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Volumn 114, Issue 1, 1998, Pages 25-36

Cytochromes and oxygen radicals as putative members of the oxygen sensing pathway

Author keywords

Carotid body, O2 sensing signal pathways; Control of breathing, carotid body; Enzymes, cytochromes; Enzymes, NAD(P)H oxidase; Mammals, humans; Mediators, reactive oxygen species

Indexed keywords

CELL MEMBRANE PROTEIN; CHELATING AGENT; COBALT; CYTOCHROME; CYTOCHROME B; DEFEROXAMINE; FERROUS GLUCONATE; HYDROXYL RADICAL; MITOCHONDRIAL ENZYME; OXYGEN RADICAL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE;

EID: 0345368059     PISSN: 00345687     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0034-5687(98)00078-4     Document Type: Article
Times cited : (47)

References (30)
  • 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. 95:1994;1-10.
    • (1994) Respir. Physiol. , vol.95 , pp. 1-10
    • Acker, H.1
  • 2
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn H.F., Poyton R.O. Oxygen sensing and molecular adaptation to hypoxia. Phys. Rev. 76:1996;839-885.
    • (1996) Phys. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 3
    • 0030855493 scopus 로고    scopus 로고
    • Cellular respiration during hypoxia - Role of cytochrome-oxidase as the oxygen sensor in hepatocytes
    • Chandel N.S., Budinger G.R.S., Choe S.H., Schumacker P.T. Cellular respiration during hypoxia - role of cytochrome-oxidase as the oxygen sensor in hepatocytes. J. Biol. Chem. 272:1997;18808-18816.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18808-18816
    • Chandel, N.S.1    Budinger, G.R.S.2    Choe, S.H.3    Schumacker, P.T.4
  • 5
    • 0030045543 scopus 로고    scopus 로고
    • Isoenzyme-specific regulation of genes involved in energy metabolism by hypoxia: Similarities with the regulation of erythropoietin
    • Ebert B.L., Gleadle J.M., O'Rourke J.F., Bartlett S.M., Poulton J., Ratcliffe P.J. Isoenzyme-specific regulation of genes involved in energy metabolism by hypoxia: similarities with the regulation of erythropoietin. Biochem. J. 313:1996;809-814.
    • (1996) Biochem. J. , vol.313 , pp. 809-814
    • Ebert, B.L.1    Gleadle, J.M.2    O'Rourke, J.F.3    Bartlett, S.M.4    Poulton, J.5    Ratcliffe, P.J.6
  • 6
    • 0031029982 scopus 로고    scopus 로고
    • Cobalt and desferrioxamine reveal crucial members of the oxygen sensing pathway in HepG2 cells
    • Ehleben W., Porwol T., Fandrey J., Kummer W., Acker H. Cobalt and desferrioxamine reveal crucial members of the oxygen sensing pathway in HepG2 cells. Kidney Int. 51:1997;483-491.
    • (1997) Kidney Int. , vol.51 , pp. 483-491
    • Ehleben, W.1    Porwol, T.2    Fandrey, J.3    Kummer, W.4    Acker, H.5
  • 7
    • 0027970536 scopus 로고
    • Role of hydrogen-peroxide in hypoxia-induced erythropoietin production
    • Fandrey J., Frede S., Jelkmann W. Role of hydrogen-peroxide in hypoxia-induced erythropoietin production. Biochem. J. 303:1994;507-510.
    • (1994) Biochem. J. , vol.303 , pp. 507-510
    • Fandrey, J.1    Frede, S.2    Jelkmann, W.3
  • 8
    • 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. Cobalt chloride and desferrioxamine antagonize the inhibition of erythropoietin production by reactive oxygen species. Kidney Int. 51:1997;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
  • 9
    • 0028844810 scopus 로고
    • Diphenylene iodonium inhibits the induction of erythropoietin and other mammalian genes by hypoxia-implications for the mechanism of oxygen sensing
    • Gleadle J.M., Ebert B.L., Ratcliffe P.J. Diphenylene iodonium inhibits the induction of erythropoietin and other mammalian genes by hypoxia-implications for the mechanism of oxygen sensing. Eur. J. Biochem. 234:1995;92-99.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 92-99
    • Gleadle, J.M.1    Ebert, B.L.2    Ratcliffe, P.J.3
  • 10
    • 0027516683 scopus 로고
    • Photometric characteristics of haem proteins in erythropoietin producing hepatoma cells (HepG2)
    • Görlach A., Holtermann G., Jelkmann W. et al. Photometric characteristics of haem proteins in erythropoietin producing hepatoma cells (HepG2). Biochem. J. 290:1993;771-776.
    • (1993) Biochem. J. , vol.290 , pp. 771-776
    • Görlach, A.1    Holtermann, G.2    Jelkmann, W.3
  • 11
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene:evidence that the oxygen sensor is a heme protein
    • Goldberg M.A., Dunning S.P., Bunn H.F. Regulation of the erythropoietin gene:evidence that the oxygen sensor is a heme protein. Science. 242:1988;1412-1415.
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 12
    • 0028364576 scopus 로고
    • Biological origin of free radicals and mechanisms of antioxidant protection
    • Gutteridge J.M. Biological origin of free radicals and mechanisms of antioxidant protection. Chem. Biol. Interact. 91:1994;133-140.
    • (1994) Chem. Biol. Interact. , vol.91 , pp. 133-140
    • Gutteridge, J.M.1
  • 13
    • 0344622606 scopus 로고
    • The serial cultivation of human diploid strains
    • Hayflick L., Moorhead P.S. The serial cultivation of human diploid strains. Exp. Cell. Res. 25:1961;585-621.
    • (1961) Exp. Cell. Res. , vol.25 , pp. 585-621
    • Hayflick, L.1    Moorhead, P.S.2
  • 15
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its a subunit
    • Huang L.E., Arany Z., Livingston D.M., Bunn H.F. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its a subunit. J. Biol. Chem. 271:1996;32253-32259.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 17
    • 0024445290 scopus 로고
    • A comparison of cobalt(II) and iron(II) hydroxyl and superoxide free radical formation
    • Kadiiska M.B., Maples K.R., Mason R.P. A comparison of cobalt(II) and iron(II) hydroxyl and superoxide free radical formation. Arch. Biochem. Biophys. 275(1):1989;98-111.
    • (1989) Arch. Biochem. Biophys. , vol.275 , Issue.1 , pp. 98-111
    • Kadiiska, M.B.1    Maples, K.R.2    Mason, R.P.3
  • 19
    • 0029040451 scopus 로고
    • Immunohistochemical demonstration of 4 subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body
    • Kummer W., Acker H. Immunohistochemical demonstration of 4 subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body. J.Appl. Physiol. 78:1995;1904-1909.
    • (1995) J.Appl. Physiol. , vol.78 , pp. 1904-1909
    • Kummer, W.1    Acker, H.2
  • 20
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • Lander H.M. An essential role for free radicals and derived species in signal transduction. FASEB J. 11:1997;118-124.
    • (1997) FASEB J. , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 22
    • 0024425516 scopus 로고
    • Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α
    • Meier B., Radeke H.H., Selle S. et al. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α Biochem. J. 263:1989;539-545.
    • (1989) Biochem. J. , vol.263 , pp. 539-545
    • Meier, B.1    Radeke, H.H.2    Selle, S.3
  • 23
    • 0030441978 scopus 로고    scopus 로고
    • 3-D imaging of rhodamine 123 fluorescence distribution in human melanoma cells by means of confocal laser scanning microscopy
    • Porwol T., Merten E., Opitz N., Acker H. 3-D imaging of rhodamine 123 fluorescence distribution in human melanoma cells by means of confocal laser scanning microscopy. Acta Anat. 157:1996;116-125.
    • (1996) Acta Anat. , vol.157 , pp. 116-125
    • Porwol, T.1    Merten, E.2    Opitz, N.3    Acker, H.4
  • 24
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic-cells
    • Richardson D.R., Ponka P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic-cells. Biochim. Biophys. Acta-Rev. Biomembr. 1331:1997;1-40.
    • (1997) Biochim. Biophys. Acta-Rev. Biomembr. , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 26
    • 0030741295 scopus 로고    scopus 로고
    • Tomography of cells by confocal laser scanning microscopy and computer-assisted 3-dimensional image reconstruction: Localization of cathepsin B in tumor cells penetrating collagen gels in vitro
    • Strohmaier A.R., Porwol T., Acker H., Spiess E. Tomography of cells by confocal laser scanning microscopy and computer-assisted 3-dimensional image reconstruction: localization of cathepsin B in tumor cells penetrating collagen gels in vitro. J. Histochem. Cytochem. 45(7):1997;975-983.
    • (1997) J. Histochem. Cytochem. , vol.45 , Issue.7 , pp. 975-983
    • Strohmaier, A.R.1    Porwol, T.2    Acker, H.3    Spiess, E.4
  • 27
    • 0026316194 scopus 로고
    • Effect of inhibitors of oxidative phosphorylation on erythropoietin mRNA in isolated perfused rat kidneys
    • Tan C.C., Ratcliffe P.J. Effect of inhibitors of oxidative phosphorylation on erythropoietin mRNA in isolated perfused rat kidneys. Am. J. Physiol. 261(30):1991;982-986.
    • (1991) Am. J. Physiol. , vol.261 , Issue.30 , pp. 982-986
    • Tan, C.C.1    Ratcliffe, P.J.2
  • 28
    • 0029841060 scopus 로고    scopus 로고
    • + channel may function as an oxygen sensor complex in airway chemoreceptors and small-cell lung-carcinoma cell-lines
    • + channel may function as an oxygen sensor complex in airway chemoreceptors and small-cell lung-carcinoma cell-lines. PNAS. 93:1996;13182-13187.
    • (1996) PNAS , vol.93 , pp. 13182-13187
    • Wang, D.S.1    Youngson, C.2    Wong, V.3
  • 30
    • 0030612611 scopus 로고    scopus 로고
    • 2-sensing protein (nadph oxidase) in chemoreceptor cells
    • 2-sensing protein (nadph oxidase) in chemoreceptor cells. Micro Res. Tech. 37:1997;101-106.
    • (1997) Micro Res. Tech. , vol.37 , pp. 101-106
    • Youngson, C.1    Nurse, C.2    Yeger, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.