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Volumn 35, Issue 4, 2003, Pages 331-340

Multiple organ pathology, metabolic abnormalities and impaired homeostasis of reactive oxygen species in Epas1-/- mice

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL PAS DOMAIN PROTEIN 1; HYPOXIA INDUCIBLE FACTOR 2ALPHA; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0344826529     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1266     Document Type: Article
Times cited : (425)

References (50)
  • 1
    • 0034901463 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Oxygen homeostasis and disease pathophysiology
    • Semenza, G.L. Hypoxia-inducible factor 1: oxygen homeostasis and disease pathophysiology. Trends Mol. Med. 7, 345-350 (2001).
    • (2001) Trends Mol. Med. , vol.7 , pp. 345-350
    • Semenza, G.L.1
  • 3
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian, H., McKnight, S.L. & Russell, D.W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11, 72-82 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 4
    • 0034681378 scopus 로고    scopus 로고
    • A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1α and the HIF-like factor
    • Lando, D., Pongratz, I., Poellinger, L. & Whitelaw, M.L. A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1α and the HIF-like factor. J. Biol. Chem. 275, 4618-4627 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4618-4627
    • Lando, D.1    Pongratz, I.2    Poellinger, L.3    Whitelaw, M.L.4
  • 5
    • 0032478823 scopus 로고    scopus 로고
    • Selection and analysis of a mutant cell line defective in the hypoxia-inducible factor-1 α-subunit (HIF-1α). Characterization of hif-1α-dependent and -independent hypoxia-inducible gene expression
    • Wood, S.M. et al. Selection and analysis of a mutant cell line defective in the hypoxia-inducible factor-1 α-subunit (HIF-1α). Characterization of hif-1α-dependent and - independent hypoxia-inducible gene expression. J. Biol. Chem. 273, 8360-8368 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8360-8368
    • Wood, S.M.1
  • 6
    • 0033593219 scopus 로고    scopus 로고
    • Oxygen-regulated and transactivating domains in endothelial PAS protein 1: Comparison with hypoxia-inducible factor-1α
    • O'Rourke, J.F., Tian, Y.M., Ratcliffe, P.J. & Pugh, C.W. Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1α. J. Biol. Chem. 274, 2060-2071 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2060-2071
    • O'Rourke, J.F.1    Tian, Y.M.2    Ratcliffe, P.J.3    Pugh, C.W.4
  • 7
    • 0031971047 scopus 로고    scopus 로고
    • Expression of ARNT, ARNT2, HIFα, HIF2α and An receptor mRNAs in the developing mouse
    • Jain, S., Maltepe, E., Lu, M.M., Simon, C. & Bradfield, C.A. Expression of ARNT, ARNT2, HIFα, HIF2α and An receptor mRNAs in the developing mouse. Mech. Dev. 73, 117-123 (1998).
    • (1998) Mech. Dev. , vol.73 , pp. 117-123
    • Jain, S.1    Maltepe, E.2    Lu, M.M.3    Simon, C.4    Bradfield, C.A.5
  • 8
    • 15444342958 scopus 로고    scopus 로고
    • 2 homeostasis by hypoxia-inducible factor 1α
    • 2 homeostasis by hypoxia-inducible factor 1α. Genes Dev. 12, 149-162 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 149-162
    • Iyer, N.V.1
  • 9
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1α is required for solid tumor formation and embryonic vascularization
    • Ryan, H.E., Lo, J. & Johnson, R.S. HIF-1α is required for solid tumor formation and embryonic vascularization. EMBO J. 17, 3005-3015 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 10
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian, H., Hammer, R.E., Matsumoto, A.M., Russell, D.W. & McKnight, S.L. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 12, 3320-3324 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 11
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS-1/hypoxia-inducible factor 2α plays an important role in vascular remodeling
    • Peng, J., Zhang, L., Drysdale, L. & Fong, G.H. The transcription factor EPAS-1/hypoxia-inducible factor 2α plays an important role in vascular remodeling. Proc. Natl. Acad. Sci. USA 97, 8386-8391 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 12
    • 0041440036 scopus 로고    scopus 로고
    • The HIF family member EPAS1/HIF-2α is required for normal hematopoiesis in mice
    • Scortegagna, M., Morris, M.A., Oktay, Y., Bennett, M. & Garcia, J.A. The HIF family member EPAS1/HIF-2α is required for normal hematopoiesis in mice. Blood 102, 1634-1640 (2003).
    • (2003) Blood , vol.102 , pp. 1634-1640
    • Scortegagna, M.1    Morris, M.A.2    Oktay, Y.3    Bennett, M.4    Garcia, J.A.5
  • 13
    • 0028936222 scopus 로고
    • Ragged red fibers in normal aging and inflammatory myopathy
    • Rifai, Z., Welle, S., Kamp, C. & Thornton, C.A. Ragged red fibers in normal aging and inflammatory myopathy. Ann. Neurol. 37, 24-29 (1995).
    • (1995) Ann. Neurol. , vol.37 , pp. 24-29
    • Rifai, Z.1    Welle, S.2    Kamp, C.3    Thornton, C.A.4
  • 14
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D.C. Mitochondrial diseases in man and mouse. Science 283, 1482-1488 (1999).
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 15
    • 0036119297 scopus 로고    scopus 로고
    • Measurement of superoxide radical and hydrogen peroxide production in isolated cells and subcellular organelles
    • Boveris, A., Alvarez, S., Bustamante, J. & Valdez, L. Measurement of superoxide radical and hydrogen peroxide production in isolated cells and subcellular organelles. Methods Enzymol. 349, 280-287 (2002).
    • (2002) Methods Enzymol. , vol.349 , pp. 280-287
    • Boveris, A.1    Alvarez, S.2    Bustamante, J.3    Valdez, L.4
  • 17
    • 0033517717 scopus 로고    scopus 로고
    • Transcriptional induction of metallothionein-I and -II genes in the livers of Cu,Zn-superoxide dismutase knockout mice
    • Ghoshal, K., Majumder, S., Li, Z., Bray, T.M. & Jacob, S.T. Transcriptional induction of metallothionein-I and -II genes in the livers of Cu,Zn-superoxide dismutase knockout mice. Biochem. Biophys. Res. Commun. 264, 735-742 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 735-742
    • Ghoshal, K.1    Majumder, S.2    Li, Z.3    Bray, T.M.4    Jacob, S.T.5
  • 19
    • 0035827635 scopus 로고    scopus 로고
    • Tumor necrosis factor-α selectively induces MnSOD expression via mitochordria-to-nucleus signaling, whereas interleukin-1β utilizes an alternative pathway
    • Rogers, R.J., Monnier, J.M. & Nick, H.S. Tumor necrosis factor-α selectively induces MnSOD expression via mitochordria-to-nucleus signaling, whereas interleukin-1β utilizes an alternative pathway. J. Biol. Chem. 276, 20419-20427 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20419-20427
    • Rogers, R.J.1    Monnier, J.M.2    Nick, H.S.3
  • 20
    • 0032171622 scopus 로고    scopus 로고
    • Peroxynitrite modulates MnSOD gene expression in lung epithelial cells
    • Jackson, R.M., Parish, G. & Helton, E.S. Peroxynitrite modulates MnSOD gene expression in lung epithelial cells. Free Radic. Biol. Med. 25, 463-472 (1998).
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 463-472
    • Jackson, R.M.1    Parish, G.2    Helton, E.S.3
  • 21
    • 0029123437 scopus 로고
    • Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1
    • Wang, G.L., Jiang, B.H. & Semenza, G.L. Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 212, 550-556 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 550-556
    • Wang, G.L.1    Jiang, B.H.2    Semenza, G.L.3
  • 22
    • 0031940986 scopus 로고    scopus 로고
    • A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase
    • Melov, S. et al. A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat. Genet. 18, 159-163 (1998).
    • (1998) Nat. Genet. , vol.18 , pp. 159-163
    • Melov, S.1
  • 23
    • 0035500460 scopus 로고    scopus 로고
    • Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice
    • Huang, T.-T. et al. Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice. Free Radic. Biol. Med. 31, 1101-1110 (2001).
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1101-1110
    • Huang, T.-T.1
  • 24
    • 0025859044 scopus 로고
    • A quantitative genetic analysis of tissue-specific catalase activity in Mus musculus
    • Schisler, N.J. & Singh, S.M. A quantitative genetic analysis of tissue-specific catalase activity in Mus musculus. Biochem. Genet. 29, 65-89 (1991).
    • (1991) Biochem. Genet. , vol.29 , pp. 65-89
    • Schisler, N.J.1    Singh, S.M.2
  • 25
    • 0021876079 scopus 로고
    • Tissue-specific developmental regulation of superoxide dismutase (SOD-1 and SOD-2) activities in genetic strains of mice
    • Schisler, N.J. & Singh, S.M. Tissue-specific developmental regulation of superoxide dismutase (SOD-1 and SOD-2) activities in genetic strains of mice. Biochem. Genet. 23, 291-308 (1985).
    • (1985) Biochem. Genet. , vol.23 , pp. 291-308
    • Schisler, N.J.1    Singh, S.M.2
  • 26
    • 0032533922 scopus 로고    scopus 로고
    • Characterization of the murine gene encoding Aop2 (antioxidant protein 2) and identification of two highly related genes
    • Phelan, S.A., Johnson, K.A., Beier, D.R. & Paigen, B. Characterization of the murine gene encoding Aop2 (antioxidant protein 2) and identification of two highly related genes. Genomics 54, 132-139 (1998).
    • (1998) Genomics , vol.54 , pp. 132-139
    • Phelan, S.A.1    Johnson, K.A.2    Beier, D.R.3    Paigen, B.4
  • 27
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro, S. & Schon, E.A. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 348, 2656-2668 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 28
    • 0028325389 scopus 로고
    • Primary defect of juvenile visceral steatosis (jvs) mouse with systemic carnitine deficiency is probably in renal carnitine transport system
    • Horiuchi, M. et al. Primary defect of juvenile visceral steatosis (jvs) mouse with systemic carnitine deficiency is probably in renal carnitine transport system. Biochim. Biophys. Acta 1226, 25-30 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1226 , pp. 25-30
    • Horiuchi, M.1
  • 29
    • 0029049928 scopus 로고
    • Mitochondrial abnormalities of muscle tissue in mice with juvenile visceral steatosis associated with systemic carnitine deficiency
    • Miyagawa, J. et al. Mitochondrial abnormalities of muscle tissue in mice with juvenile visceral steatosis associated with systemic carnitine deficiency. Virchows Arch. 426, 271-279 (1995).
    • (1995) Virchows Arch. , vol.426 , pp. 271-279
    • Miyagawa, J.1
  • 30
    • 0030682077 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in a murine model of primary carnitine deficiency. Systemic pathology and trial of replacement therapy
    • Kaido, M. et al. Mitochondrial abnormalities in a murine model of primary carnitine deficiency. Systemic pathology and trial of replacement therapy. Eur. Neurol. 38, 302-309 (1997).
    • (1997) Eur. Neurol. , vol.38 , pp. 302-309
    • Kaido, M.1
  • 31
    • 0035682982 scopus 로고    scopus 로고
    • Antioxidant changes in the hypertrophied heart due to energy metabolic disorder
    • Kamiya, H. et al. Antioxidant changes in the hypertrophied heart due to energy metabolic disorder. Basic Res. Cardiol. 96, 431-438 (2001).
    • (2001) Basic Res. Cardiol. , vol.96 , pp. 431-438
    • Kamiya, H.1
  • 32
    • 0031011211 scopus 로고    scopus 로고
    • A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator
    • Graham, B.H. et al. A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator. Nat. Genet. 16, 226-234 (1997).
    • (1997) Nat. Genet. , vol.16 , pp. 226-234
    • Graham, B.H.1
  • 34
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Li, Y. et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 11, 376-381 (1995).
    • (1995) Nat. Genet. , vol.11 , pp. 376-381
    • Li, Y.1
  • 35
    • 0029838063 scopus 로고    scopus 로고
    • Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
    • Lebovitz, R.M. et al. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc. Natl. Acad. Sci. USA 93, 9782-9787 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9782-9787
    • Lebovitz, R.M.1
  • 36
    • 0035896748 scopus 로고    scopus 로고
    • Absence of mitochondrial superoxide dismutase results in a murine hemolytic anemia responsive to therapy with a catalytic antioxidant
    • Friedman, J.S. et al. Absence of mitochondrial superoxide dismutase results in a murine hemolytic anemia responsive to therapy with a catalytic antioxidant. J. Exp. Med. 193, 925-934 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 925-934
    • Friedman, J.S.1
  • 37
    • 0032561328 scopus 로고    scopus 로고
    • Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
    • Williams, M.D. et al. Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J. Biol. Chem. 273, 28510-28515 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28510-28515
    • Williams, M.D.1
  • 38
  • 39
    • 0033499889 scopus 로고    scopus 로고
    • Peroxynitrite inactivation of tyrosine hydroxylase: Mediation by sulfhydryl oxidation, not tyrosine nitration
    • Kuhn, D.M., Aretha, C.W. & Geddes, T.J. Peroxynitrite inactivation of tyrosine hydroxylase: mediation by sulfhydryl oxidation, not tyrosine nitration. J. Neurosci. 19, 10289-10294 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 10289-10294
    • Kuhn, D.M.1    Aretha, C.W.2    Geddes, T.J.3
  • 40
    • 0028834228 scopus 로고
    • Peroxynitrite-mediated inhibition of DOPA synthesis in PC 12 cells
    • Ischiropoulos, H., Duran, D. & Horwitz, J. Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells. J. Neurochem. 65, 2366-2372 (1995).
    • (1995) J. Neurochem. , vol.65 , pp. 2366-2372
    • Ischiropoulos, H.1    Duran, D.2    Horwitz, J.3
  • 41
    • 0031042677 scopus 로고    scopus 로고
    • Dopamine- and L-β-3,4-dihydroxyphenylalanine hydrochloride (L-Dopa)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY 5Y cells. Effects of oxidative stress and antioxidative factors
    • Lai, C.T. & Yu, P.H. Dopamine- and L-β -3,4-dihydroxyphenylalanine hydrochloride (L-Dopa)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY5Y cells. Effects of oxidative stress and antioxidative factors. Biochem. Pharmacol. 53, 363-372 (1997).
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 363-372
    • Lai, C.T.1    Yu, P.H.2
  • 42
    • 0036838636 scopus 로고    scopus 로고
    • Hyperglycemic switch from mitochondrial nitric oxide to superoxide production in endothelial cells
    • Brodsky, S.V., Gao, S., Li, H. & Goligorsky, M.S. Hyperglycemic switch from mitochondrial nitric oxide to superoxide production in endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 283, H2130-H2139 (2002).
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Brodsky, S.V.1    Gao, S.2    Li, H.3    Goligorsky, M.S.4
  • 43
    • 0037907756 scopus 로고    scopus 로고
    • Haem oxygenase 1 gene induction by glucose deprivation is mediated by reactive oxygen species via the mitochondrial electron-transport chain
    • Chang, S.H., Garcia, J., Melendez, J.A., Kilberg, M.S. & Agarwal, A. Haem oxygenase 1 gene induction by glucose deprivation is mediated by reactive oxygen species via the mitochondrial electron-transport chain. Biochem. J. 371, 877-885 (2003).
    • (2003) Biochem. J. , vol.371 , pp. 877-885
    • Chang, S.H.1    Garcia, J.2    Melendez, J.A.3    Kilberg, M.S.4    Agarwal, A.5
  • 44
    • 0030612345 scopus 로고    scopus 로고
    • Lactate and PO2 modulate superoxide anion production in bovine cardiac myocytes: Potential role of NADH oxidase
    • Mohazzab, H.K., Kaminski, P.M. & Wolin, M.S. Lactate and PO2 modulate superoxide anion production in bovine cardiac myocytes: potential role of NADH oxidase. Circulation 96, 614-620 (1997).
    • (1997) Circulation , vol.96 , pp. 614-620
    • Mohazzab, H.K.1    Kaminski, P.M.2    Wolin, M.S.3
  • 45
    • 0037189542 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis
    • Lu, H., Forbes, R.A. & Verma, A. Hypoxia-inducible factor 1 activation by aerobic glycolysis implicates the Warburg effect in carcinogenesis. J. Biol. Chem. 277, 23111-23115 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 23111-23115
    • Lu, H.1    Forbes, R.A.2    Verma, A.3
  • 46
    • 0033159721 scopus 로고    scopus 로고
    • Hypoxic modulation of manganese superoxide dismutase promoter activity and gene expression in lung epithelial cells
    • Ohman, T., Parish, G. & Jackson, R.M. Hypoxic modulation of manganese superoxide dismutase promoter activity and gene expression in lung epithelial cells. Am. J. Respir. Cell Mol. Biol. 21, 119-127 (1999).
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.21 , pp. 119-127
    • Ohman, T.1    Parish, G.2    Jackson, R.M.3
  • 47
    • 0036122920 scopus 로고    scopus 로고
    • Transcription regulation of human manganese superoxide dismutase gene
    • St Clair, D.K., Porntadavity, S., Xu, Y. & Kiningham, K. Transcription regulation of human manganese superoxide dismutase gene. Methods Enzymol. 349, 306-312 (2002).
    • (2002) Methods Enzymol. , vol.349 , pp. 306-312
    • St. Clair, D.K.1    Porntadavity, S.2    Xu, Y.3    Kiningham, K.4
  • 49
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B.L. & Zhulin, I.B. PAS domains: internal sensors of oxygen, redox potential, and light. Microbio. Mol. Biol. Rev. 63, 479-506 (1999).
    • (1999) Microbio. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 50
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn, H.F. & Poyton, R.O. Oxygen sensing and molecular adaptation to hypoxia. Physiol. Rev. 76, 839-885 (1996).
    • (1996) Physiol. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2


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