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Volumn 50, Issue 3, 2004, Pages 277-285

Effect of long-term excessive L-methionine consumption on transferrin receptor abundance and mitochondrial H2O2 generation in rat liver

Author keywords

H2O2 generation; Iron metabolism; Methionine; Mitochondria; Transferrin receptor

Indexed keywords

GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; IRON; METHIONINE; TRANSFERRIN RECEPTOR;

EID: 24344504943     PISSN: 13449702     EISSN: None     Source Type: Journal    
DOI: 10.1248/jhs.50.277     Document Type: Article
Times cited : (6)

References (38)
  • 2
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell, B. and Gutteridge, J. M. (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol., 186, 1-85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 3
    • 0002573398 scopus 로고    scopus 로고
    • The IRE, the IRP and cytosolic aconitase: Posttranslational regulation of mammalian iron metabolism
    • (Silver, S. and Walden W., eds.), Chapman and Hall, NewYork
    • Eisenstein, R. S., Kennedy, M. C. and Bennert, H. (1997) The IRE, the IRP and cytosolic aconitase: posttranslational regulation of mammalian iron metabolism. In Metal Ions and Gene Regulation (Silver, S. and Walden W., eds.), Chapman and Hall, NewYork, pp. 157-216.
    • (1997) Metal Ions and Gene Regulation , pp. 157-216
    • Eisenstein, R.S.1    Kennedy, M.C.2    Bennert, H.3
  • 4
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze, M. W. and Kühn, L. C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. U.S.A., 93, 8175-8182.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 5
    • 0027452550 scopus 로고
    • Regulating the rate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., Rouault, T. A. and Harford, J. B. (1993) Regulating the rate of mRNA: the control of cellular iron metabolism. Cell, 72, 19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 7
    • 0032410688 scopus 로고    scopus 로고
    • Iron regulatory proteins, iron responsive elements and iron homeostasis
    • Eisenstein, R. S. and Blemings, K. P. (1998) Iron regulatory proteins, iron responsive elements and iron homeostasis. J. Nutr., 128, 2295-2298.
    • (1998) J. Nutr. , vol.128 , pp. 2295-2298
    • Eisenstein, R.S.1    Blemings, K.P.2
  • 9
    • 0030806863 scopus 로고    scopus 로고
    • 2-), superoxide dismutase, and related matters
    • -), superoxide dismutase, and related matters. J. Biol. Chem., 272, 18515-18517.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 10
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H. and Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol. Rev., 59, 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 11
    • 0033858010 scopus 로고    scopus 로고
    • Long-term consumption of a methionine-supplemented diet increases iron and lipid peroxide levels in rat liver
    • Mori, N. and Hirayama, K. (2000) Long-term consumption of a methionine-supplemented diet increases iron and lipid peroxide levels in rat liver. J. Nutr., 130, 2349-2355.
    • (2000) J. Nutr. , vol.130 , pp. 2349-2355
    • Mori, N.1    Hirayama, K.2
  • 12
    • 0027487229 scopus 로고
    • AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet
    • Reeves, P. G., Nielsen, F. H. and Fahey, G. C. (1993) AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J. Nutr., 123, 1939-1951.
    • (1993) J. Nutr. , vol.123 , pp. 1939-1951
    • Reeves, P.G.1    Nielsen, F.H.2    Fahey, G.C.3
  • 13
    • 0025303916 scopus 로고
    • Transferrin receptor expression in rat liver: Immunohistochemical and biochemical analysis of the effect of age and iron storage
    • Sciot, R., Verhoeven, G., van Eyken, P., Cailleau, J. and Desmet, V. J. (1990) Transferrin receptor expression in rat liver: Immunohistochemical and biochemical analysis of the effect of age and iron storage. Hepatology, 11, 416-427.
    • (1990) Hepatology , vol.11 , pp. 416-427
    • Sciot, R.1    Verhoeven, G.2    Van Eyken, P.3    Cailleau, J.4    Desmet, V.J.5
  • 14
    • 0002675717 scopus 로고
    • Mitochondrial isolation from liver and kidney: Strategy, techniques, and criteria for purity
    • (Lash, L. H. and Jones, D. P., eds.), Academic Press, San Diego
    • Lash, L. H. and Sall, J. M. (1993) Mitochondrial isolation from liver and kidney: strategy, techniques, and criteria for purity. In Methods in Toxicology: Mitochondrial dysfunction (Lash, L. H. and Jones, D. P., eds.), Academic Press, San Diego, pp. 8-28.
    • (1993) Methods in Toxicology: Mitochondrial Dysfunction , pp. 8-28
    • Lash, L.H.1    Sall, J.M.2
  • 16
    • 77957003282 scopus 로고
    • Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios
    • Estabrook, R. W. (1967) Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios. Methods Enzymol., 10, 41-47.
    • (1967) Methods Enzymol. , vol.10 , pp. 41-47
    • Estabrook, R.W.1
  • 17
    • 0020642791 scopus 로고
    • 2 production by macrophages and Neutrophils with Homovanillic acid and horse-radish peroxidase
    • 2 production by macrophages and Neutrophils with Homovanillic acid and horse-radish peroxidase. J. Immunol. Methods, 63, 347-357.
    • (1983) J. Immunol. Methods , vol.63 , pp. 347-357
    • Ruch, W.1    Cooper, P.H.2    Baggiolini, M.3
  • 18
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium-deficient rat liver
    • Lawrence, R. A. and Bürk, R. F. (1976) Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun., 71, 952-958.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Bürk, R.F.2
  • 19
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz, D. R. and Oberley, L. W. (1989) An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal. Biochem., 179, 8-18.
    • (1989) Anal. Biochem. , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 20
    • 0032540274 scopus 로고    scopus 로고
    • Converse modulation of IRP1 and IRP2 by immunological stimuli in murine RAW 264.7 macrophages
    • Bouton, C., Oliveira, L. and Drapier, J. C. (1998) Converse modulation of IRP1 and IRP2 by immunological stimuli in murine RAW 264.7 macrophages. J. Biol. Chem., 273, 9403-9408.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9403-9408
    • Bouton, C.1    Oliveira, L.2    Drapier, J.C.3
  • 21
    • 0030873539 scopus 로고    scopus 로고
    • An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide
    • Kennedy, M. C., Antholine, W. E. and Beinert, H. (1997) An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide. J. Biol. Chem., 272, 20340-20347.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20340-20347
    • Kennedy, M.C.1    Antholine, W.E.2    Beinert, H.3
  • 22
    • 0032571304 scopus 로고    scopus 로고
    • Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxigenation
    • Hanson, E. S. and Leibold, E. A. (1998) Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxigenation. J. Biol. Chem., 273, 7588-7593.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7588-7593
    • Hanson, E.S.1    Leibold, E.A.2
  • 23
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins, E. A., Robalinho, R. L. and Meneghini, R. (1995) Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Arch. Biochem. Biophys., 316, 128-134.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 24
    • 0032167632 scopus 로고    scopus 로고
    • Activation of iron regulatory protein-1 by oxidative stress in vitro
    • Pantopoulos, K. and Hentze, M. W. (1998) Activation of iron regulatory protein-1 by oxidative stress in vitro. Proc. Natl. Acad. Sci. U.S.A., 95, 10559-10563.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10559-10563
    • Pantopoulos, K.1    Hentze, M.W.2
  • 25
    • 0035827697 scopus 로고    scopus 로고
    • 2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts
    • 2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts. J. Biol. Chem., 276, 19738-19745.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19738-19745
    • Caltagirone, A.1    Weiss, G.2    Pantopoulos, K.3
  • 26
    • 0026673472 scopus 로고
    • Mitochondrial production of pro-oxidants and cellular senescence
    • Sohal, R. S. and Brunk, U. T. (1992) Mitochondrial production of pro-oxidants and cellular senescence. Mutat. Res., 275, 295-304.
    • (1992) Mutat. Res. , vol.275 , pp. 295-304
    • Sohal, R.S.1    Brunk, U.T.2
  • 27
    • 0034751958 scopus 로고    scopus 로고
    • 2 production and oxidative DNA damage in rat liver mitochondria and location of the free radical source
    • 2 production and oxidative DNA damage in rat liver mitochondria and location of the free radical source. J. Bioenerg. Biomembr., 33, 279-287.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 279-287
    • Gredilla, R.1    Barja, G.2    López-Torres, M.3
  • 28
    • 0036569788 scopus 로고    scopus 로고
    • Influence of aging and long-term caloric restriction on oxygen radical generation and oxidative and DNA damage in rat liver mitochondria
    • López-Torres, M. Gredilla, R., Sanz, A. and Baria, G. (2002) Influence of aging and long-term caloric restriction on oxygen radical generation and oxidative and DNA damage in rat liver mitochondria. Free Radic. Biol. Med., 32, 882-889.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 882-889
    • López-Torres, M.1    Gredilla, R.2    Sanz, A.3    Baria, G.4
  • 29
    • 0023032002 scopus 로고
    • Methionine metabolism in mammals
    • Finkelstein, J. D. and Martin, J. J. (1986) Methionine metabolism in mammals. J. Biol. Chem., 261, 1582-1587.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1582-1587
    • Finkelstein, J.D.1    Martin, J.J.2
  • 30
    • 0002601998 scopus 로고
    • Mitochondrial generation of reactive oxygen species
    • (Paulet, A., Douste-Blazy, L. and Paoletti, R., eds.), Plenum Press, New York
    • Turrens, J. F. and McCord, J. M. (1990) Mitochondrial generation of reactive oxygen species. In Free Rradicals, Lipoproteins, and Membrane Lipids (Paulet, A., Douste-Blazy, L. and Paoletti, R., eds.), Plenum Press, New York, pp. 203-212.
    • (1990) Free Rradicals, Lipoproteins, and Membrane Lipids , pp. 203-212
    • Turrens, J.F.1    McCord, J.M.2
  • 31
    • 0002437327 scopus 로고
    • Production of superoxide in mitochondria
    • (Oberley, L. W., ed.), CRC Press, Boca Ratan
    • Boveris, A. and Cadenas, E. (1982) Production of superoxide in mitochondria. In Superoxid Dismutase, II (Oberley, L. W., ed.), CRC Press, Boca Ratan, pp. 15-30.
    • (1982) Superoxid Dismutase, II , pp. 15-30
    • Boveris, A.1    Cadenas, E.2
  • 32
    • 0001837912 scopus 로고
    • Superoxide radical and hydrogen peroxide in mitochondria
    • (Pryor, W. A., ed.), Academic Press, New York
    • Forman, H. J. and Boveris, A. (1982) Superoxide radical and hydrogen peroxide in mitochondria. In Free Radicals in Biology (Pryor, W. A., ed.), Academic Press, New York, pp. 65-90.
    • (1982) Free Radicals in Biology , pp. 65-90
    • Forman, H.J.1    Boveris, A.2
  • 34
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja, G. (1999) Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr., 31, 347-366.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 347-366
    • Barja, G.1
  • 35
    • 0015319592 scopus 로고
    • The biological clock
    • Harman, D. (1972) The biological clock. J. Am. Geriatr. Soc., 20, 145-147.
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 36
    • 0026023219 scopus 로고
    • Hydrogen peroxide release by mitochondria increases during aging
    • Sohal, R. S. and Sohal, B. H. (1991) Hydrogen peroxide release by mitochondria increases during aging. Mech. Ageing Dev., 57, 187-202.
    • (1991) Mech. Ageing Dev. , vol.57 , pp. 187-202
    • Sohal, R.S.1    Sohal, B.H.2
  • 37
    • 0028342438 scopus 로고
    • Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse
    • Sohal, R. S., Ku, H.-H., Agarwal, S. Forster, M. J. and Lal, H. (1994) Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse. Mech. Aging Dev., 74, 121-133.
    • (1994) Mech. Aging Dev. , vol.74 , pp. 121-133
    • Sohal, R.S.1    Ku, H.-H.2    Agarwal, S.3    Forster, M.J.4    Lal, H.5
  • 38
    • 0035933846 scopus 로고    scopus 로고
    • IRP1 activation by extracellular oxidative stress in the perfused rat liver
    • Mueller, A., Pantopoulos, K., Hübner, C. A., Stremmel, W. and Hentze, M. W. (2001) IRP1 activation by extracellular oxidative stress in the perfused rat liver. J. Biol. Chem., 276, 23192-23196.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23192-23196
    • Mueller, A.1    Pantopoulos, K.2    Hübner, C.A.3    Stremmel, W.4    Hentze, M.W.5


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