메뉴 건너뛰기




Volumn 129, Issue 1, 2007, Pages 111-122

HIF-1 Regulates Cytochrome Oxidase Subunits to Optimize Efficiency of Respiration in Hypoxic Cells

Author keywords

CELLBIO; HUMDISEASE; RNA

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYTOCHROME C OXIDASE; ENDOPEPTIDASE LA; HYPOXIA INDUCIBLE FACTOR 1; ISOPROTEIN; OXYGEN; PROTEIN COX4 1; PROTEIN COX4 2; PROTEIN SUBUNIT; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 33947724515     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.01.047     Document Type: Article
Times cited : (1002)

References (43)
  • 1
    • 0028871222 scopus 로고
    • Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of yeast cytochrome c
    • Allen L.A., Zhao X.-J., Caughey W., and Poyton R.O. Isoforms of yeast cytochrome c oxidase subunit V affect the binuclear reaction center and alter the kinetics of interaction with the isoforms of yeast cytochrome c. J. Biol. Chem. 270 (1995) 110-118
    • (1995) J. Biol. Chem. , vol.270 , pp. 110-118
    • Allen, L.A.1    Zhao, X.-J.2    Caughey, W.3    Poyton, R.O.4
  • 2
    • 33745155785 scopus 로고    scopus 로고
    • An abnormal mitochondrial-hypoxia inducible factor-1α-Kv channel pathway disrupts oxygen sensing and triggers pulmonary arterial hypertension in fawn hooded rats: similarities to human pulmonary arterial hypertension
    • Bonnet S., Michelakis E.D., Porter C.J., Andrade-Navarro M.A., Thebaud B., Bonnet S., Haromy A., Harry G., Moudgil R., McMurtry M.S., et al. An abnormal mitochondrial-hypoxia inducible factor-1α-Kv channel pathway disrupts oxygen sensing and triggers pulmonary arterial hypertension in fawn hooded rats: similarities to human pulmonary arterial hypertension. Circulation 113 (2006) 2630-2641
    • (2006) Circulation , vol.113 , pp. 2630-2641
    • Bonnet, S.1    Michelakis, E.D.2    Porter, C.J.3    Andrade-Navarro, M.A.4    Thebaud, B.5    Bonnet, S.6    Haromy, A.7    Harry, G.8    Moudgil, R.9    McMurtry, M.S.10
  • 3
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • Bruick R.K. Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc. Natl. Acad. Sci. USA 97 (2000) 9082-9087
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 5
    • 0032052215 scopus 로고    scopus 로고
    • Structure/function of oxygen-regulated isoforms in cytochrome c oxidase
    • Burke P.V., and Poyton R.O. Structure/function of oxygen-regulated isoforms in cytochrome c oxidase. J. Exp. Biol. 201 (1998) 1163-1175
    • (1998) J. Exp. Biol. , vol.201 , pp. 1163-1175
    • Burke, P.V.1    Poyton, R.O.2
  • 7
    • 0024467192 scopus 로고
    • Communication between mitochondria and the nucleus in regulation of cytochrome genes in the yeast Saccharomyces cerevisiae
    • Forsburg S.L., and Guarente L. Communication between mitochondria and the nucleus in regulation of cytochrome genes in the yeast Saccharomyces cerevisiae. Annu. Rev. Cell Biol. 5 (1989) 153-180
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 153-180
    • Forsburg, S.L.1    Guarente, L.2
  • 11
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation
    • Hu C.J., Wang L.Y., Chodosh L.A., Keith B., and Simon M.C. Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation. Mol. Cell. Biol. 23 (2003) 9361-9374
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9361-9374
    • Hu, C.J.1    Wang, L.Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 12
    • 0035804655 scopus 로고    scopus 로고
    • Mammalian subunit IV isoforms of cytochrome c oxidase
    • Hutteman M., Kadenbach B., and Grossman L.I. Mammalian subunit IV isoforms of cytochrome c oxidase. Gene 267 (2001) 111-123
    • (2001) Gene , vol.267 , pp. 111-123
    • Hutteman, M.1    Kadenbach, B.2    Grossman, L.I.3
  • 16
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang B.-H., Rue E., Wang G.L., Roe R., and Semenza G.L. 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
  • 17
    • 0344874751 scopus 로고    scopus 로고
    • Cell type-specific regulation of angiogenic growth factor gene expression and induction of angiogenesis in nonischemic tissue by a constitutively active form of hypoxia-inducible factor 1
    • Kelly B.D., Hackett S.F., Hirota K., Oshima Y., Cai Z., Berg-Dixon S., Rowan A., Yan Z., Campochiaro P.A., and Semenza G.L. Cell type-specific regulation of angiogenic growth factor gene expression and induction of angiogenesis in nonischemic tissue by a constitutively active form of hypoxia-inducible factor 1. Circ. Res. 93 (2003) 1074-1081
    • (2003) Circ. Res. , vol.93 , pp. 1074-1081
    • Kelly, B.D.1    Hackett, S.F.2    Hirota, K.3    Oshima, Y.4    Cai, Z.5    Berg-Dixon, S.6    Rowan, A.7    Yan, Z.8    Campochiaro, P.A.9    Semenza, G.L.10
  • 18
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia
    • Kim J.W., Tchernyshyov I., Semenza G.L., and Dang C.V. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab. 3 (2006) 177-185
    • (2006) Cell Metab. , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 19
    • 0346655211 scopus 로고    scopus 로고
    • BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1α
    • Kim J.Y., Ahn H.J., Ryu J.H., Suk K., and Park J.H. BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1α. J. Exp. Med. 199 (2004) 113-124
    • (2004) J. Exp. Med. , vol.199 , pp. 113-124
    • Kim, J.Y.1    Ahn, H.J.2    Ryu, J.H.3    Suk, K.4    Park, J.H.5
  • 20
    • 33645090169 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent repression of E-cadherin in von Hippel-Lindau tumor suppressor-null renal cell carcinoma mediated by TCF3, ZFHX1A, and ZFHX1B
    • Krishnamachary B., Zagzag D., Nagasawa H., Rainey K., Okuyama H., Baek J.H., and Semenza G.L. Hypoxia-inducible factor-1-dependent repression of E-cadherin in von Hippel-Lindau tumor suppressor-null renal cell carcinoma mediated by TCF3, ZFHX1A, and ZFHX1B. Cancer Res. 66 (2006) 2725-2731
    • (2006) Cancer Res. , vol.66 , pp. 2725-2731
    • Krishnamachary, B.1    Zagzag, D.2    Nagasawa, H.3    Rainey, K.4    Okuyama, H.5    Baek, J.H.6    Semenza, G.L.7
  • 21
    • 0032052761 scopus 로고    scopus 로고
    • Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast
    • Kwast K.E., Burke P.V., and Poyton R.O. Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast. J. Exp. Biol. 201 (1998) 1177-1195
    • (1998) J. Exp. Biol. , vol.201 , pp. 1177-1195
    • Kwast, K.E.1    Burke, P.V.2    Poyton, R.O.3
  • 22
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., and Bruick R.K. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16 (2002) 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
  • 23
    • 4544361863 scopus 로고    scopus 로고
    • Induction of ID2 expression by hypoxia-inducible factor-1: a role in dedifferentiation of hypoxic neuroblastoma cells
    • Lofstedt T., Jogi A., Sigvardsson M., Gradin K., Poellinger L., Pahlman S., and Axelson H. Induction of ID2 expression by hypoxia-inducible factor-1: a role in dedifferentiation of hypoxic neuroblastoma cells. J. Biol. Chem. 279 (2004) 39223-39231
    • (2004) J. Biol. Chem. , vol.279 , pp. 39223-39231
    • Lofstedt, T.1    Jogi, A.2    Sigvardsson, M.3    Gradin, K.4    Poellinger, L.5    Pahlman, S.6    Axelson, H.7
  • 24
    • 0346468275 scopus 로고
    • Oxygen regulation of anaerobic and aerobic genes mediated by a common factor in yeast
    • Lowry C.V., and Zitomer R.S. Oxygen regulation of anaerobic and aerobic genes mediated by a common factor in yeast. Proc. Natl. Acad. Sci. USA 81 (1984) 6129-6133
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6129-6133
    • Lowry, C.V.1    Zitomer, R.S.2
  • 25
    • 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., Guzy R.D., Pan Y., Young R.M., Cash T.P., Schumacker P.T., and Simon M.C. Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation. Cell Metab. 1 (2005) 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
  • 27
    • 0022976206 scopus 로고
    • Nuclear functions required for cytochrome c oxidase biogenesis in Saccharomyces cerevisiae
    • McEwen J.E., Ko C., Kloeckener-Gruissem B., and Poyton R.O. Nuclear functions required for cytochrome c oxidase biogenesis in Saccharomyces cerevisiae. J. Biol. Chem. 261 (1986) 11872-11879
    • (1986) J. Biol. Chem. , vol.261 , pp. 11872-11879
    • McEwen, J.E.1    Ko, C.2    Kloeckener-Gruissem, B.3    Poyton, R.O.4
  • 28
    • 0034647742 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
    • Mukhopadhyay C.K., Mazumder B., and Fox P.L. Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency. J. Biol. Chem. 275 (2000) 21048-21054
    • (2000) J. Biol. Chem. , vol.275 , pp. 21048-21054
    • Mukhopadhyay, C.K.1    Mazumder, B.2    Fox, P.L.3
  • 29
    • 0031924141 scopus 로고    scopus 로고
    • Extramitochondrial ATP/ADP ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV
    • Napiwotzki J., and Kadenbach B. Extramitochondrial ATP/ADP ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV. Biol. Chem. 379 (1998) 335-339
    • (1998) Biol. Chem. , vol.379 , pp. 335-339
    • Napiwotzki, J.1    Kadenbach, B.2
  • 31
    • 33744959141 scopus 로고    scopus 로고
    • Expression of vascular endothelial growth factor receptor 1 in bone marrow-derived mesenchymal cells is dependent on hypoxia-inducible factor 1
    • Okuyama H., Krishnamachary B., Zhou Y.F., Nagasawa H., Bosch-Marce M., and Semenza G.L. Expression of vascular endothelial growth factor receptor 1 in bone marrow-derived mesenchymal cells is dependent on hypoxia-inducible factor 1. J. Biol. Chem. 281 (2006) 15554-15563
    • (2006) J. Biol. Chem. , vol.281 , pp. 15554-15563
    • Okuyama, H.1    Krishnamachary, B.2    Zhou, Y.F.3    Nagasawa, H.4    Bosch-Marce, M.5    Semenza, G.L.6
  • 32
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I., Cairns R.A., Fontana L., Lim A.L., and Denko N.C. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab. 3 (2006) 187-197
    • (2006) Cell Metab. , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 33
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda S., and Caro J. Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J. Biol. Chem. 272 (1997) 22642-22647
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 35
    • 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
    • Semenza G.L., Jiang B.-H., Leung S.W., Passantino R., Concordet J.-P., Maire P., and Giallongo A. 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
  • 36
    • 0030021835 scopus 로고    scopus 로고
    • The mouse gene for vascular endothelial growth factor. Genomic structure, definition of the transcriptional unit, and characterization of transcriptional and post-transcriptional regulatory sequences
    • Shima D.T., Kuroki M., Deutsch U., Ng Y.S., Adamis A.P., and D'Amore P. The mouse gene for vascular endothelial growth factor. Genomic structure, definition of the transcriptional unit, and characterization of transcriptional and post-transcriptional regulatory sequences. J. Biol. Chem. 271 (1996) 3877-3883
    • (1996) J. Biol. Chem. , vol.271 , pp. 3877-3883
    • Shima, D.T.1    Kuroki, M.2    Deutsch, U.3    Ng, Y.S.4    Adamis, A.P.5    D'Amore, P.6
  • 37
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H., McKnight S.L., and Russell D.W. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 11 (1997) 72-82
    • (1997) Genes Dev. , vol.11 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 41
    • 0025877222 scopus 로고
    • The isoforms of yeast cytochrome c oxidase alter the in vivo kinetic properties of the holoenzyme
    • Waterland R.A., Basu A., Chance B., and Poyton R.O. The isoforms of yeast cytochrome c oxidase alter the in vivo kinetic properties of the holoenzyme. J. Biol. Chem. 266 (1991) 4180-4186
    • (1991) J. Biol. Chem. , vol.266 , pp. 4180-4186
    • Waterland, R.A.1    Basu, A.2    Chance, B.3    Poyton, R.O.4
  • 43
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
    • Yu F., White S.B., Zhao Q., and Lee F.S. HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc. Natl. Acad. Sci. USA 98 (2001) 9630-9635
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Zhao, Q.3    Lee, F.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.