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Volumn 2, Issue 2, 2007, Pages 177-186

Comparison of hypoxia-inducible factor-1 alpha in hypoxia-sensitive and hypoxia-tolerant fish species

Author keywords

Evolution; Hydroxylation; Oxygen; Teleost fish; Transcription factor

Indexed keywords

HYPOXIA INDUCIBLE FACTOR 1ALPHA; OXYGEN;

EID: 34247473555     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2007.03.001     Document Type: Article
Times cited : (69)

References (55)
  • 1
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr. Opin. Struct. Biol. 14 (2004) 679-686
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 679-686
    • Barford, D.1
  • 2
    • 0032724622 scopus 로고    scopus 로고
    • Mechanisms for redox control of gene expression
    • Bauer C.E., Elsen S., and Bird T.H. Mechanisms for redox control of gene expression. Annu. Rev. Microbiol. 53 (1999) 495-523
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 495-523
    • Bauer, C.E.1    Elsen, S.2    Bird, T.H.3
  • 3
    • 26444482460 scopus 로고    scopus 로고
    • Molecular phylogeny and divergence times of deuterostome animals
    • Blair J.E., and Hedges S.B. Molecular phylogeny and divergence times of deuterostome animals. Mol. Biol. Evol. 22 (2005) 2275-2284
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2275-2284
    • Blair, J.E.1    Hedges, S.B.2
  • 4
    • 0035012870 scopus 로고    scopus 로고
    • Reactive oxygen species regulate oxygen-sensitive potassium flux in rainbow trout erythrocytes
    • Bogdanova A., and Nikinmaa M. Reactive oxygen species regulate oxygen-sensitive potassium flux in rainbow trout erythrocytes. J. Gen. Physiol. 117 (2001) 181-190
    • (2001) J. Gen. Physiol. , vol.117 , pp. 181-190
    • Bogdanova, A.1    Nikinmaa, M.2
  • 6
    • 0015894781 scopus 로고
    • Oxygen dissociation and content of blood from Alaskan burbot (Lota lota), pike (Esox lucius) and grayling (Thymallus arcticus)
    • Cameron J.N. Oxygen dissociation and content of blood from Alaskan burbot (Lota lota), pike (Esox lucius) and grayling (Thymallus arcticus). Comp. Biochem. Physiol. A 46 (1973) 491-496
    • (1973) Comp. Biochem. Physiol. A , vol.46 , pp. 491-496
    • Cameron, J.N.1
  • 8
    • 0034910849 scopus 로고    scopus 로고
    • Implications of hypoxia for the brain size and gill morphometry of mormyrid fishes
    • Chapman L.J., and Hulen K.G. Implications of hypoxia for the brain size and gill morphometry of mormyrid fishes. J. Zool. 254 (2001) 461-472
    • (2001) J. Zool. , vol.254 , pp. 461-472
    • Chapman, L.J.1    Hulen, K.G.2
  • 14
    • 33748187417 scopus 로고    scopus 로고
    • Regulating cellular oxygen sensing by hydroxylation
    • Fandrey J., Gorr T.A., and Gassmann M. Regulating cellular oxygen sensing by hydroxylation. Cardiovasc. Res. 71 (2006) 642-651
    • (2006) Cardiovasc. Res. , vol.71 , pp. 642-651
    • Fandrey, J.1    Gorr, T.A.2    Gassmann, M.3
  • 15
    • 0033029038 scopus 로고    scopus 로고
    • Evolution of the vertebrate cardio-pulmonary system
    • Farmer C.G. Evolution of the vertebrate cardio-pulmonary system. Annu. Rev. Physiol. 61 (1999) 573-592
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 573-592
    • Farmer, C.G.1
  • 16
    • 0345047703 scopus 로고    scopus 로고
    • Modelling the habitat preferences of preadult and adult fishes on the shoreline of the large, lowland Elbe River
    • Fladung E., Scholten M., and Thiel R. Modelling the habitat preferences of preadult and adult fishes on the shoreline of the large, lowland Elbe River. J. Appl. Ichtyol. 19 (2003) 303-314
    • (2003) J. Appl. Ichtyol. , vol.19 , pp. 303-314
    • Fladung, E.1    Scholten, M.2    Thiel, R.3
  • 17
    • 0344845350 scopus 로고    scopus 로고
    • Long-term investigations of migratory behaviour of asp (Aspius aspius L.) in the middle part of the Elbe River, Germany
    • Friedrich F. Long-term investigations of migratory behaviour of asp (Aspius aspius L.) in the middle part of the Elbe River, Germany. J. Appl. Ichthyol. 19 (2003) 294-302
    • (2003) J. Appl. Ichthyol. , vol.19 , pp. 294-302
    • Friedrich, F.1
  • 18
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger R.P. Fe(II)/alpha-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. 39 (2004) 21-68
    • (2004) Crit. Rev. Biochem. Mol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 19
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., and Myllyharju J. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278 (2003) 30772-30780
    • (2003) J. Biol. Chem. , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 23
    • 0033247080 scopus 로고    scopus 로고
    • Proposed habitats of early tetrapods: gills, kidneys, and the water-land transition
    • Janis C.M., and Farmer C. Proposed habitats of early tetrapods: gills, kidneys, and the water-land transition. Zool. J. Linn. Soc. -Lond. 126 (1999) 117-126
    • (1999) Zool. J. Linn. Soc. -Lond. , vol.126 , pp. 117-126
    • Janis, C.M.1    Farmer, C.2
  • 24
    • 0034940761 scopus 로고    scopus 로고
    • The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is required for adaptation to hypoxia
    • Jiang H.Q., Guo R., and Powell-Coffman J.A. The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is required for adaptation to hypoxia. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7916-7921
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7916-7921
    • Jiang, H.Q.1    Guo, R.2    Powell-Coffman, J.A.3
  • 25
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1a
    • Kallio P.J., Okamoto K., O'Brien S., Carrero P., Makino Y., Tanaka H., and Poellinger L. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1a. EMBO J. 17 (1998) 6573-6586
    • (1998) EMBO J. , vol.17 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'Brien, S.3    Carrero, P.4    Makino, Y.5    Tanaka, H.6    Poellinger, L.7
  • 26
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases
    • Koivunen P., Hirsila M., Gunzler V., Kivirikko K.I., and Myllyharju J. Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. J. Biol. Chem. 279 (2004) 9899-9904
    • (2004) J. Biol. Chem. , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsila, M.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 27
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    • Koivunen P., Hirsila M., Kivirikko K.I., and Myllyharju J. The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases. J. Biol. Chem. 281 (2006) 28712-28720
    • (2006) J. Biol. Chem. , vol.281 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 28
    • 0036273419 scopus 로고    scopus 로고
    • Evidence for a slowed rate of molecular evolution in the order Acipenseriformes
    • Krieger J., and Fuerst P.A. Evidence for a slowed rate of molecular evolution in the order Acipenseriformes. Mol. Biol. Evol. 19 (2002) 891-897
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 891-897
    • Krieger, J.1    Fuerst, P.A.2
  • 29
    • 0032580152 scopus 로고    scopus 로고
    • A molecular timescale for vertebrate evolution
    • Kumar S., and Hedges S.B. A molecular timescale for vertebrate evolution. Nature 392 (1998) 917-920
    • (1998) Nature , vol.392 , pp. 917-920
    • Kumar, S.1    Hedges, S.B.2
  • 30
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5 (2004) 150-163
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 31
    • 0034681378 scopus 로고    scopus 로고
    • A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1 alpha and the HIF-like factor
    • Lando D., Pongratz I., Poellinger L., and Whitelaw M.L. A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1 alpha and the HIF-like factor. J. Biol. Chem. 275 (2000) 4618-4627
    • (2000) J. Biol. Chem. , vol.275 , pp. 4618-4627
    • Lando, D.1    Pongratz, I.2    Poellinger, L.3    Whitelaw, M.L.4
  • 32
    • 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. Gene Dev. 16 (2002) 1466-1471
    • (2002) Gene 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
  • 33
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch
    • Lando D., Peet D.J., Whelan D.A., Gorman J.J., and Whitelaw M.L. Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295 (2002) 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
  • 34
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson N., Willam C., Maxwell P.H., Pugh C.W., and Ratcliffe P.J. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 20 (2001) 5197-5206
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 36
    • 0030012683 scopus 로고    scopus 로고
    • The Drosophila melanogaster similar bHLH-PAS gene encodes a protein related to human hypoxia-inducible factor 1 alpha and Drosophila single-minded
    • Nambu J.R., Chen W., Hu S., and Crews S.T. The Drosophila melanogaster similar bHLH-PAS gene encodes a protein related to human hypoxia-inducible factor 1 alpha and Drosophila single-minded. Gene 172 (1996) 249-254
    • (1996) Gene , vol.172 , pp. 249-254
    • Nambu, J.R.1    Chen, W.2    Hu, S.3    Crews, S.T.4
  • 37
    • 0036024287 scopus 로고    scopus 로고
    • Oxygen-dependent cellular functions - why fishes and their aquatic environment are a prime choice of study
    • Nikinmaa M. Oxygen-dependent cellular functions - why fishes and their aquatic environment are a prime choice of study. Comp. Biochem. Physiol. A 133 (2002) 1-16
    • (2002) Comp. Biochem. Physiol. A , vol.133 , pp. 1-16
    • Nikinmaa, M.1
  • 38
    • 17844372978 scopus 로고    scopus 로고
    • Oxygen-dependent gene expression in fishes
    • Nikinmaa M., and Rees B.B. Oxygen-dependent gene expression in fishes. Am. J. Physiol. - Reg. I. 288 (2005) R1079-R1090
    • (2005) Am. J. Physiol. - Reg. I. , vol.288
    • Nikinmaa, M.1    Rees, B.B.2
  • 39
    • 2642536298 scopus 로고    scopus 로고
    • Redox state regulates HIF-1 alpha and its DNA binding and phosphorylation in salmonid cells
    • Nikinmaa M., Pursiheimo S., and Soitamo A.J. Redox state regulates HIF-1 alpha and its DNA binding and phosphorylation in salmonid cells. J. Cell Sci. 117 (2004) 3201-3206
    • (2004) J. Cell Sci. , vol.117 , pp. 3201-3206
    • Nikinmaa, M.1    Pursiheimo, S.2    Soitamo, A.J.3
  • 40
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
    • Ohh M., Park C.W., Ivan N., Hoffman M.A., Kim T.Y., Huang L.E., Pavletich N., Chau V., and Kaelin W.G. Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat. Cell Biol. 2 (2000) 423-427
    • (2000) Nat. Cell Biol. , vol.2 , pp. 423-427
    • Ohh, M.1    Park, C.W.2    Ivan, N.3    Hoffman, M.A.4    Kim, T.Y.5    Huang, L.E.6    Pavletich, N.7    Chau, V.8    Kaelin, W.G.9
  • 42
    • 0037974523 scopus 로고    scopus 로고
    • Functional genomics and the comparative physiology of hypoxia
    • Powell F.L. Functional genomics and the comparative physiology of hypoxia. Annu. Rev. Physiol. 65 (2003) 203-230
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 203-230
    • Powell, F.L.1
  • 43
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Krawetz S., and Misener S. (Eds), Humana Press, Totowa, NJ
    • Rozen S., and Skaletsky H.J. Primer3 on the WWW for general users and for biologist programmers. In: Krawetz S., and Misener S. (Eds). Bioinformatics Methods and Protocols: Methods in Molecular Biology (2000), Humana Press, Totowa, NJ 365-386
    • (2000) Bioinformatics Methods and Protocols: Methods in Molecular Biology , pp. 365-386
    • Rozen, S.1    Skaletsky, H.J.2
  • 44
    • 24344443670 scopus 로고    scopus 로고
    • Hypoxia-dependent activation of HIF into a transcriptional regulator
    • Ruas J.L., and Poellinger L. Hypoxia-dependent activation of HIF into a transcriptional regulator. Semin. Cell Dev. Biol. 16 (2005) 514-522
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 514-522
    • Ruas, J.L.1    Poellinger, L.2
  • 46
    • 0034006016 scopus 로고    scopus 로고
    • HIF-1: mediator of physiological and pathophysiological responses to hypoxia
    • Semenza G.L. HIF-1: mediator of physiological and pathophysiological responses to hypoxia. J. Appl. Physiol. 88 (2000) 1474-1480
    • (2000) J. Appl. Physiol. , vol.88 , pp. 1474-1480
    • Semenza, G.L.1
  • 47
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G.L. Targeting HIF-1 for cancer therapy. Nat. Rev., Cancer 3 (2003) 721-732
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 48
    • 0035827617 scopus 로고    scopus 로고
    • Characterization of a hypoxia-inducible factor (HIF-1a) from rainbow trout. Accumulation of protein occurs at normal venous oxygen tension
    • Soitamo A.J., Rabergh C.M.I., Gassmann M., Sistonen L., and Nikinmaa M. Characterization of a hypoxia-inducible factor (HIF-1a) from rainbow trout. Accumulation of protein occurs at normal venous oxygen tension. J. Biol. Chem. 276 (2001) 19699-19705
    • (2001) J. Biol. Chem. , vol.276 , pp. 19699-19705
    • Soitamo, A.J.1    Rabergh, C.M.I.2    Gassmann, M.3    Sistonen, L.4    Nikinmaa, M.5
  • 49
    • 12244255369 scopus 로고    scopus 로고
    • Are genome evolution, organism complexity and species diversity linked?
    • Stellwag E.J. Are genome evolution, organism complexity and species diversity linked?. Int. Comp. Biol. 44 (2004) 358-365
    • (2004) Int. Comp. Biol. , vol.44 , pp. 358-365
    • Stellwag, E.J.1
  • 51
    • 0027968068 scopus 로고
    • Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. Clustal-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0029400202 scopus 로고
    • Oxygen transfer in fish: morphological and molecular adjustments
    • Val A.L. Oxygen transfer in fish: morphological and molecular adjustments. Braz. J. Med. Biol. Res. 28 (1995) 1119-1127
    • (1995) Braz. J. Med. Biol. Res. , vol.28 , pp. 1119-1127
    • Val, A.L.1
  • 53
    • 0016766373 scopus 로고
    • Oxygenation properties of hemoglobins from flatfish plaice (Pleuronectes platessa) and flounder (Platichthys flesus)
    • Weber R.E., and Dewilde J.A.M. Oxygenation properties of hemoglobins from flatfish plaice (Pleuronectes platessa) and flounder (Platichthys flesus). J. Comp. Physiol. 101 (1975) 99-110
    • (1975) J. Comp. Physiol. , vol.101 , pp. 99-110
    • Weber, R.E.1    Dewilde, J.A.M.2
  • 54
    • 0034107952 scopus 로고    scopus 로고
    • Mammalian oxygen sensing, signalling and gene regulation
    • Wenger R.H. Mammalian oxygen sensing, signalling and gene regulation. J. Exp. Biol. 203 (2000) 1253-1263
    • (2000) J. Exp. Biol. , vol.203 , pp. 1253-1263
    • Wenger, R.H.1
  • 55
    • 22444433668 scopus 로고    scopus 로고
    • Oxidant and redox signaling in vascular oxygen sensing mechanisms: basic concepts, current controversies, and potential importance of cytosolic NADPH
    • Wolin M.S., Ahmad M., and Gupte S.A. Oxidant and redox signaling in vascular oxygen sensing mechanisms: basic concepts, current controversies, and potential importance of cytosolic NADPH. Am. J. Physiol. 289 (2005) L159-L173
    • (2005) Am. J. Physiol. , vol.289
    • Wolin, M.S.1    Ahmad, M.2    Gupte, S.A.3


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