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Volumn 360, Issue 1464, 2005, Pages 2201-2210

The oxygen sensing signal cascade under the influence of reactive oxygen species

Author keywords

Carotid body; Cytochrome aa3; HIF prolyl hydroxylase; NADPH oxidase; Oxygen sensing; Reactive oxygen species

Indexed keywords

CYTOCHROME; ENZYME ACTIVITY; FREE RADICAL; HOMEOSTASIS; HYPOXIA; MITOCHONDRION; OXYGEN; PHYSIOLOGICAL RESPONSE; SIGNAL;

EID: 33744982959     PISSN: 09628436     EISSN: None     Source Type: Journal    
DOI: 10.1098/rstb.2005.1760     Document Type: Conference Paper
Times cited : (54)

References (83)
  • 1
    • 4644259153 scopus 로고    scopus 로고
    • Cellular oxygen sensing need in CNS function: Physiological and pathological implications [Review]
    • doi:10.1242/jeb.01075
    • Acker, T. & Acker, H. 2004 Cellular oxygen sensing need in CNS function: physiological and pathological implications [Review]. J. Exp. Biol. 207, 3171-3188. (doi:10.1242/jeb.01075.)
    • (2004) J. Exp. Biol , vol.207 , pp. 3171-3188
    • Acker, T.1    Acker, H.2
  • 2
    • 0017750618 scopus 로고
    • 2 decrease after perfusion stop within the carotid body of the cat in vivo and in vitro
    • doi:10.1007/BF00591569
    • 2 decrease after perfusion stop within the carotid body of the cat in vivo and in vitro. Pflüg. Arch. 369, 135-140. (doi:10.1007/BF00591569.)
    • (1977) Pflüg. Arch , vol.369 , pp. 135-140
    • Acker, H.1    Lübbers, D.W.2
  • 3
    • 0019258344 scopus 로고
    • Measurements of the partial pressure of oxygen in the carotid body of fetal sheep and newborn lambs
    • Acker, H., Lübbers, D. W., Purves, M. J. & Tan, E. D. 1980 Measurements of the partial pressure of oxygen in the carotid body of fetal sheep and newborn lambs. J. Dev. Physiol. 2, 323-328.
    • (1980) J. Dev. Physiol , vol.2 , pp. 323-328
    • Acker, H.1    Lübbers, D.W.2    Purves, M.J.3    Tan, E.D.4
  • 5
    • 0033571436 scopus 로고    scopus 로고
    • Lack of oxygen sensing by mitochondria in platelets
    • doi:10.1046/j.1432-1327.1999.00846.x
    • Arthur, P. G., Ngo, C. T., Moretta, P. & Guppy, M. 1999 Lack of oxygen sensing by mitochondria in platelets. Eur. J. Biochem. 266, 215-219. (doi:10.1046/j.1432-1327.1999.00846.x.)
    • (1999) Eur. J. Biochem , vol.266 , pp. 215-219
    • Arthur, P.G.1    Ngo, C.T.2    Moretta, P.3    Guppy, M.4
  • 6
    • 0034602950 scopus 로고    scopus 로고
    • Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma
    • doi:10.1126/science.287.5454.848
    • Baysal, B. E. et al. 2000 Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma. Science 287, 848-851. (doi:10.1126/science.287.5454.848.)
    • (2000) Science , vol.287 , pp. 848-851
    • Baysal, B.E.1
  • 7
    • 2542458360 scopus 로고    scopus 로고
    • Visualization of the three-dimensional organization of hypoxia-inducible factor-1 alpha and interacting cofactors in subnuclear structures
    • doi:10.1515/BC.2004.017
    • Berchner-Pfannschmidt, U., Wotzlaw, C., Merten, E., Acker, H. & Fandrey, J. 2004 Visualization of the three-dimensional organization of hypoxia-inducible factor-1 alpha and interacting cofactors in subnuclear structures. Biol. Chem. 385, 231-237. (doi:10.1515/BC.2004.017.)
    • (2004) Biol. Chem , vol.385 , pp. 231-237
    • Berchner-Pfannschmidt, U.1    Wotzlaw, C.2    Merten, E.3    Acker, H.4    Fandrey, J.5
  • 8
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 alpha in normoxia
    • doi:10.1093/emboj/cdg392
    • Berra, E., Benizri, E., Ginouves, A., Volmat, V., Roux, D. & Pouyssegur, J. 2003 HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 alpha in normoxia. EMBO J. 22, 4082-4090. (doi:10.1093/emboj/cdg392.)
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 9
    • 0031791118 scopus 로고    scopus 로고
    • Effects of modulators of the production and degradation of hydrogen-peroxide on erythropoietin synthesis
    • doi:10.1016/S0034- 5687(98)00080-2
    • Canbolat, O., Fandrey, J. & Jelkmann, W. 1998 Effects of modulators of the production and degradation of hydrogen-peroxide on erythropoietin synthesis. Respir. Physiol. 114, 175-183. (doi:10.1016/S0034- 5687(98)00080-2.)
    • (1998) Respir. Physiol , vol.114 , pp. 175-183
    • Canbolat, O.1    Fandrey, J.2    Jelkmann, W.3
  • 10
    • 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. 2000 Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell Biol. 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
  • 13
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • doi:10.1016/S0378-1119(01)00449-8
    • Cheng, G. J., Cao, Z. H., Xu, X. X., Van Meir, E. G. & Lambeth, J. D. 2001 Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269, 131-140. (doi:10.1016/S0378-1119(01)00449-8.)
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.J.1    Cao, Z.H.2    Xu, X.X.3    Van Meir, E.G.4    Lambeth, J.D.5
  • 14
    • 0037432686 scopus 로고    scopus 로고
    • Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells
    • doi:10.1016/S0006-291X(03)00453-4
    • Cioffi, C. L., Liu, X. Q., Kosinski, P. A., Garay, M. & Bowen, B. R. 2003 Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells. Biochem. Biophys. Res. Commun. 303, 947-953. (doi:10.1016/S0006-291X(03)00453-4.)
    • (2003) Biochem. Biophys. Res. Commun , vol.303 , pp. 947-953
    • Cioffi, C.L.1    Liu, X.Q.2    Kosinski, P.A.3    Garay, M.4    Bowen, B.R.5
  • 16
    • 1542300383 scopus 로고    scopus 로고
    • The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen
    • doi:10.1074/jbc.M308862200
    • del Peso, L., Castellanos, M. C., Temes, E., Martin-Puig, S., Cuevas, Y., Olmos, G. & Landazuri, M. O. 2003 The von Hippel Lindau/hypoxia-inducible factor (HIF) pathway regulates the transcription of the HIF-proline hydroxylase genes in response to low oxygen. J. Biol. Chem. 278, 48 690-48 695. (doi:10.1074/jbc.M308862200.)
    • (2003) J. Biol. Chem , vol.278
    • del Peso, L.1    Castellanos, M.C.2    Temes, E.3    Martin-Puig, S.4    Cuevas, Y.5    Olmos, G.6    Landazuri, M.O.7
  • 17
    • 11144337759 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Regulation by hypoxic and non-hypoxic activators
    • doi:10.1016/j.biocel. 2004.08.012
    • Dery, M. A. C., Michaud, M. D. & Richard, D. E. 2005 Hypoxia-inducible factor 1: regulation by hypoxic and non-hypoxic activators. Int. J. Biochem. Cell Biol. 37, 535-540. (doi:10.1016/j.biocel. 2004.08.012.)
    • (2005) Int. J. Biochem. Cell Biol , vol.37 , pp. 535-540
    • Dery, M.A.C.1    Michaud, M.D.2    Richard, D.E.3
  • 18
    • 15744368783 scopus 로고    scopus 로고
    • The expression of the NADPH oxidase subunit p22phox is regulated by a redox-sensitive pathway in endothelial cells
    • doi:10.1016/j.freeradbiomed. 2004.09.036
    • Djordjevic, T., Pogrebniak, A., BelAiba, R. S., Bonello, S., Wotzlaw, C., Acker, H., Hess, J. & Gorlach, A. 2005 The expression of the NADPH oxidase subunit p22phox is regulated by a redox-sensitive pathway in endothelial cells. Free Radic. Biol. Med. 38, 616-630. (doi:10.1016/j.freeradbiomed. 2004.09.036.)
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 616-630
    • Djordjevic, T.1    Pogrebniak, A.2    BelAiba, R.S.3    Bonello, S.4    Wotzlaw, C.5    Acker, H.6    Hess, J.7    Gorlach, A.8
  • 19
    • 0026767130 scopus 로고
    • i in type I cells isolated from the rabbit carotid body
    • i in type I cells isolated from the rabbit carotid body. J. Physiol. (Lond.) 450, 33-61.
    • (1992) J. Physiol. (Lond.) , vol.450 , pp. 33-61
    • Duchen, M.R.1    Biscoe, T.J.2
  • 21
    • 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
    • doi:10.1093/emboj/18.7.1905
    • Ema, M., Hirota, K., Mimura, J., Abe, H., Yodoi, J., Sogawa, K., Poellinger, L. & Fujii-Kuriyama, Y. 1999 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. 18, 1905-1914. (doi:10.1093/emboj/18.7.1905.)
    • (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
  • 22
    • 17944375360 scopus 로고    scopus 로고
    • Epstein, A. C. et al. 2001 C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54. (doi:10.1016/S0092-8674(01)00507-4.)
    • Epstein, A. C. et al. 2001 C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54. (doi:10.1016/S0092-8674(01)00507-4.)
  • 23
    • 0346734132 scopus 로고    scopus 로고
    • Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor
    • doi:10.1073/pnas.2533374100
    • Erbel, P. J. A., Card, P. B., Karakuzu, O., Bruick, R. K. & Gardner, K. H. 2003 Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor. Proc. Natl Acad. Sci. USA 100, 15 504-15 509. (doi:10.1073/pnas.2533374100. )
    • (2003) Proc. Natl Acad. Sci. USA , vol.100
    • Erbel, P.J.A.1    Card, P.B.2    Karakuzu, O.3    Bruick, R.K.4    Gardner, K.H.5
  • 24
    • 2442693041 scopus 로고    scopus 로고
    • Oxygen-dependent and tissue-specific regulation of erythropoietin gene expression
    • Fandrey, J. 2004 Oxygen-dependent and tissue-specific regulation of erythropoietin gene expression. Am. J. Physiol. Regul. Integr. Comp. Physiol. 286, R977-R988.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.286
    • Fandrey, J.1
  • 25
    • 0034466201 scopus 로고    scopus 로고
    • Reactive oxygen species as regulators of oxygen dependent gene expression
    • Fandrey, J. & Genius, J. 2000 Reactive oxygen species as regulators of oxygen dependent gene expression. Adv. Exp. Med. Biol. 475, 153-159.
    • (2000) Adv. Exp. Med. Biol , vol.475 , pp. 153-159
    • Fandrey, J.1    Genius, J.2
  • 26
    • 0031038417 scopus 로고    scopus 로고
    • Cobalt chloride and desferrioxamine antagonize the inhibition of erythropoietin production by reactive oxygen species
    • Fandrey, J., Frede, S., Ehleben, W., Porwol, T., Acker, H. & Jelkmann, W. 1997 Cobalt chloride and desferrioxamine antagonize the inhibition of erythropoietin production by reactive oxygen species. Kidney Int. 51, 492-496.
    • (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
  • 28
    • 0033886347 scopus 로고    scopus 로고
    • Oxidative stress and expression of p22phox are involved in the up-regulation of tissue factor in vascular smooth muscle cells in response to activated platelets
    • doi:10.1096/fj.14.11.1518
    • Görlach, A., Brandes, R. P., Bassus, S., Kronemann, N., Kirchmaier, C. M., Busse, R. & Schini-Kerth, V. B. 2000a Oxidative stress and expression of p22phox are involved in the up-regulation of tissue factor in vascular smooth muscle cells in response to activated platelets. FASEB J. 14, 1518-1528. (doi:10.1096/fj.14.11.1518.)
    • (2000) FASEB J , vol.14 , pp. 1518-1528
    • Görlach, A.1    Brandes, R.P.2    Bassus, S.3    Kronemann, N.4    Kirchmaier, C.M.5    Busse, R.6    Schini-Kerth, V.B.7
  • 29
    • 0034617071 scopus 로고    scopus 로고
    • A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall
    • Görlach, A., Brandes, R. P., Nguyen, K., Amidi, M., Dehghani, F. & Busse, R. 2000b A gp91phox containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall. Circ. Res. 87, 26-32.
    • (2000) Circ. Res , vol.87 , pp. 26-32
    • Görlach, A.1    Brandes, R.P.2    Nguyen, K.3    Amidi, M.4    Dehghani, F.5    Busse, R.6
  • 31
    • 11144356447 scopus 로고    scopus 로고
    • Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia inducible factor 1 via increase in reactive oxygen species
    • doi:10.1016/j. freeradbiomed.2004.02.071
    • Goyal, P. et al. 2004 Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia inducible factor 1 via increase in reactive oxygen species. Free Radic. Biol. Med. 36, 1279-1288. (doi:10.1016/j. freeradbiomed.2004.02.071.)
    • (2004) Free Radic. Biol. Med , vol.36 , pp. 1279-1288
    • Goyal, P.1
  • 32
    • 3142674291 scopus 로고    scopus 로고
    • Oxygen sensation and social feeding mediated by a C-elegans guanylate cyclase homologue
    • doi:10.1038/nature02714
    • Gray, J. M., Karow, D. S., Lu, H., Chang, A. J., Chang, J. S., Ellis, R. E., Marietta, M. A. & Bargmann, C. I. 2004 Oxygen sensation and social feeding mediated by a C-elegans guanylate cyclase homologue. Nature 430, 317-322. (doi:10.1038/nature02714.)
    • (2004) Nature , vol.430 , pp. 317-322
    • Gray, J.M.1    Karow, D.S.2    Lu, H.3    Chang, A.J.4    Chang, J.S.5    Ellis, R.E.6    Marietta, M.A.7    Bargmann, C.I.8
  • 33
    • 0035860375 scopus 로고    scopus 로고
    • A non-hypoxic, ROS-sensitive pathway mediates TNF-alpha-dependent regulation of HIF-1alpha
    • doi:10.1016/S0014-5793(01)02833-2
    • Haddad, J. J. & Land, S. C. 2001 A non-hypoxic, ROS-sensitive pathway mediates TNF-alpha-dependent regulation of HIF-1alpha. FEBS Lett. 505, 269-274. (doi:10.1016/S0014-5793(01)02833-2.)
    • (2001) FEBS Lett , vol.505 , pp. 269-274
    • Haddad, J.J.1    Land, S.C.2
  • 34
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1 alpha
    • doi:10.1126/science.1088805
    • Hagen, T., Taylor, C. T., Lam, F. & Moncada, S. 2003 Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1 alpha. Science 302, 1975-1978. (doi:10.1126/science.1088805.)
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 35
    • 18544386401 scopus 로고    scopus 로고
    • Hypoxia inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family
    • doi:10.1074/jbc.C200273200
    • Hewitson, K. S. et al. 2002 Hypoxia inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J. Biol. Chem. 277, 26 351-26 355. (doi:10.1074/jbc.C200273200.)
    • (2002) J. Biol. Chem , vol.277
    • Hewitson, K.S.1
  • 36
    • 0035877728 scopus 로고    scopus 로고
    • Rac1 activity is required for the activation of hypoxia-inducible factor 1
    • doi:10.1074/jbc.M100677200
    • Hirota, K. & Semenza, G. L. 2001 Rac1 activity is required for the activation of hypoxia-inducible factor 1. J. Biol. Chem. 276, 21 166-21 172. (doi:10.1074/jbc.M100677200.)
    • (2001) J. Biol. Chem , vol.276
    • Hirota, K.1    Semenza, G.L.2
  • 37
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • doi:10.1074/jbc.M304982200
    • Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I. & Myllyharju, J. 2003 Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278, 30 772-30 780. (doi:10.1074/jbc.M304982200.)
    • (2003) J. Biol. Chem , vol.278
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 38
    • 0037490210 scopus 로고    scopus 로고
    • Hypoxia-inducible factor and its biomedical relevance
    • doi:10.1074/jbc.R200030200
    • Huang, L. E. & Bunn, H. F. 2003 Hypoxia-inducible factor and its biomedical relevance. J. Biol. Chem. 278, 19 575-19 578. (doi:10.1074/jbc.R200030200.)
    • (2003) J. Biol. Chem , vol.278
    • Huang, L.E.1    Bunn, H.F.2
  • 39
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • doi:10.1074/jbc.271.50.32253
    • Huang, L. E., Arany, Z., Livingston, D. M. & Bunn, H. F. 1996 Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J. Biol. Chem. 271, 32 253-32 259. (doi:10.1074/jbc.271.50.32253.)
    • (1996) J. Biol. Chem , vol.271
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 40
    • 0034282213 scopus 로고    scopus 로고
    • NADPH oxidase: A universal oxygen sensor?
    • doi:10.1016/S0891-5849(00)00320-8
    • Jones, R. D., Hancock, J. T. & Morice, A. H. 2000 NADPH oxidase: a universal oxygen sensor? Free Radic. Biol. Med. 29, 416-424. (doi:10.1016/S0891-5849(00)00320-8.)
    • (2000) Free Radic. Biol. Med , vol.29 , pp. 416-424
    • Jones, R.D.1    Hancock, J.T.2    Morice, A.H.3
  • 41
    • 0033621496 scopus 로고    scopus 로고
    • Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase
    • doi:10.1074/jbc.274.53.37974
    • Kannt, A., Pfitzner, U., Ruitenberg, M., Hellwig, P., Ludwig, B., Mantele, W., Fendler, K. & Michel, H. 1999 Mutation of Arg-54 strongly influences heme composition and rate and directionality of electron transfer in Paracoccus denitrificans cytochrome c oxidase. J. Biol. Chem. 274, 37 974-37 981. (doi:10.1074/jbc.274.53.37974.)
    • (1999) J. Biol. Chem , vol.274
    • Kannt, A.1    Pfitzner, U.2    Ruitenberg, M.3    Hellwig, P.4    Ludwig, B.5    Mantele, W.6    Fendler, K.7    Michel, H.8
  • 42
    • 0035030363 scopus 로고    scopus 로고
    • Respiratory control in neonatal mice with NADPH oxidase deficiency
    • doi:10.1016/S0034-5687(01)00205-5
    • Kazemian, P., Stephenson, R., Yeger, H. & Cutz, E. 2001 Respiratory control in neonatal mice with NADPH oxidase deficiency. Resp. Physiol. 126, 89-101. (doi:10.1016/S0034-5687(01)00205-5.)
    • (2001) Resp. Physiol , vol.126 , pp. 89-101
    • Kazemian, P.1    Stephenson, R.2    Yeger, H.3    Cutz, E.4
  • 43
    • 0037154262 scopus 로고    scopus 로고
    • Defective carotid body function and impaired ventilatory responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1 alpha
    • doi:10.1073/pnas. 022634199
    • Kline, D. D., Peng, Y. J., Manalo, D. J., Semenza, G. L. & Prabhakar, N. R. 2002 Defective carotid body function and impaired ventilatory responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1 alpha. Proc. Natl Acad. Sci. USA 99, 821-826. (doi:10.1073/pnas. 022634199.)
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 821-826
    • Kline, D.D.1    Peng, Y.J.2    Manalo, D.J.3    Semenza, G.L.4    Prabhakar, N.R.5
  • 44
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles, H. J., Raval, R. R., Harris, A. L. & Ratcliffe, P. J. 2003 Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res. 63, 1764-1768.
    • (2003) Cancer Res , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 45
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free-radicals and derived species in signal-transduction
    • Lander, H. M. 1997 An essential role for free-radicals and derived species in signal-transduction. FASEB J. 11, 118-124.
    • (1997) FASEB J , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 46
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • doi:10.1126/science.1068592
    • Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J. & Whitelaw, M. L. 2002 Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science 295, 858-861. (doi:10.1126/science.1068592.)
    • (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
  • 47
    • 0035702819 scopus 로고    scopus 로고
    • New control of mitochondrial membrane potential and ROS formation - a hypothesis
    • doi:10.1515/BC.2001.198
    • Lee, I., Bender, E., Arnold, S. & Kadenbach, B. 2001 New control of mitochondrial membrane potential and ROS formation - a hypothesis. Biol. Chem. 382, 1629-1636. (doi:10.1515/BC.2001.198.)
    • (2001) Biol. Chem , vol.382 , pp. 1629-1636
    • Lee, I.1    Bender, E.2    Arnold, S.3    Kadenbach, B.4
  • 48
    • 0037470162 scopus 로고    scopus 로고
    • Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau
    • doi:10.1074/jbc.M210385200
    • Lee, C., Kim, S. J., Jeong, D. G., Lee, S. M. & Ryu, S. E. 2003 Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau. J. Biol. Chem. 278, 7558-7563. (doi:10.1074/jbc.M210385200.)
    • (2003) J. Biol. Chem , vol.278 , pp. 7558-7563
    • Lee, C.1    Kim, S.J.2    Jeong, D.G.3    Lee, S.M.4    Ryu, S.E.5
  • 50
    • 0036433394 scopus 로고    scopus 로고
    • Mammalian EGLN genes have distinct patterns of mRNA expression and regulation
    • Lieb, M. E., Menzies, K., Moschella, M. C., Ni, R. & Taubman, M. B. 2002 Mammalian EGLN genes have distinct patterns of mRNA expression and regulation. Biochem. Cell Biol. 80, 421-426.
    • (2002) Biochem. Cell Biol , vol.80 , pp. 421-426
    • Lieb, M.E.1    Menzies, K.2    Moschella, M.C.3    Ni, R.4    Taubman, M.B.5
  • 51
    • 1842639126 scopus 로고    scopus 로고
    • Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor
    • doi:10.1074/jbc.M313614200
    • Linke, S., Stojkoski, C., Kewley, R. J., Booker, G. W., Whitelaw, M. L. & Peet, D. J. 2004 Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor. J. Biol. Chem. 279, 14 391-14 397. (doi:10.1074/jbc.M313614200.)
    • (2004) J. Biol. Chem , vol.279
    • Linke, S.1    Stojkoski, C.2    Kewley, R.J.3    Booker, G.W.4    Whitelaw, M.L.5    Peet, D.J.6
  • 52
    • 1642447143 scopus 로고    scopus 로고
    • A Fenton reaction at the endoplasmic reticulum is involved in the redox control of hypoxia-inducible gene expression
    • doi:10.1073/pnas.0400265101
    • Liu, Q., Berchner-Pfannschmidt, U., Moller, U., Brecht, M., Wotzlaw, C., Acker, H., Jungermann, K. & Kietzmann, T. 2004 A Fenton reaction at the endoplasmic reticulum is involved in the redox control of hypoxia-inducible gene expression. Proc. Natl Acad. Sci. USA 101, 4302-4307. (doi:10.1073/pnas.0400265101.)
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4302-4307
    • Liu, Q.1    Berchner-Pfannschmidt, U.2    Moller, U.3    Brecht, M.4    Wotzlaw, C.5    Acker, H.6    Jungermann, K.7    Kietzmann, T.8
  • 53
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • doi:10.1074/jbc.274.34.24147
    • Lok, C. N. & Ponka, P. 1999 Identification of a hypoxia response element in the transferrin receptor gene. J. Biol. Chem. 274, 24 147-24 152. (doi:10.1074/jbc.274.34.24147.)
    • (1999) J. Biol. Chem , vol.274
    • Lok, C.N.1    Ponka, P.2
  • 54
    • 0037386143 scopus 로고    scopus 로고
    • Intracellular localisation of human HIF-1 alpha hydroxylases: Implications for oxygen sensing
    • doi:10.1242/jcs.00318
    • Metzen, E. et al. 2003 Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing. J. Cell Sci. 116, 1319-1326. (doi:10.1242/jcs.00318.)
    • (2003) J. Cell Sci , vol.116 , pp. 1319-1326
    • Metzen, E.1
  • 55
    • 0015369803 scopus 로고
    • Mitochondrial respiratory chain of carotid body and chemoreceptor response to changes in oxygen tension
    • Mills, E. & Jöbsis, F. F. 1972 Mitochondrial respiratory chain of carotid body and chemoreceptor response to changes in oxygen tension. J. Neurophysiol. 35, 405-428.
    • (1972) J. Neurophysiol , vol.35 , pp. 405-428
    • Mills, E.1    Jöbsis, F.F.2
  • 56
    • 0034647742 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
    • doi:10.1074/jbc.M000636200
    • Mukhopadhyay, C. K., Mazumder, B. & Fox, P. L. 2000 Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency. J. Biol. Chem. 275, 21 048-21 054. (doi:10.1074/jbc.M000636200.)
    • (2000) J. Biol. Chem , vol.275
    • Mukhopadhyay, C.K.1    Mazumder, B.2    Fox, P.L.3
  • 57
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • doi:10.1016/S0891-5849(01)00724-9
    • Nordberg, J. & Arner, E. S. 2001 Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. Med. 31, 1287-1312. (doi:10.1016/S0891-5849(01)00724-9.)
    • (2001) Free Radic. Biol. Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 58
    • 0035968183 scopus 로고    scopus 로고
    • Modulation of mitochondrial function by hydrogen peroxide
    • doi:10.1074/jbc.M100320200
    • Nulton-Persson, A. C. & Szweda, L. I. 2001 Modulation of mitochondrial function by hydrogen peroxide. J. Biol. Chem. 276, 23 357-23 361. (doi:10.1074/jbc.M100320200.)
    • (2001) J. Biol. Chem , vol.276
    • Nulton-Persson, A.C.1    Szweda, L.I.2
  • 59
    • 0036391915 scopus 로고    scopus 로고
    • Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors
    • doi:10.1016/S0006-291X(02)00862-8
    • Oehme, F., Ellinghaus, P., Kolkhof, P., Smith, T., Ramakrishnan, S., Hutter, J., Schramm, M. & Flamme, I. 2002 Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors. Biochem. Biophys. Res. Commun. 296, 343. (doi:10.1016/S0006-291X(02)00862-8.)
    • (2002) Biochem. Biophys. Res. Commun , vol.296 , pp. 343
    • Oehme, F.1    Ellinghaus, P.2    Kolkhof, P.3    Smith, T.4    Ramakrishnan, S.5    Hutter, J.6    Schramm, M.7    Flamme, I.8
  • 60
    • 0035721699 scopus 로고    scopus 로고
    • Acute oxygen sensing: Diverse but convergent mechanisms in airway and arterial chemoreceptors
    • doi:10.1186/rr51
    • Peers, C. & Kemp, P. J. 2001 Acute oxygen sensing: diverse but convergent mechanisms in airway and arterial chemoreceptors. Respir. Res. 2, 145-149. (doi:10.1186/rr51.)
    • (2001) Respir. Res , vol.2 , pp. 145-149
    • Peers, C.1    Kemp, P.J.2
  • 61
    • 0032529027 scopus 로고    scopus 로고
    • The influence of nickel and cobalt on putative members of the oxygen-sensing pathway of erythropoietin-producing HepG2 cells
    • doi:10.1046/j.1432-1327.1998.2560016.x
    • Porwol, T., Ehleben, W., Zierold, K., Fandrey, J. & Acker, H. 1998 The influence of nickel and cobalt on putative members of the oxygen-sensing pathway of erythropoietin-producing HepG2 cells. Eur. J. Biochem. 256, 16-23. (doi:10.1046/j.1432-1327.1998.2560016.x.)
    • (1998) Eur. J. Biochem , vol.256 , pp. 16-23
    • Porwol, T.1    Ehleben, W.2    Zierold, K.3    Fandrey, J.4    Acker, H.5
  • 62
    • 0034282388 scopus 로고    scopus 로고
    • Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1alpha in vascular smooth muscle cells
    • Richard, D. E., Berra, E. & Pouyssegur, J. 2000 Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1alpha in vascular smooth muscle cells. J. Biol. Chem. 275, 26 765-26 771.
    • (2000) J. Biol. Chem , vol.275
    • Richard, D.E.1    Berra, E.2    Pouyssegur, J.3
  • 63
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • doi:10.1074/jbc.272. 32.20055
    • Rolfs, A., Kvietikova, I., Gassmann, M. & Wenger, R. H. 1997 Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J. Biol. Chem. 272, 20 055-20 062. (doi:10.1074/jbc.272. 32.20055.)
    • (1997) J. Biol. Chem , vol.272
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 64
    • 0034725841 scopus 로고    scopus 로고
    • Mice lacking in gp91 phox subunit of NAD(P)H oxidase showed glomus cell [Ca2+](i) and respiratory responses to hypoxia
    • doi:10.1016/S0006-8993(00)02458-6
    • Roy, A., Rozanov, C., Mokashi, A., Daudu, P., Al mehdi, A. B., Shams, H. & Lahiri, S. 2000 Mice lacking in gp91 phox subunit of NAD(P)H oxidase showed glomus cell [Ca2+](i) and respiratory responses to hypoxia. Brain Res. 872, 188-193. (doi:10.1016/S0006-8993(00)02458-6.)
    • (2000) Brain Res , vol.872 , pp. 188-193
    • Roy, A.1    Rozanov, C.2    Mokashi, A.3    Daudu, P.4    Al mehdi, A.B.5    Shams, H.6    Lahiri, S.7
  • 65
    • 3042789543 scopus 로고    scopus 로고
    • Effects of iron-chelators onion-channels and HIF-1 alpha in the carotid body
    • doi:10.1016/j.resp.2004.03.010
    • Roy, A., Li, J. Q., Baby, S. M., Mokashi, A., Buerk, D. G. & Lahiri, S. 2004 Effects of iron-chelators onion-channels and HIF-1 alpha in the carotid body. Respir. Physiol. Neurobiol. 141, 115-123. (doi:10.1016/j.resp.2004.03.010.)
    • (2004) Respir. Physiol. Neurobiol , vol.141 , pp. 115-123
    • Roy, A.1    Li, J.Q.2    Baby, S.M.3    Mokashi, A.4    Buerk, D.G.5    Lahiri, S.6
  • 67
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • doi:10.1038/nrc1187
    • Semenza, G. L. 2003 Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3, 721-732. (doi:10.1038/nrc1187.)
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 68
    • 0035933716 scopus 로고    scopus 로고
    • Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway
    • doi:10.1074/jbc.C100177200
    • Srinivas, V., Leshchinsky, I., Sang, N., King, M. P., Minchenko, A. & Caro, J. 2001 Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway. J. Biol. Chem. 276, 21 995-21 998. (doi:10.1074/jbc.C100177200.)
    • (2001) J. Biol. Chem , vol.276
    • Srinivas, V.1    Leshchinsky, I.2    Sang, N.3    King, M.P.4    Minchenko, A.5    Caro, J.6
  • 69
    • 0036676159 scopus 로고    scopus 로고
    • 2 affinity correlates as putative oxygen sensor with rat carotid body chemoreceptor discharge
    • 2 affinity correlates as putative oxygen sensor with rat carotid body chemoreceptor discharge. FASEB J. 16, 1277-1279.
    • (2002) FASEB J , vol.16 , pp. 1277-1279
    • Streller, T.1    Huckstorf, C.2    Pfeiffer, C.3    Acker, H.4
  • 71
    • 0035157487 scopus 로고    scopus 로고
    • Tabata, M. et al. 2001 Stimulation of GATA-2 as a mechanism of hydrogen peroxide suppression in hypoxia-induced erythropoietin gene expression. J. Cell. Physiol. 186, 260-267. (doi:10.1002/1097-4652(200002) 186:2〈260::AID-JCP1025〉3.0.CO;2-K.)
    • Tabata, M. et al. 2001 Stimulation of GATA-2 as a mechanism of hydrogen peroxide suppression in hypoxia-induced erythropoietin gene expression. J. Cell. Physiol. 186, 260-267. (doi:10.1002/1097-4652(200002) 186:2〈260::AID-JCP1025〉3.0.CO;2-K.)
  • 72
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia
    • doi:10.1074/jbc.274.34.24142
    • Tacchini, L., Bianchi, L., Bernelli-Zazzera, A. & Cairo, G. 1999 Transferrin receptor induction by hypoxia. J. Biol. Chem. 274, 24 142-24 146. (doi:10.1074/jbc.274.34.24142.)
    • (1999) J. Biol. Chem , vol.274
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 73
    • 0035880239 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain
    • doi:10.1182/blood.V98.2.296
    • Vaux, E. C., Metzen, E., Yeates, K. M. & Ratcliffe, P. J. 2001 Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain. Blood 98, 296-302. (doi:10.1182/blood.V98.2.296.)
    • (2001) Blood , vol.98 , pp. 296-302
    • Vaux, E.C.1    Metzen, E.2    Yeates, K.M.3    Ratcliffe, P.J.4
  • 74
    • 0029123437 scopus 로고
    • Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1
    • doi:10.1006/bbrc.1995.2005
    • Wang, G. L., Jiang, B. H. & Semenza, G. L. 1995 Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 212, 550-556. (doi:10.1006/bbrc.1995.2005.)
    • (1995) Biochem. Biophys. Res. Commun , vol.212 , pp. 550-556
    • Wang, G.L.1    Jiang, B.H.2    Semenza, G.L.3
  • 75
    • 31544460550 scopus 로고    scopus 로고
    • Regulation of the multidrug resistance transporter P-glycoprotein in multicellular tumor spheroids by hypoxia inducible factor-1 and reactive oxygen species
    • Wartenberg, M. et al. 2003 Regulation of the multidrug resistance transporter P-glycoprotein in multicellular tumor spheroids by hypoxia inducible factor-1 and reactive oxygen species. FASEB J. 17, U546-U567.
    • (2003) FASEB J , vol.17
    • Wartenberg, M.1
  • 77
    • 0142144338 scopus 로고    scopus 로고
    • The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1 alpha and vascular endothelial growth factor formation
    • Welsh, S. J., Williams, R. R., Birmingham, A., Newman, D. J., Kirkpatrick, D. L. & Powis, G. 2003 The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1 alpha and vascular endothelial growth factor formation. Mol. Cancer Ther. 2, 235-243.
    • (2003) Mol. Cancer Ther , vol.2 , pp. 235-243
    • Welsh, S.J.1    Williams, R.R.2    Birmingham, A.3    Newman, D.J.4    Kirkpatrick, D.L.5    Powis, G.6
  • 78
    • 0036320934 scopus 로고    scopus 로고
    • 2-regulated gene expression
    • doi:10.1096/fj.01-0944rev
    • 2-regulated gene expression. FASEB J. 16, 1151-1162. (doi:10.1096/fj.01-0944rev.)
    • (2002) FASEB J , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 79
    • 0030583293 scopus 로고    scopus 로고
    • In vivo expression of mRNAs encoding hypoxia-inducible factor 1
    • doi:10.1006/bbrc.1996.1199
    • Wiener, C. M., Booth, G. & Semenza, G. L. 1996 In vivo expression of mRNAs encoding hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 225, 485-488. (doi:10.1006/bbrc.1996.1199.)
    • (1996) Biochem. Biophys. Res. Commun , vol.225 , pp. 485-488
    • Wiener, C.M.1    Booth, G.2    Semenza, G.L.3
  • 80
    • 0032189844 scopus 로고    scopus 로고
    • Induction of endothelial PAS domain protein-1 by hypoxia: Characterisation and comparison with hypoxia-inducible factor-1 alpha
    • Wiesener, M. S. et al. 1998 Induction of endothelial PAS domain protein-1 by hypoxia: characterisation and comparison with hypoxia-inducible factor-1 alpha. Blood 92, 2260-2268.
    • (1998) Blood , vol.92 , pp. 2260-2268
    • Wiesener, M.S.1
  • 81
    • 0037315337 scopus 로고    scopus 로고
    • Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs
    • Wiesener, M. S. et al. 2003 Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs. FASEB J. 17, 271-273.
    • (2003) FASEB J , vol.17 , pp. 271-273
    • Wiesener, M.S.1
  • 83
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1alpha expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics
    • Zhong, H., Chiles, K., Laughner, E., Hanrahan, C., Georgescu, M. M., Simons, J. W. & Semenza, G. L. 2000 Modulation of hypoxia-inducible factor 1alpha expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics. Cancer Res. 60, 1541-1545.
    • (2000) Cancer Res , vol.60 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Laughner, E.3    Hanrahan, C.4    Georgescu, M.M.5    Simons, J.W.6    Semenza, G.L.7


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