H.T.2
  • 29
    • 84883527272 scopus 로고    scopus 로고
    • Novel therapeutic strategy with hypoxia-inducible factors via reversible epigenetic regulation mechanisms in progressive tubulointerstitial fibrosis
    • I. Mimura, T. Tanaka, and M. Nangaku Novel therapeutic strategy with hypoxia-inducible factors via reversible epigenetic regulation mechanisms in progressive tubulointerstitial fibrosis Semin. Nephrol. 33 2013 375 382
    • (2013) Semin. Nephrol. , vol.33 , pp. 375-382
    • Mimura, I.1    Tanaka, T.2    Nangaku, M.3
  • 30
    • 84879556042 scopus 로고    scopus 로고
    • Epigenetic regulation of hypoxia inducible factor in diseases and therapeutics
    • M.P. Nguyen, S. Lee, and Y.M. Lee Epigenetic regulation of hypoxia inducible factor in diseases and therapeutics Arch. Pharm. Res. 36 2013 252 263
    • (2013) Arch. Pharm. Res. , vol.36 , pp. 252-263
    • Nguyen, M.P.1    Lee, S.2    Lee, Y.M.3
  • 31
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • P. Carmeliet, and R.K. Jain Angiogenesis in cancer and other diseases Nature 407 2000 249 257
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 32
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • P. Carmeliet Angiogenesis in life, disease and medicine Nature 438 2005 932 936
    • (2005) Nature , vol.438 , pp. 932-936
    • Carmeliet, P.1
  • 33
    • 77957328518 scopus 로고    scopus 로고
    • Intrahepatic angiogenesis and sinusoidal remodeling in chronic liver disease: New targets for the treatment of portal hypertension?
    • D. Thabut, and V. Shah Intrahepatic angiogenesis and sinusoidal remodeling in chronic liver disease: new targets for the treatment of portal hypertension? J. Hepatol. 53 2010 976 980
    • (2010) J. Hepatol. , vol.53 , pp. 976-980
    • Thabut, D.1    Shah, V.2
  • 35
    • 0036234428 scopus 로고    scopus 로고
    • Hypoxia-induced VEGF and collagen i expressions are associated with angiogenesis and fibrogenesis in experimental cirrhosis
    • C. Corpechot, V. Barbu, D. Wendum, N. Kinnman, C. Rey, R. Poupon, C. Housset, and O. Rosmorduc Hypoxia-induced VEGF and collagen I expressions are associated with angiogenesis and fibrogenesis in experimental cirrhosis Hepatology 35 2002 1010 1021
    • (2002) Hepatology , vol.35 , pp. 1010-1021
    • Corpechot, C.1    Barbu, V.2    Wendum, D.3    Kinnman, N.4    Rey, C.5    Poupon, R.6    Housset, C.7    Rosmorduc, O.8
  • 37
    • 77956828137 scopus 로고    scopus 로고
    • Irresponsiveness of two retinoblastoma cases to conservative therapy correlates with up- regulation of hERG1 channels and of the VEGF-A pathway
    • P. Fortunato, S. Pillozzi, A. Tamburini, L. Pollazzi, A. Franchi, A. La Torre, and A. Arcangeli Irresponsiveness of two retinoblastoma cases to conservative therapy correlates with up- regulation of hERG1 channels and of the VEGF-A pathway BMC Cancer 10 2010 504
    • (2010) BMC Cancer , vol.10 , pp. 504
    • Fortunato, P.1    Pillozzi, S.2    Tamburini, A.3    Pollazzi, L.4    Franchi, A.5    La Torre, A.6    Arcangeli, A.7
  • 40
    • 84880263145 scopus 로고    scopus 로고
    • Inhibition of VEGF expression through blockade of Hif1alpha and STAT3 signalling mediates the anti-angiogenic effect of melatonin in HepG2 liver cancer cells
    • S. Carbajo-Pescador, R. Ordonez, M. Benet, R. Jover, A. Garcia-Palomo, J.L. Mauriz, and J. Gonzalez-Gallego Inhibition of VEGF expression through blockade of Hif1alpha and STAT3 signalling mediates the anti-angiogenic effect of melatonin in HepG2 liver cancer cells Br. J. Cancer 109 2013 83 91
    • (2013) Br. J. Cancer , vol.109 , pp. 83-91
    • Carbajo-Pescador, S.1    Ordonez, R.2    Benet, M.3    Jover, R.4    Garcia-Palomo, A.5    Mauriz, J.L.6    Gonzalez-Gallego, J.7
  • 42
    • 84864088681 scopus 로고    scopus 로고
    • Osteoblast-specific transcription factor Osterix (Osx) and HIF-1alpha cooperatively regulate gene expression of vascular endothelial growth factor (VEGF)
    • D. Chen, W. Tian, Y. Li, W. Tang, and C. Zhang Osteoblast-specific transcription factor Osterix (Osx) and HIF-1alpha cooperatively regulate gene expression of vascular endothelial growth factor (VEGF) Biochem. Biophys. Res. Commun. 424 2012 176 181
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 176-181
    • Chen, D.1    Tian, W.2    Li, Y.3    Tang, W.4    Zhang, C.5
  • 44
    • 84884167082 scopus 로고    scopus 로고
    • Feedback regulation of telomerase reverse transcriptase: New insight into the evolving field of telomerase in cancer
    • X.Q. Wu, C. Huang, X. He, Y.Y. Tian, D.X. Zhou, Y. He, X.H. Liu, and J. Li Feedback regulation of telomerase reverse transcriptase: new insight into the evolving field of telomerase in cancer Cell. Signal 25 2013 2462 2468
    • (2013) Cell. Signal , vol.25 , pp. 2462-2468
    • Wu, X.Q.1    Huang, C.2    He, X.3    Tian, Y.Y.4    Zhou, D.X.5    He, Y.6    Liu, X.H.7    Li, J.8
  • 45
    • 0034731522 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces expression of connective tissue growth factor via KDR, Flt1, and phosphatidylinositol 3-kinase-akt-dependent pathways in retinal vascular cells
    • K. Suzuma, K. Naruse, I. Suzuma, N. Takahara, K. Ueki, L.P. Aiello, and G.L. King Vascular endothelial growth factor induces expression of connective tissue growth factor via KDR, Flt1, and phosphatidylinositol 3-kinase-akt-dependent pathways in retinal vascular cells J. Biol. Chem. 275 2000 40725 40731
    • (2000) J. Biol. Chem. , vol.275 , pp. 40725-40731
    • Suzuma, K.1    Naruse, K.2    Suzuma, I.3    Takahara, N.4    Ueki, K.5    Aiello, L.P.6    King, G.L.7
  • 46
    • 43249095919 scopus 로고    scopus 로고
    • Tumor angiogenesis
    • R.S. Kerbel Tumor angiogenesis N. Engl. J. Med. 358 2008 2039 2049
    • (2008) N. Engl. J. Med. , vol.358 , pp. 2039-2049
    • Kerbel, R.S.1
  • 48
    • 84855661853 scopus 로고    scopus 로고
    • Activation of PI3 kinase/Akt/HIF-1alpha pathway contributes to hypoxia-induced epithelial-mesenchymal transition and chemoresistance in hepatocellular carcinoma
    • M. Jiao, and K.J. Nan Activation of PI3 kinase/Akt/HIF-1alpha pathway contributes to hypoxia-induced epithelial-mesenchymal transition and chemoresistance in hepatocellular carcinoma Int. J. Oncol. 40 2012 461 468
    • (2012) Int. J. Oncol. , vol.40 , pp. 461-468
    • Jiao, M.1    Nan, K.J.2
  • 49
    • 84888867015 scopus 로고    scopus 로고
    • Ascofuranone suppresses EGF-induced HIF-1alpha protein synthesis by inhibition of the Akt/mTOR/p70S6K pathway in MDA-MB-231 breast cancer cells
    • Y.J. Jeong, H.J. Cho, J. Magae, I.K. Lee, K.G. Park, and Y.C. Chang Ascofuranone suppresses EGF-induced HIF-1alpha protein synthesis by inhibition of the Akt/mTOR/p70S6K pathway in MDA-MB-231 breast cancer cells Toxicol. Appl. Pharmacol. 273 2013 542 550
    • (2013) Toxicol. Appl. Pharmacol. , vol.273 , pp. 542-550
    • Jeong, Y.J.1    Cho, H.J.2    Magae, J.3    Lee, I.K.4    Park, K.G.5    Chang, Y.C.6
  • 50
    • 0035860246 scopus 로고    scopus 로고
    • MAPK and Akt act cooperatively but independently on hypoxia inducible factor-1alpha in rasV12 upregulation of VEGF
    • A. Sodhi, S. Montaner, H. Miyazaki, and J.S. Gutkind MAPK and Akt act cooperatively but independently on hypoxia inducible factor-1alpha in rasV12 upregulation of VEGF Biochem. Biophys. Res. Commun. 287 2001 292 300
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 292-300
    • Sodhi, A.1    Montaner, S.2    Miyazaki, H.3    Gutkind, J.S.4
  • 51
    • 84903562286 scopus 로고    scopus 로고
    • A framework to examine the role of epigenetics in health disparities among native Americans
    • T.N. Brockie, M. Heinzelmann, and J. Gill A framework to examine the role of epigenetics in health disparities among native Americans Nurs. Res. Pract. 2013 2013 410395
    • (2013) Nurs. Res. Pract. , vol.2013 , pp. 410395
    • Brockie, T.N.1    Heinzelmann, M.2    Gill, J.3
  • 52
    • 84886234157 scopus 로고    scopus 로고
    • Epigenetic mechanisms of neurodegeneration in Huntington's disease
    • J. Lee, Y.J. Hwang, K.Y. Kim, N.W. Kowall, and H. Ryu Epigenetic mechanisms of neurodegeneration in Huntington's disease Neurotherapeutics 10 2013 664 676
    • (2013) Neurotherapeutics , vol.10 , pp. 664-676
    • Lee, J.1    Hwang, Y.J.2    Kim, K.Y.3    Kowall, N.W.4    Ryu, H.5
  • 53
    • 79251576774 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: The epigenetic therapeutics that repress hypoxia-inducible factors
    • S. Chen, and N. Sang Histone deacetylase inhibitors: the epigenetic therapeutics that repress hypoxia-inducible factors J. Biomed. Biotechnol. 2011 2011 197946
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 197946
    • Chen, S.1    Sang, N.2
  • 55
    • 84864011802 scopus 로고    scopus 로고
    • MicroRNA-146a modulates TGF-beta1-induced hepatic stellate cell proliferation by targeting SMAD4
    • Y. He, C. Huang, X. Sun, X.R. Long, X.W. Lv, and J. Li MicroRNA-146a modulates TGF-beta1-induced hepatic stellate cell proliferation by targeting SMAD4 Cell. Signal 24 2012 1923 1930
    • (2012) Cell. Signal , vol.24 , pp. 1923-1930
    • He, Y.1    Huang, C.2    Sun, X.3    Long, X.R.4    Lv, X.W.5    Li, J.6
  • 56
    • 0036544755 scopus 로고    scopus 로고
    • Micro RNAs are complementary to 3′ UTR sequence motifs that mediate negative post-transcriptional regulation
    • E.C. Lai Micro RNAs are complementary to 3′ UTR sequence motifs that mediate negative post-transcriptional regulation Nat. Genet. 30 2002 363 364
    • (2002) Nat. Genet. , vol.30 , pp. 363-364
    • Lai, E.C.1
  • 57
    • 77952160818 scopus 로고    scopus 로고
    • MicroRNA-101 negatively regulates Ezh2 and its expression is modulated by androgen receptor and HIF-1alpha/HIF-1beta
    • P. Cao, Z. Deng, M. Wan, W. Huang, S.D. Cramer, J. Xu, M. Lei, and G. Sui MicroRNA-101 negatively regulates Ezh2 and its expression is modulated by androgen receptor and HIF-1alpha/HIF-1beta Mol. Cancer 9 2010 108
    • (2010) Mol. Cancer , vol.9 , pp. 108
    • Cao, P.1    Deng, Z.2    Wan, M.3    Huang, W.4    Cramer, S.D.5    Xu, J.6    Lei, M.7    Sui, G.8
  • 59
    • 70449602451 scopus 로고    scopus 로고
    • Regulation of HIF-1alpha and VEGF by miR-20b tunes tumor cells to adapt to the alteration of oxygen concentration
    • Z. Lei, B. Li, Z. Yang, H. Fang, G.M. Zhang, Z.H. Feng, and B. Huang Regulation of HIF-1alpha and VEGF by miR-20b tunes tumor cells to adapt to the alteration of oxygen concentration PLoS One 4 2009 e7629
    • (2009) PLoS One , vol.4 , pp. 7629
    • Lei, Z.1    Li, B.2    Yang, Z.3    Fang, H.4    Zhang, G.M.5    Feng, Z.H.6    Huang, B.7
  • 60
    • 48649102010 scopus 로고    scopus 로고
    • Identification of hypoxia-inducible factor-1 alpha as a novel target for miR-17-92 microRNA cluster
    • A. Taguchi, K. Yanagisawa, M. Tanaka, K. Cao, Y. Matsuyama, H. Goto, and T. Takahashi Identification of hypoxia-inducible factor-1 alpha as a novel target for miR-17-92 microRNA cluster Cancer Res. 68 2008 5540 5545
    • (2008) Cancer Res. , vol.68 , pp. 5540-5545
    • Taguchi, A.1    Yanagisawa, K.2    Tanaka, M.3    Cao, K.4    Matsuyama, Y.5    Goto, H.6    Takahashi, T.7
  • 62
    • 84862026516 scopus 로고    scopus 로고
    • Regulatory effects of microRNA-92 (miR-92) on VHL gene expression and the hypoxic activation of miR-210 in clear cell renal cell carcinoma
    • V.A. Valera, B.A. Walter, W.M. Linehan, and M.J. Merino Regulatory effects of microRNA-92 (miR-92) on VHL gene expression and the hypoxic activation of miR-210 in clear cell renal cell carcinoma J. Cancer 2 2011 515 526
    • (2011) J. Cancer , vol.2 , pp. 515-526
    • Valera, V.A.1    Walter, B.A.2    Linehan, W.M.3    Merino, M.J.4
  • 63
    • 0022540321 scopus 로고
    • CpG-rich islands and the function of DNA methylation
    • A.P. Bird CpG-rich islands and the function of DNA methylation Nature 321 1986 209 213
    • (1986) Nature , vol.321 , pp. 209-213
    • Bird, A.P.1
  • 65
    • 79951810386 scopus 로고    scopus 로고
    • Tumor-associated CpG demethylation augments hypoxia-induced effects by positive autoregulation of HIF-1alpha
    • M. Koslowski, U. Luxemburger, O. Tureci, and U. Sahin Tumor-associated CpG demethylation augments hypoxia-induced effects by positive autoregulation of HIF-1alpha Oncogene 30 2011 876 882
    • (2011) Oncogene , vol.30 , pp. 876-882
    • Koslowski, M.1    Luxemburger, U.2    Tureci, O.3    Sahin, U.4
  • 67
    • 84892375525 scopus 로고    scopus 로고
    • Identification and interrogation of combinatorial histone modifications
    • K.R. Karch, J.E. Denizio, B.E. Black, and B.A. Garcia Identification and interrogation of combinatorial histone modifications Front. Genet. 4 2013 264
    • (2013) Front. Genet. , vol.4 , pp. 264
    • Karch, K.R.1    Denizio, J.E.2    Black, B.E.3    Garcia, B.A.4
  • 68
    • 40649114443 scopus 로고    scopus 로고
    • Hypoxia induces a novel signature of chromatin modifications and global repression of transcription
    • A.B. Johnson, N. Denko, and M.C. Barton Hypoxia induces a novel signature of chromatin modifications and global repression of transcription Mutat. Res. 640 2008 174 179
    • (2008) Mutat. Res. , vol.640 , pp. 174-179
    • Johnson, A.B.1    Denko, N.2    Barton, M.C.3
  • 71
    • 79960785531 scopus 로고    scopus 로고
    • Epigenetics: New questions on the response to hypoxia
    • J.I. Perez-Perri, J.M. Acevedo, and P. Wappner Epigenetics: new questions on the response to hypoxia Int. J. Mol. Sci. 12 2011 4705 4721
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 4705-4721
    • Perez-Perri, J.I.1    Acevedo, J.M.2    Wappner, P.3
  • 72
    • 77954661616 scopus 로고    scopus 로고
    • Epigenetics, the epicenter of the hypoxic response
    • J.A. Watson, C.J. Watson, A. McCann, and J. Baugh Epigenetics, the epicenter of the hypoxic response Epigenetics 5 2010 293 296
    • (2010) Epigenetics , vol.5 , pp. 293-296
    • Watson, J.A.1    Watson, C.J.2    McCann, A.3    Baugh, J.4
  • 74
  • 75
    • 84878391134 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor beta1/Smad3 signaling decreases hypoxia-inducible factor-1alpha protein stability by inducing prolyl hydroxylase 2 expression in human periodontal ligament cells
    • T. Watanabe, A. Yasue, and E. Tanaka Inhibition of transforming growth factor beta1/Smad3 signaling decreases hypoxia-inducible factor-1alpha protein stability by inducing prolyl hydroxylase 2 expression in human periodontal ligament cells J. Periodontol. 84 2013 1346 1352
    • (2013) J. Periodontol. , vol.84 , pp. 1346-1352
    • Watanabe, T.1    Yasue, A.2    Tanaka, E.3
  • 76
    • 84884215604 scopus 로고    scopus 로고
    • Expression and significance of HIF-1alpha in pulmonary fibrosis induced by paraquat
    • H. Xie, J.T. Tan, R.L. Wang, X.X. Meng, X. Tang, and S. Gao Expression and significance of HIF-1alpha in pulmonary fibrosis induced by paraquat Exp. Biol. Med. Maywood 238 2013 1062 1068
    • (2013) Exp. Biol. Med. Maywood , vol.238 , pp. 1062-1068
    • Xie, H.1    Tan, J.T.2    Wang, R.L.3    Meng, X.X.4    Tang, X.5    Gao, S.6
  • 79
    • 84886780221 scopus 로고    scopus 로고
    • Transcriptional upregulation of HIF-1alpha by NF-kappaB/p65 and its associations with beta-catenin/p300 complexes in endometrial carcinoma cells
    • T. Yoshida, M. Hashimura, T. Mastumoto, Y. Tazo, H. Inoue, T. Kuwata, and M. Saegusa Transcriptional upregulation of HIF-1alpha by NF-kappaB/p65 and its associations with beta-catenin/p300 complexes in endometrial carcinoma cells Lab. Invest. 93 2013 1184 1193
    • (2013) Lab. Invest. , vol.93 , pp. 1184-1193
    • Yoshida, T.1    Hashimura, M.2    Mastumoto, T.3    Tazo, Y.4    Inoue, H.5    Kuwata, T.6    Saegusa, M.7
  • 80
    • 84885045030 scopus 로고    scopus 로고
    • Involvement of the HIF-1alpha and Wnt/beta-catenin pathways in the protective effects of losartan on fatty liver graft with ischaemia/reperfusion injury
    • Y.Y. Yang, P.C. Lee, Y.T. Huang, W.P. Lee, Y.J. Kuo, K.C. Lee, Y.C. Hsieh, T.Y. Lee, and H.C. Lin Involvement of the HIF-1alpha and Wnt/beta-catenin pathways in the protective effects of losartan on fatty liver graft with ischaemia/reperfusion injury Clin. Sci. Lond 126 2014 163 174
    • (2014) Clin. Sci. Lond , vol.126 , pp. 163-174
    • Yang, Y.Y.1    Lee, P.C.2    Huang, Y.T.3    Lee, W.P.4    Kuo, Y.J.5    Lee, K.C.6    Hsieh, Y.C.7    Lee, T.Y.8    Lin, H.C.9
  • 81
    • 1242271198 scopus 로고    scopus 로고
    • Topoisomerase I-mediated inhibition of hypoxia-inducible factor 1: Mechanism and therapeutic implications
    • A. Rapisarda, B. Uranchimeg, O. Sordet, Y. Pommier, R.H. Shoemaker, and G. Melillo Topoisomerase I-mediated inhibition of hypoxia-inducible factor 1: mechanism and therapeutic implications Cancer Res. 64 2004 1475 1482
    • (2004) Cancer Res. , vol.64 , pp. 1475-1482
    • Rapisarda, A.1    Uranchimeg, B.2    Sordet, O.3    Pommier, Y.4    Shoemaker, R.H.5    Melillo, G.6
  • 83
  • 84
    • 84863241726 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha inhibition by a pyrrolopyrazine metabolite of oltipraz as a consequence of microRNAs 199a-5p and 20a induction
    • S.G. Kang, W.H. Lee, Y.H. Lee, Y.S. Lee, and S.G. Kim Hypoxia-inducible factor-1alpha inhibition by a pyrrolopyrazine metabolite of oltipraz as a consequence of microRNAs 199a-5p and 20a induction Carcinogenesis 33 2012 661 669
    • (2012) Carcinogenesis , vol.33 , pp. 661-669
    • Kang, S.G.1    Lee, W.H.2    Lee, Y.H.3    Lee, Y.S.4    Kim, S.G.5


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