메뉴 건너뛰기




Volumn 177, Issue 6, 2007, Pages 1029-1036

The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CYTOCHROME B; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IRON SULFUR PROTEIN; REACTIVE OXYGEN METABOLITE; STIGMATELLIN; UBIQUINOL CYTOCHROME C REDUCTASE; MITOCHONDRIAL PROTEIN;

EID: 34250745912     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200609074     Document Type: Article
Times cited : (476)

References (49)
  • 1
    • 0035971220 scopus 로고    scopus 로고
    • Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension
    • Aragones, J., D.R. Jones, S. Martin, M.A. San Juan, A. Alfranca, F. Vidal, A. Vara, I. Merida, and M.O. Landazuri. 2001. Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension. J. Biol. Chem. 276:10548-10555.
    • (2001) J. Biol. Chem , vol.276 , pp. 10548-10555
    • Aragones, J.1    Jones, D.R.2    Martin, S.3    San Juan, M.A.4    Alfranca, A.5    Vidal, F.6    Vara, A.7    Merida, I.8    Landazuri, M.O.9
  • 2
    • 26444439977 scopus 로고    scopus 로고
    • Mitochondrial regulation of oxygen sensing
    • Bell, E.L., B.M. Emerling, and N.S. Chandel. 2005. Mitochondrial regulation of oxygen sensing. Mitochondrion. 5:322-332.
    • (2005) Mitochondrion , vol.5 , pp. 322-332
    • Bell, E.L.1    Emerling, B.M.2    Chandel, N.S.3
  • 3
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris, A., E. Cadenas, and A.O. Stoppani. 1976. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156:435-444.
    • (1976) Biochem. J , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 4
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R.K., and S.L. McKnight. 2001. A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 6
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas, E., A. Boveris, C.I. Ragan, and A.O. Stoppani. 1977. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180:248-257.
    • (1977) Arch. Biochem. Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 10
    • 27144528715 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact
    • Doege, K., S. Heine, I. Jensen, W. Jelkmann, and E. Metzen. 2005. Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact. Blood. 106:2311-2317.
    • (2005) Blood , vol.106 , pp. 2311-2317
    • Doege, K.1    Heine, S.2    Jensen, I.3    Jelkmann, W.4    Metzen, E.5
  • 12
    • 20344386238 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling
    • Emerling, B.M., L.C. Platanias, E. Black, A.R. Nebreda, R.J. Davis, and N.S. Chandel. 2005. Mitochondrial reactive oxygen species activation of p38 mitogen-activated protein kinase is required for hypoxia signaling. Mol. Cell. Biol. 25:4853-4862.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4853-4862
    • Emerling, B.M.1    Platanias, L.C.2    Black, E.3    Nebreda, A.R.4    Davis, R.J.5    Chandel, N.S.6
  • 13
    • 17944375360 scopus 로고    scopus 로고
    • Epstein, A.C., J.M. Gleadle, L.A. McNeill, K.S. Hewitson, J. O'Rourke, D.R. Mole, M. Mukherji, E. Metzen, M.I. Wilson, A. Dhanda, 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.
    • Epstein, A.C., J.M. Gleadle, L.A. McNeill, K.S. Hewitson, J. O'Rourke, D.R. Mole, M. Mukherji, E. Metzen, M.I. Wilson, A. Dhanda, 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.
  • 15
    • 0035929367 scopus 로고    scopus 로고
    • The site of production of superoxide radical in mitochondrial complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2
    • Genova, M.L., B. Ventura, G. Giuliano, C. Bovina, G. Formiggini, G. Parenti Castelli, and G. Lenaz. 2001. The site of production of superoxide radical in mitochondrial complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2. FEBS Lett. 505:364-368.
    • (2001) FEBS Lett , vol.505 , pp. 364-368
    • Genova, M.L.1    Ventura, B.2    Giuliano, G.3    Bovina, C.4    Formiggini, G.5    Parenti Castelli, G.6    Lenaz, G.7
  • 19
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1alpha
    • Hagen, T., C.T. Taylor, F. Lam, and S. Moncada. 2003. Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1alpha. Science. 302:1975-1978.
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 20
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • Han, D., E. Williams, and E. Cadenas. 2001. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 353:411-416.
    • (2001) Biochem. J , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 21
    • 0035877728 scopus 로고    scopus 로고
    • Rac1 activity is required for the activation of hypoxia-inducible factor 1
    • Hirota, K., and G.L. Semenza. 2001. Rac1 activity is required for the activation of hypoxia-inducible factor 1. J. Biol. Chem. 276:21166-21172.
    • (2001) J. Biol. Chem , vol.276 , pp. 21166-21172
    • Hirota, K.1    Semenza, G.L.2
  • 23
    • 0038730358 scopus 로고    scopus 로고
    • Protonmotive pathways and mechanisms in the cytochrome bc1 complex
    • Hunte, C., H. Palsdottir, and B.L. Trumpower. 2003. Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett. 545:39-46.
    • (2003) FEBS Lett , vol.545 , pp. 39-46
    • Hunte, C.1    Palsdottir, H.2    Trumpower, B.L.3
  • 26
    • 0036903625 scopus 로고    scopus 로고
    • Complex I-mediated reactive oxygen species generation: Modulation by cytochrome c and NAD(P)+ oxidation-reduction state
    • Kushnareva, Y., A.N. Murphy, and A. Andreyev. 2002. Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation-reduction state. Biochem. J. 368:545-553.
    • (2002) Biochem. J , vol.368 , pp. 545-553
    • Kushnareva, Y.1    Murphy, A.N.2    Andreyev, A.3
  • 27
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D., D.J. Peet, J.J. Gorman, D.A. Whelan, M.L. Whitelaw, and R.K. Bruick. 2002a. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16:1466-1471.
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 28
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • Lando, D., D.J. Peet, D.A. Whelan, J.J. Gorman, and M.L. Whitelaw. 2002b. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science. 295:858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 30
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology
    • Lenaz, G. 2001. The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life. 52:159-164.
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 31
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon, P.C., K. Hirota, and G.L. Semenza. 2001. FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15:2675-2686.
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 32
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation
    • Mansfield, K.D., R.D. Guzy, Y. Pan, R.M. Young, T.P. Cash, P.T. Schumacker, and M.C. Simon. 2005. Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation. Cell Metab. 1:393-399.
    • (2005) Cell Metab , vol.1 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 34
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F.L., Y. Liu, and H. Van Remmen. 2004. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279:49064-49073.
    • (2004) J. Biol. Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 36
    • 33846630894 scopus 로고    scopus 로고
    • Multiple factors affecting cellular redox status and energy metabolism modulate HIF prolyl hydroxylase activity in vivo and in vitro
    • Pan, Y., K.D. Mansfield, C.C. Bertozzi, V. Rudenko, D.A. Chan, A.J. Giaccia, and M.C. Simon. 2006. Multiple factors affecting cellular redox status and energy metabolism modulate HIF prolyl hydroxylase activity in vivo and in vitro. Mol. Cell. Biol. 27:912-925.
    • (2006) Mol. Cell. Biol , vol.27 , pp. 912-925
    • Pan, Y.1    Mansfield, K.D.2    Bertozzi, C.C.3    Rudenko, V.4    Chan, D.A.5    Giaccia, A.J.6    Simon, M.C.7
  • 37
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in realtime RT-PCR
    • Pfaffl, M.W. 2001. A new mathematical model for relative quantification in realtime RT-PCR. Nucleic Acids Res. 29:e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 38
    • 0033767317 scopus 로고    scopus 로고
    • An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production
    • Rana, M., I. de Coo, F. Diaz, H. Smeets, and C.T. Moraes. 2000. An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production. Ann. Neurol. 48:774-781.
    • (2000) Ann. Neurol , vol.48 , pp. 774-781
    • Rana, M.1    de Coo, I.2    Diaz, F.3    Smeets, H.4    Moraes, C.T.5
  • 39
    • 18144378426 scopus 로고    scopus 로고
    • A targeted antioxidant reveals the importance of mitochondrial reactive oxygen species in the hypoxic signaling of HIF-1α
    • Sanjuan-Pla, A., A.M. Cervera, N. Apostolova, R. Garcia-Bou, V.M. Victor, M.P. Murphy, and K.J. McCreath. 2005. A targeted antioxidant reveals the importance of mitochondrial reactive oxygen species in the hypoxic signaling of HIF-1α. FEBS Lett. 579:2669-2674.
    • (2005) FEBS Lett , vol.579 , pp. 2669-2674
    • Sanjuan-Pla, A.1    Cervera, A.M.2    Apostolova, N.3    Garcia-Bou, R.4    Victor, V.M.5    Murphy, M.P.6    McCreath, K.J.7
  • 41
    • 0034663989 scopus 로고    scopus 로고
    • HIF-1 and human disease: One highly involved factor
    • Semenza, G.L. 2000. HIF-1 and human disease: one highly involved factor. Genes Dev. 14:1983-1991.
    • (2000) Genes Dev , vol.14 , pp. 1983-1991
    • Semenza, G.L.1
  • 43
    • 0038348531 scopus 로고    scopus 로고
    • HIF-1alpha mRNA and protein upregulation involves Rho GTPase expression during hypoxia in renal cell carcinoma
    • Turcotte, S., R.R. Desrosiers, and R. Beliveau. 2003. HIF-1alpha mRNA and protein upregulation involves Rho GTPase expression during hypoxia in renal cell carcinoma. J. Cell Sci. 116:2247-2260.
    • (2003) J. Cell Sci , vol.116 , pp. 2247-2260
    • Turcotte, S.1    Desrosiers, R.R.2    Beliveau, R.3
  • 44
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J.F. 2003. Mitochondrial formation of reactive oxygen species. J. Physiol. 552:335-344.
    • (2003) J. Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 45
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens, J.F., and A. Boveris. 1980. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191:421-427.
    • (1980) Biochem. J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 46
    • 0020397137 scopus 로고
    • The effect of hyperoxia on superoxide production by lung submitochondrial particles
    • Turrens, J.F., B.A. Freeman, J.G. Levitt, and J.D. Crapo. 1982. The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch. Biochem. Biophys. 217:401-410.
    • (1982) Arch. Biochem. Biophys , vol.217 , pp. 401-410
    • Turrens, J.F.1    Freeman, B.A.2    Levitt, J.G.3    Crapo, J.D.4
  • 47
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens, J.F., A. Alexandre, and A.L. Lehninger. 1985. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237:408-414.
    • (1985) Arch. Biochem. Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 49
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinatecytochrome c reductase from bovine heart mitochondria
    • Zhang, L., L. Yu, and C.A. Yu. 1998. Generation of superoxide anion by succinatecytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273:33972-33976.
    • (1998) J. Biol. Chem , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.