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Volumn 274, Issue 1 43-1, 1998, Pages

Role of H2O2 and heme-containing O2 sensors in hypoxic regulation of tyrosine hydroxylase gene expression

Author keywords

Carotid body; Catecholamines; Chemoreceptors; Dopamine; Oxygen dependent regulation; Pheochromocytoma

Indexed keywords

BUCILLAMINE; CATECHOLAMINE; DEFEROXAMINE; FLUORESCEIN; HYDROGEN PEROXIDE; MESSENGER RNA; TYROSINE DECARBOXYLASE; ACETYLCYSTEINE; ACTIN; AMITROLE; ANTIOXIDANT; CATALASE; HEME; OXYGEN; TIOPRONIN; TYROSINE 3 MONOOXYGENASE;

EID: 0031600968     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.274.1.c167     Document Type: Article
Times cited : (73)

References (44)
  • 1
    • 0028137580 scopus 로고
    • Mechanisms and meaning of cellular oxygen sensing in the organism
    • Acker, H. Mechanisms and meaning of cellular oxygen sensing in the organism. Respir. Physiol. 95: 1-10, 1994.
    • (1994) Respir. Physiol. , vol.95 , pp. 1-10
    • Acker, H.1
  • 4
    • 0024394697 scopus 로고
    • The antioxidant action of N-acetylcysteine: Its reaction with hydrogen peroxide, hydroxyradical, superoxide, and hypochlorous acid
    • Aruoma, O. I., B. Halliwell, B. M. Hoey, and J. Butler. The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyradical, superoxide, and hypochlorous acid. Free Radic. Biol. Med. 6: 593-597, 1989.
    • (1989) Free Radic. Biol. Med. , vol.6 , pp. 593-597
    • Aruoma, O.I.1    Halliwell, B.2    Hoey, B.M.3    Butler, J.4
  • 5
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., J. B. Davis, R. Lesley, and D. Schubert. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77: 817-827, 1994.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 6
    • 0021027358 scopus 로고
    • Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay
    • Cathcart, R., E. Schwiers, and B. N. Ames. Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Anal. Biochem. 134: 111-116, 1983.
    • (1983) Anal. Biochem. , vol.134 , pp. 111-116
    • Cathcart, R.1    Schwiers, E.2    Ames, B.N.3
  • 7
    • 0030932662 scopus 로고    scopus 로고
    • Long-term exposure to ozone alters peripheral and central catecholamine activity in rats
    • Cottet-Emard, J.-M., Y. Dalmaz, J. Pequignot, L. Peyrin, and J.-M. Pequinot. Long-term exposure to ozone alters peripheral and central catecholamine activity in rats. Pflügers Arch. 433: 744-749, 1997.
    • (1997) Pflügers Arch. , vol.433 , pp. 744-749
    • Cottet-Emard, J.-M.1    Dalmaz, Y.2    Pequignot, J.3    Peyrin, L.4    Pequinot, J.-M.5
  • 9
    • 0030690459 scopus 로고    scopus 로고
    • Molecular aspects of oxygen sensing in physiological adaptation to hypoxia
    • In press
    • Czyzyk-Krzeska, M. F. Molecular aspects of oxygen sensing in physiological adaptation to hypoxia. Resp. Physiol. In press.
    • Resp. Physiol.
    • Czyzyk-Krzeska, M.F.1
  • 10
    • 0026577610 scopus 로고
    • Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia
    • Czyzyk-Krzeska, M. F., D. A. Bayliss, E. E. Lawson, and D. E. Millhorn. Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia. J. Neurochem. 58: 1538-1546, 1992.
    • (1992) J. Neurochem. , vol.58 , pp. 1538-1546
    • Czyzyk-Krzeska, M.F.1    Bayliss, D.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 11
    • 0030020622 scopus 로고    scopus 로고
    • Characterization of the hypoxia inducible protein binding site within the pyrimidine rich tract in the 3′-untranslated region of the tyrosine hydroxylase mRNA
    • Czyzyk-Krzeska, M. F., and J. E. Beresh. Characterization of the hypoxia inducible protein binding site within the pyrimidine rich tract in the 3′-untranslated region of the tyrosine hydroxylase mRNA. J. Biol. Chem. 271: 3293-3299, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3293-3299
    • Czyzyk-Krzeska, M.F.1    Beresh, J.E.2
  • 12
    • 0028284559 scopus 로고
    • Hypoxia stimulates binding of a cytoplasmic protein to a pyrimidine rich sequence in the 3′-untranslated region of rat tyrosine hydroxylase mRNA
    • Czyzyk-Krzeska, M. F., Z. Dominski, R. Kole, and D. E. Millhorn. Hypoxia stimulates binding of a cytoplasmic protein to a pyrimidine rich sequence in the 3′-untranslated region of rat tyrosine hydroxylase mRNA. J. Biol. Chem. 269: 9940-9945, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9940-9945
    • Czyzyk-Krzeska, M.F.1    Dominski, Z.2    Kole, R.3    Millhorn, D.E.4
  • 13
    • 0027979247 scopus 로고
    • Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells
    • Czyzyk-Krzeska, M. F., B. A. Furnari, E. E. Lawson, and D. E. Millhorn. Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells. J. Biol. Chem. 269: 760-764, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 760-764
    • Czyzyk-Krzeska, M.F.1    Furnari, B.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 14
    • 0031033532 scopus 로고    scopus 로고
    • Post-transcriptional regulation of tyrosine hydroxylase gene expression by oxygen in PC12 cells
    • Czyzyk-Krzeska, M. F., W. R. Paulding, J. E. Beresh, and S. L. Kroll. Post-transcriptional regulation of tyrosine hydroxylase gene expression by oxygen in PC12 cells. Kidney Int. 51: 585-590, 1997.
    • (1997) Kidney Int. , vol.51 , pp. 585-590
    • Czyzyk-Krzeska, M.F.1    Paulding, W.R.2    Beresh, J.E.3    Kroll, S.L.4
  • 15
    • 0031029982 scopus 로고    scopus 로고
    • Cobalt and deferrioxamine reveal crucial members of the oxygen sensing pathway in HepG2 cells
    • Ehleben, W., T. Porwol, J. Fandrey, W. Kummer, and H. Acker. Cobalt and deferrioxamine reveal crucial members of the oxygen sensing pathway in HepG2 cells. Kidney Int. 51: 483-491, 1997.
    • (1997) Kidney Int. , vol.51 , pp. 483-491
    • Ehleben, W.1    Porwol, T.2    Fandrey, J.3    Kummer, W.4    Acker, H.5
  • 16
    • 0031038417 scopus 로고    scopus 로고
    • Cobalt chloride and deferrioxamine antagonize the inhibition of erythropoietin production by reactive oxygen species
    • Fandrey, J., S. Frede, W. Ehleben, T. Porwol, H. Acker, and W. Jelkmann. Cobalt chloride and deferrioxamine antagonize the inhibition of erythropoietin production by reactive oxygen species. Kidney Int. 51: 492-496, 1997.
    • (1997) Kidney Int. , vol.51 , pp. 492-496
    • Fandrey, J.1    Frede, S.2    Ehleben, W.3    Porwol, T.4    Acker, H.5    Jelkmann, W.6
  • 17
    • 0027970536 scopus 로고
    • Role of hydrogen peroxide in hypoxia-induced erythropoietin production
    • Fandrey, J., S. Frede, and W. Jelkmann. Role of hydrogen peroxide in hypoxia-induced erythropoietin production. Biochem. J. 303: 507-510, 1994.
    • (1994) Biochem. J. , vol.303 , pp. 507-510
    • Fandrey, J.1    Frede, S.2    Jelkmann, W.3
  • 18
    • 0023144674 scopus 로고
    • Adaptation of neurotransmitter synthesis to chronic hypoxia in cell culture
    • Feinsilver, S. H., R. Wong, and D. M. Rayabin. Adaptation of neurotransmitter synthesis to chronic hypoxia in cell culture. Biochim. Biophys. Acta 928: 56-62, 1987.
    • (1987) Biochim. Biophys. Acta , vol.928 , pp. 56-62
    • Feinsilver, S.H.1    Wong, R.2    Rayabin, D.M.3
  • 19
    • 0020334226 scopus 로고
    • Effects of hypoxia on catecholamine synthesis in rabbit carotid body in vitro
    • Fidone, S., C. Gonzalez, and K. Yoshizaki. Effects of hypoxia on catecholamine synthesis in rabbit carotid body in vitro. J. Physiol. (Lond.) 333: 81-91, 1982.
    • (1982) J. Physiol. (Lond.) , vol.333 , pp. 81-91
    • Fidone, S.1    Gonzalez, C.2    Yoshizaki, K.3
  • 20
    • 0020334228 scopus 로고
    • Effects of low oxygen on the release of dopamine from rabbit carotid body in vitro
    • Fidone, S., C. Gonzalez, and K. Yoshizaki. Effects of low oxygen on the release of dopamine from rabbit carotid body in vitro. J. Physiol. (Lond.) 333: 93-110, 1982.
    • (1982) J. Physiol. (Lond.) , vol.333 , pp. 93-110
    • Fidone, S.1    Gonzalez, C.2    Yoshizaki, K.3
  • 21
    • 0028844810 scopus 로고
    • Diphenylene iodonium inhibits the induction of erythropoietin and other mammalian genes by hypoxia. Implications for the oxygen sensing
    • Gleadle, J. M., B. L. Ebert, and P. J. Ratcliffe. Diphenylene iodonium inhibits the induction of erythropoietin and other mammalian genes by hypoxia. Implications for the oxygen sensing. Eur. J. Biochem. 234: 92-99, 1995.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 92-99
    • Gleadle, J.M.1    Ebert, B.L.2    Ratcliffe, P.J.3
  • 22
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • Goldberg, M. A., S. P. Dunning, and H. F. Bunn. Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein. Science 242: 1412-1415, 1988.
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 23
    • 0028095127 scopus 로고
    • Similarities between the oxygen sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin
    • Goldberg, M. A., and T. J. Schneider. Similarities between the oxygen sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin. J. Biol. Chem. 269: 4355-4359, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4355-4359
    • Goldberg, M.A.1    Schneider, T.J.2
  • 24
    • 0028815150 scopus 로고
    • Differential inhibition by iodonium compounds of induced erythropoietin expression
    • Goldwasser, E., P. Alibali, and A. Gardner. Differential inhibition by iodonium compounds of induced erythropoietin expression. J. Biol. Chem. 270: 2628-2629, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2628-2629
    • Goldwasser, E.1    Alibali, P.2    Gardner, A.3
  • 25
    • 0018677857 scopus 로고
    • Effects of hypoxia on tyrosine hydroxylase activity in rat carotid body
    • Gonzalez, C., Y. Kwok, J. Gibb, and S. Fidone. Effects of hypoxia on tyrosine hydroxylase activity in rat carotid body. J. Neurochem. 33: 713-719, 1979.
    • (1979) J. Neurochem. , vol.33 , pp. 713-719
    • Gonzalez, C.1    Kwok, Y.2    Gibb, J.3    Fidone, S.4
  • 26
    • 0028308507 scopus 로고
    • Effects of cobalt on heme proteins of erythropoietin-producing HepG2 cells in multicellular spheroid culture
    • Gorlach, A., J. Fandrey, G. Holtermann, and H. Acker. Effects of cobalt on heme proteins of erythropoietin-producing HepG2 cells in multicellular spheroid culture. FEBS Lett. 348: 216-218, 1994.
    • (1994) FEBS Lett. , vol.348 , pp. 216-218
    • Gorlach, A.1    Fandrey, J.2    Holtermann, G.3    Acker, H.4
  • 29
    • 0017603133 scopus 로고
    • Induction of tyrosine 3-monooxygenase in carotid body of rats exposed to hypoxic conditions
    • Hanbauer, I., W. Lovenberg, and E. Costa. Induction of tyrosine 3-monooxygenase in carotid body of rats exposed to hypoxic conditions. Neuropharmacology 16: 277-282, 1977.
    • (1977) Neuropharmacology , vol.16 , pp. 277-282
    • Hanbauer, I.1    Lovenberg, W.2    Costa, E.3
  • 30
    • 0029994507 scopus 로고    scopus 로고
    • Effects of transition metals on the expression of the erythropoietin gene: Further evidence that the oxygen sensor is a heme protein
    • Ho, V. T., and H. F. Bunn. Effects of transition metals on the expression of the erythropoietin gene: further evidence that the oxygen sensor is a heme protein. Biochem. Biophys. Res. Commun. 223: 175-180, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 175-180
    • Ho, V.T.1    Bunn, H.F.2
  • 31
    • 0028840937 scopus 로고
    • Induction of gene expression of catecholamine-synthesizing enzymes by insulin-like growth factor-I
    • Hwang, O., and H. J. Choi. Induction of gene expression of catecholamine-synthesizing enzymes by insulin-like growth factor-I. J. Neurochem. 65: 1988-1996, 1995.
    • (1995) J. Neurochem. , vol.65 , pp. 1988-1996
    • Hwang, O.1    Choi, H.J.2
  • 32
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., A. Sinskey, and H. F. Lodish. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.2    Lodish, H.F.3
  • 33
    • 0017339770 scopus 로고
    • Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
    • Isaacs, J., and F. Binkley. Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue. Biochim. Biophys. Acta 497: 192-204, 1977.
    • (1977) Biochim. Biophys. Acta , vol.497 , pp. 192-204
    • Isaacs, J.1    Binkley, F.2
  • 34
    • 0024445290 scopus 로고
    • A comparison of cobalt(II) and iron(II) hydroxyl and superoxide free radical formation
    • Kadiiska, M. B., K. R. Maples, and R. P. Mason. A comparison of cobalt(II) and iron(II) hydroxyl and superoxide free radical formation. Arch. Biochem. Biophys. 275: 98-111, 1989.
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 98-111
    • Kadiiska, M.B.1    Maples, K.R.2    Mason, R.P.3
  • 35
    • 0027513804 scopus 로고
    • Tyrosine hydroxylase protein and messenger RNAin the dopaminergic nigral neurons of patients with Parkinson's disease
    • Kastner, A., E. C. Hirsch, Y. Agid, and F. Jovoy-Agid. Tyrosine hydroxylase protein and messenger RNAin the dopaminergic nigral neurons of patients with Parkinson's disease. Brain Res. 606: 341-345, 1993.
    • (1993) Brain Res. , vol.606 , pp. 341-345
    • Kastner, A.1    Hirsch, E.C.2    Agid, Y.3    Jovoy-Agid, F.4
  • 36
    • 0029040451 scopus 로고
    • Immunochemical demonstration of four subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body
    • Kummer, W., and H. Acker. Immunochemical demonstration of four subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body. J. Appl. Physiol. 78: 1904-1909, 1995.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 1904-1909
    • Kummer, W.1    Acker, H.2
  • 37
    • 0000474831 scopus 로고
    • Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase
    • Margoliash, E., A. Novogrodsky, and A. Schejter. Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochem. J. 74: 339-350, 1960.
    • (1960) Biochem. J. , vol.74 , pp. 339-350
    • Margoliash, E.1    Novogrodsky, A.2    Schejter, A.3
  • 39
    • 0028859483 scopus 로고    scopus 로고
    • 2-responsive sequences on the tyrosine hydroxylase gene
    • 2-responsive sequences on the tyrosine hydroxylase gene. J. Biol. Chem. 270: 23774-23779, 1996.
    • (1996) J. Biol. Chem. , vol.270 , pp. 23774-23779
    • Norris, M.L.1    Millhorn, D.E.2
  • 40
    • 0027974133 scopus 로고
    • Assessing oxygen radicals as mediators in activation of inducible eukaryotic transcription factor NF-kappa B
    • Schreck, R., and P. A. Baeuerle. Assessing oxygen radicals as mediators in activation of inducible eukaryotic transcription factor NF-kappa B. Methods Enzymol. 234: 151-163, 1994.
    • (1994) Methods Enzymol. , vol.234 , pp. 151-163
    • Schreck, R.1    Baeuerle, P.A.2
  • 41
    • 0029087787 scopus 로고
    • Decreased carotid body sensitivity in chronic hypoxia: Role of dopamine
    • Tatsumi, K., C. K. Pickett, and J. V. Weol. Decreased carotid body sensitivity in chronic hypoxia: role of dopamine. Respir. Physiol. 101: 47-57, 1995.
    • (1995) Respir. Physiol. , vol.101 , pp. 47-57
    • Tatsumi, K.1    Pickett, C.K.2    Weol, J.V.3
  • 42
    • 0030050910 scopus 로고    scopus 로고
    • Hypoxic induction of gene expression in chronic granulomatous disease-derived B-cell lines: Oxygen sensing is independent of the cytochrome b558-containing nicotinamide adenine dinucleotide phosphate oxidase
    • Wenger, R. H., H. H. Marti, S. Schuerer-Maly, I. Kvietikova, C. Bauer, M. Gassmann, and F. E. Maly. Hypoxic induction of gene expression in chronic granulomatous disease-derived B-cell lines: oxygen sensing is independent of the cytochrome b558-containing nicotinamide adenine dinucleotide phosphate oxidase. Blood 87: 756-761, 1996.
    • (1996) Blood , vol.87 , pp. 756-761
    • Wenger, R.H.1    Marti, H.H.2    Schuerer-Maly, S.3    Kvietikova, I.4    Bauer, C.5    Gassmann, M.6    Maly, F.E.7
  • 43
    • 0024230924 scopus 로고
    • Hypoxia increases glutathione redox cycle and protects lungs against oxidants
    • White, C. W., J. H. Jackson, I. F. McMurtry, and J. E. Repine. Hypoxia increases glutathione redox cycle and protects lungs against oxidants. J. Appl. Physiol. 65: 2607-2615, 1988.
    • (1988) J. Appl. Physiol. , vol.65 , pp. 2607-2615
    • White, C.W.1    Jackson, J.H.2    McMurtry, I.F.3    Repine, J.E.4
  • 44
    • 0027327956 scopus 로고
    • Oxygen sensing in airway chemoreceptors
    • Youngson, C., C. Nurse, and E. Cutz. Oxygen sensing in airway chemoreceptors. Nature 365: 153-155, 1991.
    • (1991) Nature , vol.365 , pp. 153-155
    • Youngson, C.1    Nurse, C.2    Cutz, E.3


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