메뉴 건너뛰기




Volumn 10, Issue 9, 1999, Pages 655-664

Nitric oxide enhances the manganese superoxide dismutase-dependent suppression of proliferation in HT-1080 fibrosarcoma cells

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE SUPEROXIDE DISMUTASE; NITRIC OXIDE; NITROPRUSSIDE SODIUM;

EID: 0032858952     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 0023947742 scopus 로고
    • Free radicals in medicine. II. Involvement in human disease
    • Southorn, P. A., and Powis, G. Free radicals in medicine. II. Involvement in human disease. Mayo Clin. Proc., 63: 390-408, 1988.
    • (1988) Mayo Clin. Proc. , vol.63 , pp. 390-408
    • Southorn, P.A.1    Powis, G.2
  • 2
    • 0024849640 scopus 로고
    • Antioxidant enzyme activities in normal and transformed mouse liver cells
    • Sun, Y., Oberley, L. W., Elwell, J. H., and Sierra-Rivera, E. Antioxidant enzyme activities in normal and transformed mouse liver cells. Int. J. Cancer, 44: 1028-1033, 1989.
    • (1989) Int. J. Cancer , vol.44 , pp. 1028-1033
    • Sun, Y.1    Oberley, L.W.2    Elwell, J.H.3    Sierra-Rivera, E.4
  • 3
    • 0024796992 scopus 로고
    • Messenger RNA for manganese and copper-zinc superoxide dismutases in hepatomas: Correlation with degree of differentiation
    • Galeotti, T., Wohlrab, H., Borrello, S., and De Leo, M. E. Messenger RNA for manganese and copper-zinc superoxide dismutases in hepatomas: correlation with degree of differentiation. Biochem. Biophys. Res. Commun., 165: 581-589, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 581-589
    • Galeotti, T.1    Wohlrab, H.2    Borrello, S.3    De Leo, M.E.4
  • 5
    • 0019230916 scopus 로고
    • Cell differentiation, aging and cancer: The possible roles of superoxide and superoxide dismutases
    • Oberley, L. W., Oberley, T. D., and Buettner, G. R. Cell differentiation, aging and cancer: the possible roles of superoxide and superoxide dismutases. Med. Hypotheses, 6: 249-268, 1980.
    • (1980) Med. Hypotheses , vol.6 , pp. 249-268
    • Oberley, L.W.1    Oberley, T.D.2    Buettner, G.R.3
  • 6
    • 0018749490 scopus 로고
    • Role of superoxide dismutase in cancer: A review
    • Oberley, L. W., and Buettner, G. R. Role of superoxide dismutase in cancer: a review. Cancer Res., 39: 1141-1149, 1979.
    • (1979) Cancer Res. , vol.39 , pp. 1141-1149
    • Oberley, L.W.1    Buettner, G.R.2
  • 9
    • 0029032567 scopus 로고
    • Phenotypic changes induced in human breast cancer cells by overexpression of manganese-containing superoxide dismutase
    • Li, J. J., Oberley, L. W., St. Clair, D. K., Ridnour, L. A., and Oberley, T. D. Phenotypic changes induced in human breast cancer cells by overexpression of manganese-containing superoxide dismutase. Oncogene, 10: 1989-2000, 1995.
    • (1995) Oncogene , vol.10 , pp. 1989-2000
    • Li, J.J.1    Oberley, L.W.2    St. Clair, D.K.3    Ridnour, L.A.4    Oberley, T.D.5
  • 10
    • 0032524976 scopus 로고    scopus 로고
    • Overexpression of manganese superoxide dismutase in DU145 human prostate carcinoma cells has multiple effects on cell phenotype
    • Li, N., Oberley, T. D., Oberley, L. W., and Zhong, W. Overexpression of manganese superoxide dismutase in DU145 human prostate carcinoma cells has multiple effects on cell phenotype. Prostate, 35: 221-233, 1998.
    • (1998) Prostate , vol.35 , pp. 221-233
    • Li, N.1    Oberley, T.D.2    Oberley, L.W.3    Zhong, W.4
  • 11
    • 0030958392 scopus 로고    scopus 로고
    • Transfection and expression of MnSOD cDNA decreases tumor malignancy of human oral squamous carcinoma SCC-25 cells
    • Liu, R., Oberley, T. D., and Oberley, L. W. Transfection and expression of MnSOD cDNA decreases tumor malignancy of human oral squamous carcinoma SCC-25 cells. Hum. Gene Ther., 8: 585-595, 1997.
    • (1997) Hum. Gene Ther. , vol.8 , pp. 585-595
    • Liu, R.1    Oberley, T.D.2    Oberley, L.W.3
  • 12
    • 0031035767 scopus 로고    scopus 로고
    • Suppression of the malignant phenotype of human glioma cells by overexpression of manganese superoxide dismutase
    • Zhong, W., Oberley, L. W., Oberley, T. D., and St. Clair, D. K. Suppression of the malignant phenotype of human glioma cells by overexpression of manganese superoxide dismutase. Oncogene, 14: 481-490, 1997.
    • (1997) Oncogene , vol.14 , pp. 481-490
    • Zhong, W.1    Oberley, L.W.2    Oberley, T.D.3    St. Clair, D.K.4
  • 13
    • 0029886717 scopus 로고    scopus 로고
    • Manganese-containing superoxide dismutase overexpression causes phenotypic reversion in SV40-transformed human lung fibroblasts
    • Yan, T., Oberley, L. W., Zhong, W., and St. Clair, D. K. Manganese-containing superoxide dismutase overexpression causes phenotypic reversion in SV40-transformed human lung fibroblasts. Cancer Res., 56: 2864-2871, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 2864-2871
    • Yan, T.1    Oberley, L.W.2    Zhong, W.3    St. Clair, D.K.4
  • 14
    • 0031966914 scopus 로고    scopus 로고
    • Inhibition of cell growth in NIH/3T3 fibroblasts by overexpression of manganese superoxide dismutase: Mechanistic studies
    • Li, N., Oberley, T. D., Oberley, L. W., and Zhong, W. Inhibition of cell growth in NIH/3T3 fibroblasts by overexpression of manganese superoxide dismutase: mechanistic studies. J Cell Physiol., 175: 359-369, 1998.
    • (1998) J Cell Physiol. , vol.175 , pp. 359-369
    • Li, N.1    Oberley, T.D.2    Oberley, L.W.3    Zhong, W.4
  • 16
    • 0002395989 scopus 로고
    • The chemistry of oxygen radicals and oxygen-derived species
    • B. Halliwell and J. M. C. Gutteridge (eds.) Oxford: Claredon Press
    • Halliwell, B., and Gutteridge, J. M. C. The chemistry of oxygen radicals and oxygen-derived species. In: B. Halliwell and J. M. C. Gutteridge (eds.) Free Radicals in Biology and Medicine, pp. 20-68. Oxford: Claredon Press, 1985.
    • (1985) Free Radicals in Biology and Medicine , pp. 20-68
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 18
    • 0032493381 scopus 로고    scopus 로고
    • Lower intracellular hydrogen peroxide levels in cells overexpressing CuZn-superoxide dismutase
    • Teixeira, H. D., Schumacher, R. I., and Meneghini, R. Lower intracellular hydrogen peroxide levels in cells overexpressing CuZn-superoxide dismutase. Proc. Natl. Acad. Sci. USA, 95: 7872-7875, 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7872-7875
    • Teixeira, H.D.1    Schumacher, R.I.2    Meneghini, R.3
  • 19
    • 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
  • 20
    • 0024202127 scopus 로고
    • Induction of manganous superoxide dismutase by tumor necrosis factor: Possible protective mechanism
    • Wong, G. H. W., and Goeddel, D. V. Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism. Science, 242: 941-944, 1988.
    • (1988) Science , vol.242 , pp. 941-944
    • Wong, G.H.W.1    Goeddel, D.V.2
  • 21
    • 0025078258 scopus 로고
    • Stimulation of Mn-superoxide dismutase expression by tumor necrosis factor-α: Quantitative determination of Mn-SOD protein levels in TNF-resistant and sensitive cells by ELISA
    • Kawaguchi, T., Takeyasu, A., Matsunobu, K., Uda, T., Ishiwaza, M., Suzuki, K., Nishiura, T., Ishikawa, M., and Taniguchi, N. Stimulation of Mn-superoxide dismutase expression by tumor necrosis factor-α: quantitative determination of Mn-SOD protein levels in TNF-resistant and sensitive cells by ELISA. Biochem. Biophys. Res. Commun., 171: 1378-1386, 1990.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 1378-1386
    • Kawaguchi, T.1    Takeyasu, A.2    Matsunobu, K.3    Uda, T.4    Ishiwaza, M.5    Suzuki, K.6    Nishiura, T.7    Ishikawa, M.8    Taniguchi, N.9
  • 22
    • 0024428198 scopus 로고
    • Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • Wong, G. H. W., Elwell, J. H., Oberley, L. W., and Goeddel, D. V. Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell, 58: 923-931, 1989.
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.W.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 23
    • 0005777506 scopus 로고
    • Superoxide mediates the toxicity of paraquat for Chinese hamster ovary cells
    • Bagley, A. C., Krall, J., and Lynch, R. E. Superoxide mediates the toxicity of paraquat for Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA, 83: 3189-3193, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3189-3193
    • Bagley, A.C.1    Krall, J.2    Lynch, R.E.3
  • 24
    • 0023901508 scopus 로고
    • Superoxide mediates the toxicity of paraquat for cultured mammalian cells
    • Krall, J., Bagley, A. C., Mullenbach, G. T., Hallewell, R. A., and Lynch, R. E. Superoxide mediates the toxicity of paraquat for cultured mammalian cells. J. Biol. Chem., 263: 1910-1914, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1910-1914
    • Krall, J.1    Bagley, A.C.2    Mullenbach, G.T.3    Hallewell, R.A.4    Lynch, R.E.5
  • 25
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris, A., Oshino, N., and Chance, B. The cellular production of hydrogen peroxide. Biochem. J., 128: 617-630, 1972.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 26
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Washington DC
    • Fridovich, I. The biology of oxygen radicals. Science (Washington DC), 201: 875-880, 1978.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 28
    • 0028280787 scopus 로고
    • The toxicity of high-dose superoxide dismutase suggests that superoxide can both initiate and terminate lipid peroxidation in the reperfused heart
    • Nelson, S. K., Bose, S. K., and McCord, J. M. The toxicity of high-dose superoxide dismutase suggests that superoxide can both initiate and terminate lipid peroxidation in the reperfused heart. Free Radical Biol. Med., 16: 195-200, 1994.
    • (1994) Free Radical Biol. Med. , vol.16 , pp. 195-200
    • Nelson, S.K.1    Bose, S.K.2    McCord, J.M.3
  • 29
    • 0024420332 scopus 로고
    • Hydroethidine: A fluorescent redox probe for locating hypoxic cells in spheroids and murine tumours
    • Olive, P. L. Hydroethidine: a fluorescent redox probe for locating hypoxic cells in spheroids and murine tumours. Br. J. Cancer, 60: 332-338, 1989.
    • (1989) Br. J. Cancer , vol.60 , pp. 332-338
    • Olive, P.L.1
  • 30
    • 0022519244 scopus 로고
    • Uptake and accumulation of the vital dye hydroethidine in neoplastic cells
    • Bucana, C., Saiki, I., and Nayar, R. Uptake and accumulation of the vital dye hydroethidine in neoplastic cells. J. Histochem. Cytochem., 34: 1109-1115, 1986.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1109-1115
    • Bucana, C.1    Saiki, I.2    Nayar, R.3
  • 31
    • 0028369668 scopus 로고
    • Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells
    • Carter, W. O., Narayanan, P. K., and Robinson, J. P. Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells. J. Leukocyte Biol., 55: 253-258, 1994.
    • (1994) J. Leukocyte Biol. , vol.55 , pp. 253-258
    • Carter, W.O.1    Narayanan, P.K.2    Robinson, J.P.3
  • 32
    • 0030909971 scopus 로고    scopus 로고
    • Intracellular generation of reactive oxygen species during nonhypoxic lung ischemia
    • Al-Mehdi, A. B., Shuman, H., and Fisher, A. B. Intracellular generation of reactive oxygen species during nonhypoxic lung ischemia. Am. J. Physiol., 272: L294-L300, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Al-Mehdi, A.B.1    Shuman, H.2    Fisher, A.B.3
  • 33
    • 0027430156 scopus 로고
    • Dihydrorhodamine 123: A fluorescent probe for superoxide generation?
    • Henderson, L. M., and Chappell, J. B. Dihydrorhodamine 123: a fluorescent probe for superoxide generation? Eur. J. Biochem., 217: 973-980, 1993.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 973-980
    • Henderson, L.M.1    Chappell, J.B.2
  • 34
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway
    • Chen, Q., Olashaw, N., and Wu, J. Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway. J. Biol. Chem., 270: 28499-28502, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28499-28502
    • Chen, Q.1    Olashaw, N.2    Wu, J.3
  • 35
    • 0030761155 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells
    • Budd, S. L., Castilho, R. F., and Nicholls, D. G. Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells. FEBS Lett., 415: 21-24, 1997.
    • (1997) FEBS Lett. , vol.415 , pp. 21-24
    • Budd, S.L.1    Castilho, R.F.2    Nicholls, D.G.3
  • 36
    • 0030942257 scopus 로고    scopus 로고
    • Differences in the regulation of iron regulatory protein-1 (IRP- 1) by extra- and intracellular oxidative stress
    • Pantopoulos, K., Mueller, S., Atzberger, A., Ansorge, W., Stremmel, W., and Hentze, M. W. Differences in the regulation of iron regulatory protein-1 (IRP- 1) by extra- and intracellular oxidative stress. J. Biol. Chem., 272: 9802-9808, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9802-9808
    • Pantopoulos, K.1    Mueller, S.2    Atzberger, A.3    Ansorge, W.4    Stremmel, W.5    Hentze, M.W.6
  • 37
    • 0030999236 scopus 로고    scopus 로고
    • Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4. Regulation of superoxidation and mitogenesis
    • Chini, C. C., Grande, J. P., Chini, E. N., and Dousa, T. P. Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4. Regulation of superoxidation and mitogenesis. J. Biol. Chem., 272: 9854-9859, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9854-9859
    • Chini, C.C.1    Grande, J.P.2    Chini, E.N.3    Dousa, T.P.4
  • 38
    • 0030061844 scopus 로고    scopus 로고
    • Uptake of fluorescent dyes associated with the functional expression of the cystic fibrosis transmembrane conductance regulator in epithelial cells
    • Wersto, R. P., Rosenthal, E. R., Crystal, R. G., and Spring, K. R. Uptake of fluorescent dyes associated with the functional expression of the cystic fibrosis transmembrane conductance regulator in epithelial cells. Proc. Natl. Acad. Sci. USA, 93: 1167-1172, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1167-1172
    • Wersto, R.P.1    Rosenthal, E.R.2    Crystal, R.G.3    Spring, K.R.4
  • 39
    • 0024584020 scopus 로고
    • Nitric oxide. a macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells
    • Stuehr, D. J., and Nathan, C. F. Nitric oxide. A macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells. J. Exp. Med., 169: 1543-1555, 1989.
    • (1989) J. Exp. Med. , vol.169 , pp. 1543-1555
    • Stuehr, D.J.1    Nathan, C.F.2
  • 40
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. F. Nitric oxide as a secretory product of mammalian cells. FASEB J., 6: 3051-3064, 1992.
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.F.1
  • 41
    • 0025190536 scopus 로고
    • Cytolytic mechanisms of activated macrophages. Tumor necrosis factor and L-arginine-dependent mechanisms act synergistically as the major cytolytic mechanisms of activated macrophages
    • Higuchi, M., Higashi, N., Taki, H., and Osawa, T. Cytolytic mechanisms of activated macrophages. Tumor necrosis factor and L-arginine-dependent mechanisms act synergistically as the major cytolytic mechanisms of activated macrophages. J. Immunol., 144: 1425-1431, 1990.
    • (1990) J. Immunol. , vol.144 , pp. 1425-1431
    • Higuchi, M.1    Higashi, N.2    Taki, H.3    Osawa, T.4
  • 42
    • 0029918676 scopus 로고    scopus 로고
    • The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility
    • Farias-Eisner, R., Chaudhuri, G., Aeberhard, E., and Fukuto, J. M. The chemistry and tumoricidal activity of nitric oxide/hydrogen peroxide and the implications to cell resistance/susceptibility. J. Biol. Chem., 271: 6144-6151, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6144-6151
    • Farias-Eisner, R.1    Chaudhuri, G.2    Aeberhard, E.3    Fukuto, J.M.4
  • 43
    • 0029130821 scopus 로고
    • Increased cytotoxicity of 3-morpholinosydnonimine to HepG2 cells in the presence of superoxide dismutase. Role of hydrogen peroxide and iron
    • Gergel, D., Misik, V., Ondrias, K., and Cederbaum, A. I. Increased cytotoxicity of 3-morpholinosydnonimine to HepG2 cells in the presence of superoxide dismutase. Role of hydrogen peroxide and iron. J. Biol. Chem., 270: 20922-20929, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20922-20929
    • Gergel, D.1    Misik, V.2    Ondrias, K.3    Cederbaum, A.I.4
  • 44
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman, J. S., and Koppenol, W. H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am. J. Physiol., 271: C1424-C1437, 1996.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 45
    • 0029847980 scopus 로고    scopus 로고
    • Chemiluminescence headspace-gas analysis for determination of nitric oxide formation in biological systems
    • Brien, J. F., McLaughlin, B. E., Nakatsu, K., and Marks, G. S. Chemiluminescence headspace-gas analysis for determination of nitric oxide formation in biological systems. Methods Enzymol., 268: 83-92, 1996.
    • (1996) Methods Enzymol. , vol.268 , pp. 83-92
    • Brien, J.F.1    McLaughlin, B.E.2    Nakatsu, K.3    Marks, G.S.4
  • 46
    • 0343773381 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the redox cycling of nitroprusside
    • Ramakrishna Rao, D. N., and Cederbaum, A. I. Generation of reactive oxygen species by the redox cycling of nitroprusside. Biochim. Biophys. Acta, 1289: 195-202, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1289 , pp. 195-202
    • Ramakrishna Rao, D.N.1    Cederbaum, A.I.2
  • 47
    • 0032077132 scopus 로고    scopus 로고
    • Apparent role of hydroxyl radicals in oxidative brain injury induced by sodium nitroprusside
    • Rauhala, P., Khaldi, A., Mohanakumar, K. P., and Chiueh, C. C. Apparent role of hydroxyl radicals in oxidative brain injury induced by sodium nitroprusside. Free Radical Biol. Med., 24: 1065-1073, 1998.
    • (1998) Free Radical Biol. Med. , vol.24 , pp. 1065-1073
    • Rauhala, P.1    Khaldi, A.2    Mohanakumar, K.P.3    Chiueh, C.C.4
  • 49
    • 0030781227 scopus 로고    scopus 로고
    • Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis
    • Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., and Koppenol, W. H. Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chem. Res. Toxicol., 10: 1285-1292, 1997.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1285-1292
    • Kissner, R.1    Nauser, T.2    Bugnon, P.3    Lye, P.G.4    Koppenol, W.H.5
  • 50
    • 0030577116 scopus 로고    scopus 로고
    • The role of nitric oxide (NO-) in the carcinogenic process
    • Tamir, S., and Tannenbaum, S. R. The role of nitric oxide (NO-) in the carcinogenic process. Biochim. Biophys. Acta, 1288: F31-F36, 1996.
    • (1996) Biochim. Biophys. Acta , vol.1288
    • Tamir, S.1    Tannenbaum, S.R.2
  • 51
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytcchrome oxidase
    • Brown, G. C. Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytcchrome oxidase. FEBS Lett., 369: 136-139, 1995.
    • (1995) FEBS Lett. , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 52
    • 0029846920 scopus 로고    scopus 로고
    • Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase
    • Sampson, J. B., Rosen, H., and Beckman, J. S. Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase. Methods Enzymol., 269: 210-218, 1996.
    • (1996) Methods Enzymol. , vol.269 , pp. 210-218
    • Sampson, J.B.1    Rosen, H.2    Beckman, J.S.3
  • 54
    • 0030048479 scopus 로고    scopus 로고
    • Modulation of superoxide-dependent oxidation and hydroxylation reactions by nitric oxide
    • Miles, A. M., Bohle, D. S., Glassbrenner, P. A., Hansert, B., Wink, D. A., and Grisham, M. B. Modulation of superoxide-dependent oxidation and hydroxylation reactions by nitric oxide. J. Biol. Chem., 271: 40-47, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 40-47
    • Miles, A.M.1    Bohle, D.S.2    Glassbrenner, P.A.3    Hansert, B.4    Wink, D.A.5    Grisham, M.B.6
  • 55
    • 0021223916 scopus 로고
    • Oxygen modulates growth of human cells at physiologic partial pressures
    • Balin, A. K., Fisher, A. J., and Carter, D. M. Oxygen modulates growth of human cells at physiologic partial pressures. J. Exp. Med., 160: 152-166, 1984.
    • (1984) J. Exp. Med. , vol.160 , pp. 152-166
    • Balin, A.K.1    Fisher, A.J.2    Carter, D.M.3
  • 56
    • 0030790611 scopus 로고    scopus 로고
    • Regulation of nitric oxide synthesis by oxygen in vascular endothelial cells
    • Whorton, A. R., Simonds, D. B., and Piantadosi, C. A. Regulation of nitric oxide synthesis by oxygen in vascular endothelial cells. Am. J. Physiol., 272: L1161-L1166, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Whorton, A.R.1    Simonds, D.B.2    Piantadosi, C.A.3
  • 57
    • 0018801619 scopus 로고
    • Effects of thiols, sugars, and proteins on nitric oxide activation of guanylate cyclase
    • Braughler, J. M., Mittal, C. K., and Murad, F. Effects of thiols, sugars, and proteins on nitric oxide activation of guanylate cyclase. J. Biol. Chem., 254: 12450-12454, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12450-12454
    • Braughler, J.M.1    Mittal, C.K.2    Murad, F.3
  • 58
    • 0028116530 scopus 로고
    • Tumor cells suppress cytokine-induced nitric-oxide (NO) production in cerebral endothelial cells
    • Murata, J., Corradin, S. B., Janzer, R. C., and Juillerat-Jeanneret, L. Tumor cells suppress cytokine-induced nitric-oxide (NO) production in cerebral endothelial cells. Int. J. Cancer, 59: 699-705, 1994.
    • (1994) Int. J. Cancer , vol.59 , pp. 699-705
    • Murata, J.1    Corradin, S.B.2    Janzer, R.C.3    Juillerat-Jeanneret, L.4
  • 59
    • 0032079851 scopus 로고    scopus 로고
    • Purification and characterization of a nitric-oxide synthase from rat liver mitochondria
    • Tatoyan, A., and Giulivi, C. Purification and characterization of a nitric-oxide synthase from rat liver mitochondria. J. Biol. Chem., 273: 11044-11048, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11044-11048
    • Tatoyan, A.1    Giulivi, C.2
  • 60
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi, C., Poderoso, J. J., and Boveris, A. Production of nitric oxide by mitochondria. J. Biol. Chem., 273: 11038-11043, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 61
    • 0032526039 scopus 로고    scopus 로고
    • Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism
    • Giulivi, C. Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism. Biochem. J., 332: 673-679, 1998.
    • (1998) Biochem. J. , vol.332 , pp. 673-679
    • Giulivi, C.1
  • 62
    • 0032211767 scopus 로고    scopus 로고
    • Stimulation of soluble guanylate cyclase by superoxide dismutase is mediated by NO
    • Friebe, A., Schultz, G., and Koesling, D. Stimulation of soluble guanylate cyclase by superoxide dismutase is mediated by NO. Biochem. J., 335: 527-531, 1998.
    • (1998) Biochem. J. , vol.335 , pp. 527-531
    • Friebe, A.1    Schultz, G.2    Koesling, D.3
  • 63
    • 0029774373 scopus 로고    scopus 로고
    • Manganese superoxide dismutase modulates interleukin-1α levels in HT-1080 fibrosarcoma cells
    • Melendez, J. A., and Davies, K. J. A. Manganese superoxide dismutase modulates interleukin-1α levels in HT-1080 fibrosarcoma cells. J. Biol. Chem., 271: 18898-18903, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18898-18903
    • Melendez, J.A.1    Davies, K.J.A.2
  • 64
    • 85052774941 scopus 로고
    • Catalase activity
    • R. A. Greenwald (ed.), Boca Raton, FL: CRC Press, Inc.
    • Claiborne, A. Catalase activity. In: R. A. Greenwald (ed.), CRC Handbook of Methods for Oxygen Radical Research, pp. 283-284. Boca Raton, FL: CRC Press, Inc., 1985.
    • (1985) CRC Handbook of Methods for Oxygen Radical Research , pp. 283-284
    • Claiborne, A.1
  • 65
    • 0017831243 scopus 로고
    • Glutathione peroxidase and hydroperoxides
    • Tappel, A. L. Glutathione peroxidase and hydroperoxides. Methods Enzymol., 52: 506-513, 1978.
    • (1978) Methods Enzymol. , vol.52 , pp. 506-513
    • Tappel, A.L.1
  • 66
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and Fridovich, I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem., 244: 6049-6055, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 67
    • 0023616072 scopus 로고
    • Antioxidants protect cultured bovine lung endothelial cells from injury by endotoxin
    • Brigham, K. L., Meyrick, B., Berry, L. C., Jr., and Repine, J. E. Antioxidants protect cultured bovine lung endothelial cells from injury by endotoxin. J. Appl. Physiol., 63: 840-850, 1987.
    • (1987) J. Appl. Physiol. , vol.63 , pp. 840-850
    • Brigham, K.L.1    Meyrick, B.2    Berry L.C., Jr.3    Repine, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.