메뉴 건너뛰기




Volumn 62, Issue 19, 2002, Pages 5436-5442

Oxidative metabolism modulates signal transduction and micronucleus formation in bystander cells from α-particle-irradiated normal human fibroblast cultures

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P21; PROTEIN P53; RAF PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1;

EID: 0036791114     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (305)

References (66)
  • 1
    • 0026454677 scopus 로고
    • Induction of sister chromatid exchanges by extremely low doses of α-particles
    • Nagasawa, H., and Little, J. B. Induction of sister chromatid exchanges by extremely low doses of α-particles. Cancer Res., 52: 6394-6396, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 6394-6396
    • Nagasawa, H.1    Little, J.B.2
  • 2
    • 0029938045 scopus 로고    scopus 로고
    • α-particle-induced sister chromatid exchange in normal human lung fibroblasts: Evidence for an extranuclear target
    • Deshpande, A, Goodwin, E. H., Bailey, S. M., Marrone, B. L., and Lehnert, B. E. α-Particle-induced sister chromatid exchange in normal human lung fibroblasts: evidence for an extranuclear target. Radiat. Res., 145: 260-267, 1996.
    • (1996) Radiat. Res. , vol.145 , pp. 260-267
    • Deshpande, A.1    Goodwin, E.H.2    Bailey, S.M.3    Marrone, B.L.4    Lehnert, B.E.5
  • 3
    • 0030898609 scopus 로고    scopus 로고
    • Medium from irradiated human epithelial cells but not human fibroblasts reduces the clonogenic survival of unirradiated cells
    • Mothersill, C., and Seymour, C. Medium from irradiated human epithelial cells but not human fibroblasts reduces the clonogenic survival of unirradiated cells. Int. J. Radiat. Biol., 71: 421-427, 1997.
    • (1997) Int. J. Radiat. Biol. , vol.71 , pp. 421-427
    • Mothersill, C.1    Seymour, C.2
  • 4
    • 0028171451 scopus 로고
    • α-particle-induced p53 protein expression in a rat lung epithelial cell strain
    • Hickman, A. W., Jaramillo, R. J., Lechner, J. F., and Johnson, N. F. α-Particle-induced p53 protein expression in a rat lung epithelial cell strain. Cancer Res., 54: 5797-5800, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 5797-5800
    • Hickman, A.W.1    Jaramillo, R.J.2    Lechner, J.F.3    Johnson, N.F.4
  • 5
    • 0031770716 scopus 로고    scopus 로고
    • Intercellular communication is involved in the bystander regulation of gene expression in human cells exposed to very low fluences of α particles
    • Azzam, E. I., de Toledo, S. M., Gooding, T., and Little, J. B. Intercellular communication is involved in the bystander regulation of gene expression in human cells exposed to very low fluences of α particles. Radiat. Res., 150: 497-504, 1998.
    • (1998) Radiat. Res. , vol.150 , pp. 497-504
    • Azzam, E.I.1    De Toledo, S.M.2    Gooding, T.3    Little, J.B.4
  • 6
    • 0032723294 scopus 로고    scopus 로고
    • Unexpected sensitivity to the induction of mutations by very low doses of α-particle irradiation: Evidence for a bystander effect
    • Nagasawa, H., and Little, J. B. Unexpected sensitivity to the induction of mutations by very low doses of α-particle irradiation: evidence for a bystander effect. Radiat. Res., 152: 552-557, 1999.
    • (1999) Radiat. Res. , vol.152 , pp. 552-557
    • Nagasawa, H.1    Little, J.B.2
  • 8
    • 0031674026 scopus 로고    scopus 로고
    • Studies on bystander effects in human fibroblasts using a charged particle microbeam
    • Prise, K. M., Belyakov, O. V., Folkard, M., and Micheal, B. D. Studies on bystander effects in human fibroblasts using a charged particle microbeam. Int. J. Radiat. Biol., 74: 793-798, 1998.
    • (1998) Int. J. Radiat. Biol. , vol.74 , pp. 793-798
    • Prise, K.M.1    Belyakov, O.V.2    Folkard, M.3    Micheal, B.D.4
  • 9
    • 0035895240 scopus 로고    scopus 로고
    • Direct evidence for the participation of Gap-junction mediated intercellular communication in the transmission of damage signals from α-particle irradiated to non-irradiated cells
    • Azzam, E. I., de Toledo, S. M., and Little, J. B. Direct evidence for the participation of Gap-junction mediated intercellular communication in the transmission of damage signals from α-particle irradiated to non-irradiated cells. Proc. Natl. Acad. Sci. USA, 98: 473-478, 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 473-478
    • Azzam, E.I.1    De Toledo, S.M.2    Little, J.B.3
  • 10
    • 0033027240 scopus 로고    scopus 로고
    • Evidence for pronounced bystander effects caused by nonuniform distributions of radioactivity using a novel three-dimensional tissue culture model
    • Bishayee, A., Rao, D. V., and Howell, R. W. Evidence for pronounced bystander effects caused by nonuniform distributions of radioactivity using a novel three-dimensional tissue culture model. Radiat. Res., 152: 88-97, 1999.
    • (1999) Radiat. Res. , vol.152 , pp. 88-97
    • Bishayee, A.1    Rao, D.V.2    Howell, R.W.3
  • 11
    • 0035102134 scopus 로고    scopus 로고
    • The bystander effect in radiation oncogenesis. I. Transformation in C3H 10T1/2 cells in vitro can be initiated in the unirradiated neighbors of irradiated cells
    • Sawant, S. G., Randers-Pehrson, G., Geard, C. R., Brenner, D. J., and Hall, E. J. The bystander effect in radiation oncogenesis. I. Transformation in C3H 10T1/2 cells in vitro can be initiated in the unirradiated neighbors of irradiated cells. Radiat. Res., 155: 397-401, 2001.
    • (2001) Radiat. Res. , vol.155 , pp. 397-401
    • Sawant, S.G.1    Randers-Pehrson, G.2    Geard, C.R.3    Brenner, D.J.4    Hall, E.J.5
  • 12
    • 0030824455 scopus 로고    scopus 로고
    • α particles initiate biological production of superoxide anions and hydrogen peroxide in human cells
    • Narayanan, P. K., Goodwin, E. H., and Lehnert, B. E. α Particles initiate biological production of superoxide anions and hydrogen peroxide in human cells. Cancer Res., 57: 3963-3971, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 3963-3971
    • Narayanan, P.K.1    Goodwin, E.H.2    Lehnert, B.E.3
  • 13
    • 0030919931 scopus 로고    scopus 로고
    • Extracellular factor(s) following exposure to α particles can cause sister chromatid exchanges in normal human cells
    • Lehnert, B. E., and Goodwin, E. H. Extracellular factor(s) following exposure to α particles can cause sister chromatid exchanges in normal human cells. Cancer Res., 57: 2164-2171, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 2164-2171
    • Lehnert, B.E.1    Goodwin, E.H.2
  • 15
    • 0035144598 scopus 로고    scopus 로고
    • Free-radical initiated and gap junction-mediated bystander effect due to nonuniform distribution of incorporated radioactivity in a three-dimensional tissue culture model
    • Bishayee, A., Hill, H. Z., Stein, D., Rao, D. V., and Howell, R. W. Free-radical initiated and gap junction-mediated bystander effect due to nonuniform distribution of incorporated radioactivity in a three-dimensional tissue culture model. Radiat. Res., 155: 335-344, 2001.
    • (2001) Radiat. Res. , vol.155 , pp. 335-344
    • Bishayee, A.1    Hill, H.Z.2    Stein, D.3    Rao, D.V.4    Howell, R.W.5
  • 16
    • 0033765546 scopus 로고    scopus 로고
    • Production of a signal by irradiated cells which leads to a response in unirradiated cells characteristic of initiation of apoptosis
    • Lyng, F. M., Seymour, C. B., and Mothersill, C. Production of a signal by irradiated cells which leads to a response in unirradiated cells characteristic of initiation of apoptosis. Br. J. Cancer, 83: 1223-1230, 2000.
    • (2000) Br. J. Cancer , vol.83 , pp. 1223-1230
    • Lyng, F.M.1    Seymour, C.B.2    Mothersill, C.3
  • 17
    • 0035950528 scopus 로고    scopus 로고
    • Inflammatory-type responses after exposure to ionizing radiation in vivo: A mechanism for radiation-induced bystander effects?
    • Lorimore, S. A., Coates, P. J., Scobie, G. E., Milne, G., and Wright, E. G. Inflammatory-type responses after exposure to ionizing radiation in vivo: a mechanism for radiation-induced bystander effects? Oncogene, 20: 7085-7095, 2001.
    • (2001) Oncogene , vol.20 , pp. 7085-7095
    • Lorimore, S.A.1    Coates, P.J.2    Scobie, G.E.3    Milne, G.4    Wright, E.G.5
  • 18
    • 0023262144 scopus 로고
    • Role of superoxide dismutase in modification of radiation injury
    • Petkau, A. Role of superoxide dismutase in modification of radiation injury. Br. J. Cancer, 8 (Suppl.): 87-95, 1987.
    • (1987) Br. J. Cancer , vol.8 , pp. 87-95
    • Petkau, A.1
  • 19
    • 0029854544 scopus 로고    scopus 로고
    • Free radicals, proteins and DNA: Oxidative damage versus redox regulation
    • Halliwell, B. Free radicals, proteins and DNA: oxidative damage versus redox regulation. Biochem. Soc. Trans., 24: 1023-1027, 1996.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 1023-1027
    • Halliwell, B.1
  • 20
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames, B. N., Shigenaga, M. K., and Hagen, T. M. Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. USA. 90: 7915-7922, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 21
    • 0028006359 scopus 로고
    • Reactive oxygen species, chromosome mutation, and cancer: Possible role of clastogenic factors in carcinogenesis
    • Emerit, I. Reactive oxygen species, chromosome mutation, and cancer: possible role of clastogenic factors in carcinogenesis. Free Radic. Biol. Med., 16: 99-109, 1994.
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 99-109
    • Emerit, I.1
  • 22
    • 0028567070 scopus 로고
    • The role of the cellular antioxidant defense in oxidant carcinogenesis
    • Cerutti, P., Ghosh, R., Oya, Y., and Amstad, P. The role of the cellular antioxidant defense in oxidant carcinogenesis. Environ. Health Perspect., 102 (Suppl. 10): 123-129, 1994.
    • (1994) Environ. Health Perspect. , vol.102 , pp. 123-129
    • Cerutti, P.1    Ghosh, R.2    Oya, Y.3    Amstad, P.4
  • 24
    • 0000477631 scopus 로고
    • X-ray sensitivity and DNA, synthesis in synchronous populations of Hela cells
    • Terasima, R., and Tolmach, L. J. X-ray sensitivity and DNA synthesis in synchronous populations of Hela cells. Science (Wash. DC), 140: 490-492, 1963.
    • (1963) Science (Wash. DC) , vol.140 , pp. 490-492
    • Terasima, R.1    Tolmach, L.J.2
  • 25
    • 0013973616 scopus 로고
    • X-ray sensitivity during the cell generation cycle of cultured Chinese hamster cells
    • Sinclair, W. K., and Morton, R. A. X-ray sensitivity during the cell generation cycle of cultured Chinese hamster cells. Radiat. Res., 29: 450-474, 1966.
    • (1966) Radiat. Res. , vol.29 , pp. 450-474
    • Sinclair, W.K.1    Morton, R.A.2
  • 26
    • 0021206597 scopus 로고
    • Radioprotection by superoxide dismutase of macrophage progenitor cells from mouse bone marrow
    • Petkau, A., and Chelack, W. S. Radioprotection by superoxide dismutase of macrophage progenitor cells from mouse bone marrow. Biochem. Biophys. Res. Commun., 119: 1089-1095. 1984.
    • (1984) Biochem. Biophys. Res. Commun. , vol.119 , pp. 1089-1095
    • Petkau, A.1    Chelack, W.S.2
  • 27
    • 0024242402 scopus 로고
    • Protection of bone marrow progenitor cells by superoxide dismutase
    • Petkau, A. Protection of bone marrow progenitor cells by superoxide dismutase. Mol. Cell. Biochem., 84: 133-140, 1988.
    • (1988) Mol. Cell. Biochem. , vol.84 , pp. 133-140
    • Petkau, A.1
  • 28
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C., and Fridovich, I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem., 44: 276-287, 1971.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 29
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz, D. R., and Oberley, L. W. An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal. Biochem., 179: 8-18, 1989.
    • (1989) Anal. Biochem. , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 31
    • 0021987630 scopus 로고
    • Measurement of micronuclei in lymphocytes
    • Fenech, M., and Morley, A. A. Measurement of micronuclei in lymphocytes. Mutat. Res., 147: 29-36, 1985.
    • (1985) Mutat. Res. , vol.147 , pp. 29-36
    • Fenech, M.1    Morley, A.A.2
  • 33
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis
    • Klug, D., Rabani, J., and Fridovich, I. A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J. Biol. Chem., 247: 4839-4842, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovich, I.3
  • 39
    • 0034038708 scopus 로고    scopus 로고
    • Glucose deprivation-induced oxidative stress in human tumor cells. A fundamental defect in metabolism?
    • Spitz, D. R., Sim, J. E., Ridnour, L. A., Galoforo, S. S., and Lee, Y. J. Glucose deprivation-induced oxidative stress in human tumor cells. A fundamental defect in metabolism? Ann. N. Y. Acad. Sci., 899: 349-362, 2000.
    • (2000) Ann. N. Y. Acad. Sci. , vol.899 , pp. 349-362
    • Spitz, D.R.1    Sim, J.E.2    Ridnour, L.A.3    Galoforo, S.S.4    Lee, Y.J.5
  • 40
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler, V., Yin, Z., Tew, K. D., and Ronai, Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene, 18: 6104-6111, 1999.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 41
    • 0002574684 scopus 로고    scopus 로고
    • Reactive oxygen intermediates as primary signals and second messengers in the activation of transcription factors
    • H. J. Forman and E. Cadenas (eds.). New York: Chapman & Hall
    • Schulze-Osthoff, K., Bauer, M., Vogt, M., Wesselborg, S., and Baeuerle, P. A. Reactive oxygen intermediates as primary signals and second messengers in the activation of transcription factors, In: H. J. Forman and E. Cadenas (eds.), Oxidative Stress and Signal Transduction, pp. 239-259. New York: Chapman & Hall. 1997.
    • (1997) Oxidative Stress and Signal Transduction , pp. 239-259
    • Schulze-Osthoff, K.1    Bauer, M.2    Vogt, M.3    Wesselborg, S.4    Baeuerle, P.A.5
  • 42
    • 0027618650 scopus 로고
    • Regulation of the NF-κB/rel transcription factor and IκB inhibitor system
    • Liou, H. C., and Baltimore, D. Regulation of the NF-κB/rel transcription factor and IκB inhibitor system. Curr. Opin. Cell Biol., 5: 477-487, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 477-487
    • Liou, H.C.1    Baltimore, D.2
  • 43
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • Schreck, R., Rieber, P., and Baeuerle, P. A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J., 10: 2247-2258, 1991.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 44
    • 0033163393 scopus 로고    scopus 로고
    • Is NF-κB the sensor of oxidative stress?
    • Li, N., and Karin, M. Is NF-κB the sensor of oxidative stress? FASEB J., 13: 1137-1143, 1999.
    • (1999) FASEB J. , vol.13 , pp. 1137-1143
    • Li, N.1    Karin, M.2
  • 45
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior, B. M. NADPH oxidase: an update. Blood. 93: 1464-1476, 1999.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 46
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb, M. H., and Goldsmith, E. J. How MAP kinases are regulated. J. Biol. Chem. 270: 14843-14846, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 47
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T., and Holbrook, N. J. Oxidants. oxidative stress and the biology of ageing. Nature (Lond.), 408: 239-247, 2000.
    • (2000) Nature (Lond.) , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 48
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: The regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • Kolch, W. Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem. J., 351: 289-305, 2000.
    • (2000) Biochem. J. , vol.351 , pp. 289-305
    • Kolch, W.1
  • 49
    • 0032563677 scopus 로고    scopus 로고
    • Stress-responsive" mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium
    • Sugden, P. H., and Clerk, A. "Stress-responsive" mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium. Circ. Res., 83: 345-352, 1998.
    • (1998) Circ. Res. , vol.83 , pp. 345-352
    • Sugden, P.H.1    Clerk, A.2
  • 50
    • 0032570704 scopus 로고    scopus 로고
    • Glucose deprivation-induced cytotoxicity and alterations in mitogen-activated protein kinase activation are mediated by oxidative stress in multidrug-resistant human breast carcinoma cells
    • Lee, Y. J., Galoforo, S. S., Berns, C. M., Chen, J. C., Davis, B. H., Sim, J. E., Corry, P. M., and Spitz, D. R. Glucose deprivation-induced cytotoxicity and alterations in mitogen-activated protein kinase activation are mediated by oxidative stress in multidrug-resistant human breast carcinoma cells. J. Biol. Chem., 273: 5294-5299, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5294-5299
    • Lee, Y.J.1    Galoforo, S.S.2    Berns, C.M.3    Chen, J.C.4    Davis, B.H.5    Sim, J.E.6    Corry, P.M.7    Spitz, D.R.8
  • 52
    • 0034950743 scopus 로고    scopus 로고
    • Oxidative stress in cells exposed to low levels of ionizing radiation
    • Lyng, F. M., Seymour, C. B., and Mothersill, C. Oxidative stress in cells exposed to low levels of ionizing radiation. Biochem. Soc, Trans., 29: 350-353, 2001.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 350-353
    • Lyng, F.M.1    Seymour, C.B.2    Mothersill, C.3
  • 53
    • 0034759199 scopus 로고    scopus 로고
    • HPRT mutants induced in bystander cells by very low fluences of α particles result primarily from point mutations
    • Huo, L., Nagasawa, H., and Little, J. B. HPRT mutants induced in bystander cells by very low fluences of α particles result primarily from point mutations. Radiat. Res., 156: 521-525, 2001.
    • (2001) Radiat. Res. , vol.156 , pp. 521-525
    • Huo, L.1    Nagasawa, H.2    Little, J.B.3
  • 54
    • 0030461523 scopus 로고    scopus 로고
    • Radioprotection by DMSO against the biological effects of incorporated radionuclides in vivo
    • Goddu, S. M., Narra, V. R., Harapanhalli, R. S., Howell, R. W., and Rao, D. V. Radioprotection by DMSO against the biological effects of incorporated radionuclides in vivo. Acta Oncol., 35: 901-907, 1996.
    • (1996) Acta Oncol. , vol.35 , pp. 901-907
    • Goddu, S.M.1    Narra, V.R.2    Harapanhalli, R.S.3    Howell, R.W.4    Rao, D.V.5
  • 55
    • 0018242693 scopus 로고
    • Radiation protection by superoxide dismutase
    • Petkau, A. Radiation protection by superoxide dismutase. Photochem. Photobiol., 28: 765 774, 1978.
    • (1978) Photochem. Photobiol. , vol.28 , pp. 765-774
    • Petkau, A.1
  • 56
    • 0030331858 scopus 로고    scopus 로고
    • Immunocytochemical study of uptake of exogenous carrier-free copper-zinc superoxide dismutase by peripheral blood lymphocytes
    • Edeas, M. A., Peltier, E., Claise, C., Khalfoun, Y., and Lindenbaum, A. Immunocytochemical study of uptake of exogenous carrier-free copper-zinc superoxide dismutase by peripheral blood lymphocytes. Cell. Mol. Biol. (Noisy-le-Grand), 42: 1137-1143, 1996.
    • (1996) Cell. Mol. Biol. (Noisy-le-Grand) , vol.42 , pp. 1137-1143
    • Edeas, M.A.1    Peltier, E.2    Claise, C.3    Khalfoun, Y.4    Lindenbaum, A.5
  • 57
    • 0031807178 scopus 로고    scopus 로고
    • Intracellular uptake of recombinant superoxide dismutase after intratracheal administration
    • Das, S., Horowitz, S., Robbins, C. G., el-Sabban, M. E., Sahgal, N., and Davis, J. M. Intracellular uptake of recombinant superoxide dismutase after intratracheal administration. Am. J. Physiol., 274: L673-L677, 1998.
    • (1998) Am. J. Physiol. , vol.274 , pp. L673-L677
    • Das, S.1    Horowitz, S.2    Robbins, C.G.3    El-Sabban, M.E.4    Sahgal, N.5    Davis, J.M.6
  • 58
    • 0018597050 scopus 로고
    • Permeation of liposome membrane by superoxide radical
    • Rumyantseva, G. V., Weiner, L. M., Molin, Y. N., and Budker, V. G. Permeation of liposome membrane by superoxide radical. FEBS Lett., 108: 477-480, 1979.
    • (1979) FEBS Lett. , vol.108 , pp. 477-480
    • Rumyantseva, G.V.1    Weiner, L.M.2    Molin, Y.N.3    Budker, V.G.4
  • 59
    • 0021105282 scopus 로고
    • Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids
    • Takahashi, M. A., and Asada, K. Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch, Biochem. Biophys., 226: 558-566, 1983.
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 558-566
    • Takahashi, M.A.1    Asada, K.2
  • 60
    • 0025850732 scopus 로고
    • Regulation of fast inactivation of cloned mammalian IK(A) channels by cysteine oxidation
    • Ruppersberg, J. P., Stocker, M., Pongs, O., Heinemann, S. H., Frank, R., and Koenen, M. Regulation of fast inactivation of cloned mammalian IK(A) channels by cysteine oxidation. Nature (Lond.), 352: 711-714, 1991.
    • (1991) Nature (Lond.) , vol.352 , pp. 711-714
    • Ruppersberg, J.P.1    Stocker, M.2    Pongs, O.3    Heinemann, S.H.4    Frank, R.5    Koenen, M.6
  • 61
    • 0032126920 scopus 로고    scopus 로고
    • Redox control of vascular smooth muscle proliferation
    • Griendling, K. K., and Ushio-Fukai, M. Redox control of vascular smooth muscle proliferation. J. Lab. Clin. Med., 132: 9-15, 1998.
    • (1998) J. Lab. Clin. Med. , vol.132 , pp. 9-15
    • Griendling, K.K.1    Ushio-Fukai, M.2
  • 62
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • Griendling, K. K., Sorescu, D., and Ushio-Fukai, M. NAD(P)H oxidase: role in cardiovascular biology and disease. Circ. Res., 86: 494-501, 2000.
    • (2000) Circ. Res. , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 63
    • 0030821702 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 and its mode of activation in human neutrophils by opsonized zymosan. Correlation between 42/44 kDa mitogen-activated protein kinase, cytosolic phospholipase A2 and NADPH oxidase
    • Hazan, I., Dana, R., Granot, Y., and Levy, R. Cytosolic phospholipase A2 and its mode of activation in human neutrophils by opsonized zymosan. Correlation between 42/44 kDa mitogen-activated protein kinase, cytosolic phospholipase A2 and NADPH oxidase. Biochem. J., 326: 867-876, 1997.
    • (1997) Biochem. J. , vol.326 , pp. 867-876
    • Hazan, I.1    Dana, R.2    Granot, Y.3    Levy, R.4
  • 64
    • 0031573210 scopus 로고    scopus 로고
    • Formyl peptide receptors are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways: Role in activation of reduced nicotinamide adenine dinucleotide oxidase
    • Rane, M. J., Carrithers, S. L., Arthur, J. M., Klein, J. B., and McLeish, K. R. Formyl peptide receptors are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways: role in activation of reduced nicotinamide adenine dinucleotide oxidase. J. Immunol., 159: 5070-5078, 1997.
    • (1997) J. Immunol. , vol.159 , pp. 5070-5078
    • Rane, M.J.1    Carrithers, S.L.2    Arthur, J.M.3    Klein, J.B.4    McLeish, K.R.5
  • 66
    • 0032769955 scopus 로고    scopus 로고
    • Localization of regulatory protein binding sites in the proximal region of human myometrial connexin 43 gene
    • Echetebu, C. O., Ali, M., Izban, M. G., MacKay, L., and Garfield, R. E. Localization of regulatory protein binding sites in the proximal region of human myometrial connexin 43 gene. Mol. Hum. Reprod., 5: 757-766, 1999.
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 757-766
    • Echetebu, C.O.1    Ali, M.2    Izban, M.G.3    MacKay, L.4    Garfield, R.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.