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Volumn 1703, Issue 2, 2005, Pages 135-140

Methionine oxidation and aging

Author keywords

Aging; Methionine; Methionine sulfoxide; Methionine sulfoxide reductase

Indexed keywords

AMINO ACID; CELL ENZYME; CYSTEINE; METHIONINE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFUR AMINO ACID; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 12844268130     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.08.010     Document Type: Review
Times cited : (349)

References (47)
  • 1
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • W. Vogt Oxidation of methionyl residues in proteins: tools, targets, and reversal Free Radic. Biol. Med. 18 1995 93 105
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 2
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide reductase in proteins
    • N. Brot, and H. Weissbach Biochemistry and physiological role of methionine sulfoxide reductase in proteins Arch. Biochem. Biophys. 223 1983 271 281
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 3
    • 0032522103 scopus 로고    scopus 로고
    • One-electron photooxidation of N-methionyl peptides. Mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complexes with oxygen or superoxide
    • B.L. Miller, K. Kuczera, and C. Schöneich One-electron photooxidation of N-methionyl peptides. Mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complexes with oxygen or superoxide J. Am. Chem. Soc. 120 1998 3345 3356
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3345-3356
    • Miller, B.L.1    Kuczera, K.2    Schöneich, C.3
  • 5
    • 0032815727 scopus 로고    scopus 로고
    • Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase
    • V.S. Sharov, D.A. Ferrington, T.C. Squier, and C. Schöneich Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase FEBS Lett. 455 1999 247 250
    • (1999) FEBS Lett. , vol.455 , pp. 247-250
    • Sharov, V.S.1    Ferrington, D.A.2    Squier, T.C.3    Schöneich, C.4
  • 6
    • 0034669358 scopus 로고    scopus 로고
    • Diastereoselective protein methionine oxidation by reactive oxygen species and diastereoselective repair by methionine sulfoxide reductase
    • V.S. Sharov, and C. Schöneich Diastereoselective protein methionine oxidation by reactive oxygen species and diastereoselective repair by methionine sulfoxide reductase Free Radic. Biol. Med. 29 2000 986 994
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 986-994
    • Sharov, V.S.1    Schöneich, C.2
  • 8
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • J. Moskovitz, V.K. Singh, J. Requena, B.J. Wilkinson, R.K. Jayaswal, and E.R. Stadtman Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity Biochem. Biophys. Res. Commun. 290 2002 62 65
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5    Stadtman, E.R.6
  • 10
    • 0030955353 scopus 로고    scopus 로고
    • The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
    • J. Moskovitz, B.S. Berlett, J.M. Poston, and E.R. Stadtman The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo Proc. Natl. Acad. Sci. U. S. A. 94 1997 (Sep. 2) 9585 9589
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9585-9589
    • Moskovitz, J.1    Berlett, B.S.2    Poston, J.M.3    Stadtman, E.R.4
  • 11
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
    • J. Moskovitz, M.A. Rahman, J. Strassman, S.O. Yancey, S.R. Kushner, N. Brot, and H. Weissbach Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage J. Bacteriol. 177 1995 502 507
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 12
    • 2442701595 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase a (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages
    • T. Douglas, D.S. Daniel, B.K. Parida, C. Jagannath, and S. Dhandayuthapani Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages J. Bacteriol. 186 2004 3590 3598
    • (2004) J. Bacteriol. , vol.186 , pp. 3590-3598
    • Douglas, T.1    Daniel, D.S.2    Parida, B.K.3    Jagannath, C.4    Dhandayuthapani, S.5
  • 13
    • 0035859807 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
    • G. St. John, N. Brot, J. Ruan, H. Erdjument-Bromage, P. Tempst, H. Weissbach, and C. Nathan Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates Proc. Natl. Acad. Sci. U. S. A. 98 2001 9901 9906
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9901-9906
    • St. John, G.1    Brot, N.2    Ruan, J.3    Erdjument-Bromage, H.4    Tempst, P.5    Weissbach, H.6    Nathan, C.7
  • 15
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
    • J. Moskovitz, E. Flescher, B.S. Berlett, J. Azare, J.M. Poston, and E.R. Stadtman Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress Proc. Natl. Acad. Sci. U. S. A. 95 1998 14071 14075
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.4    Poston, J.M.5    Stadtman, E.R.6
  • 18
    • 0029860843 scopus 로고    scopus 로고
    • Mechanism of sulfoxide formation through reaction of sulfur radical cation complexes with superoxide or hydroxide ion in oxygenated aqueous solution
    • B.L. Miller, T.D. Williams, and C. Schöneich Mechanism of sulfoxide formation through reaction of sulfur radical cation complexes with superoxide or hydroxide ion in oxygenated aqueous solution J. Am. Chem. Soc. 118 1996 11014 11025
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11014-11025
    • Miller, B.L.1    Williams, T.D.2    Schöneich, C.3
  • 19
    • 0000609722 scopus 로고    scopus 로고
    • Oxidation of methionine peptides by Fenton systems: The importance of peptide sequence, neighboring groups, and EDTA
    • C. Schöneich, and J. Yang Oxidation of methionine peptides by Fenton systems: the importance of peptide sequence, neighboring groups, and EDTA J. Chem. Soc., Perkin Trans. 2 1996 915 923
    • (1996) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 915-923
    • Schöneich, C.1    Yang, J.2
  • 20
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • E.R. Stadtman, J. Moskovitz, B.S. Berlett, and R.L. Levine Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism Mol. Cell. Biochem. 234-235 2002 3 9
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 21
    • 0035339675 scopus 로고    scopus 로고
    • Rat peptide methionine sulfoxide reductase: Cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging
    • I. Petropoulos, J. Mary, M. Perichon, and B. Friguet Rat peptide methionine sulfoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging Biochem. J. 355 2001 819 825
    • (2001) Biochem. J. , vol.355 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 22
    • 0032823578 scopus 로고    scopus 로고
    • Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain
    • S.P. Gabbita, M.Y. Aksenov, M.A. Lovell, and W.R. Markesbery Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain J. Neurochem. 73 1999 1660 1666
    • (1999) J. Neurochem. , vol.73 , pp. 1660-1666
    • Gabbita, S.P.1    Aksenov, M.Y.2    Lovell, M.A.3    Markesbery, W.R.4
  • 23
    • 0021140554 scopus 로고
    • Inactivation of human alpha-1-proteinase inhibitor by gas-phase cigarette smoke
    • W.A. Pryor, M.M. Dooley, and D.F. Church Inactivation of human alpha-1-proteinase inhibitor by gas-phase cigarette smoke Biochem. Biophys. Res. Commun. 122 1984 676 681
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 676-681
    • Pryor, W.A.1    Dooley, M.M.2    Church, D.F.3
  • 24
    • 0026098629 scopus 로고
    • Increased levels of oxidized methionine residues in bronchoalveolar lavage fluid proteins from patients with idiopathic pulmonary fibrosis
    • K. Maier, L. Leuschel, and U. Costabel Increased levels of oxidized methionine residues in bronchoalveolar lavage fluid proteins from patients with idiopathic pulmonary fibrosis Am. Rev. Respir. Dis. 143 1991 271 274
    • (1991) Am. Rev. Respir. Dis. , vol.143 , pp. 271-274
    • Maier, K.1    Leuschel, L.2    Costabel, U.3
  • 26
    • 9144274018 scopus 로고    scopus 로고
    • Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein
    • M.J. Hokenson, V.N. Uversky, J. Goers, G. Yamin, L.A. Munishkina, and A.L. Fink Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein Biochemistry 43 2004 4621 4633
    • (2004) Biochemistry , vol.43 , pp. 4621-4633
    • Hokenson, M.J.1    Uversky, V.N.2    Goers, J.3    Yamin, G.4    Munishkina, L.A.5    Fink, A.L.6
  • 27
    • 0028218937 scopus 로고
    • Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens
    • N. Fujii, Y. Ishibashi, K. Satoh, M. Fujino, and K. Harada Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens Biochim. Biophys. Acta 1204 1994 157 163
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 157-163
    • Fujii, N.1    Ishibashi, Y.2    Satoh, K.3    Fujino, M.4    Harada, K.5
  • 28
    • 0008318301 scopus 로고
    • Selective oxidation of cysteine and methionine in normal and senile cataractous lenses
    • M.H. Garner, and A. Spector Selective oxidation of cysteine and methionine in normal and senile cataractous lenses Proc. Natl. Acad. Sci. U. S. A. 77 1980 1274 1277
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1274-1277
    • Garner, M.H.1    Spector, A.2
  • 29
    • 0019199118 scopus 로고
    • Pyrolysis mass spectra, sulfhydryl and tryptophan content of the embryonic nuclei from adult human normal and nuclear-cataractous lenses
    • P.M. van Haard, H.J. Hoenders, J. Wollensak, and J. Haverkamp Pyrolysis mass spectra, sulfhydryl and tryptophan content of the embryonic nuclei from adult human normal and nuclear-cataractous lenses Biochim. Biophys. Acta 631 1980 177 187
    • (1980) Biochim. Biophys. Acta , vol.631 , pp. 177-187
    • Van Haard, P.M.1    Hoenders, H.J.2    Wollensak, J.3    Haverkamp, J.4
  • 30
    • 0020511018 scopus 로고
    • Age-related changes in the composition of proteins in the trabecular meshwork of the human eye
    • H.J. Horstmann, J.W. Rohen, and K. Sames Age-related changes in the composition of proteins in the trabecular meshwork of the human eye Mech. Ageing Dev. 21 1983 121 136
    • (1983) Mech. Ageing Dev. , vol.21 , pp. 121-136
    • Horstmann, H.J.1    Rohen, J.W.2    Sames, K.3
  • 31
    • 12844276988 scopus 로고
    • Methionine sulfoxide is found in the protein of the trabecular meshwork of the human eye
    • H.J. Horstmann, K. Sames, and J.W. Rohen Methionine sulfoxide is found in the protein of the trabecular meshwork of the human eye Eur. J. Cell Biol. 20 1979 122
    • (1979) Eur. J. Cell Biol. , vol.20 , pp. 122
    • Horstmann, H.J.1    Sames, K.2    Rohen, J.W.3
  • 32
    • 0030866161 scopus 로고    scopus 로고
    • Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes. Evidence against a generalized increase in oxidative stress in diabetes
    • M.C. Wells-Knecht, T.J. Lyons, D.R. McCance, S.R. Thorpe, and J.W. Baynes Age-dependent increase in ortho-tyrosine and methionine sulfoxide in human skin collagen is not accelerated in diabetes. Evidence against a generalized increase in oxidative stress in diabetes J. Clin. Invest. 100 1997 839 846
    • (1997) J. Clin. Invest. , vol.100 , pp. 839-846
    • Wells-Knecht, M.C.1    Lyons, T.J.2    McCance, D.R.3    Thorpe, S.R.4    Baynes, J.W.5
  • 36
    • 0032581012 scopus 로고    scopus 로고
    • Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase
    • J. Gao, D. Yin, Y. Yao, T.D. Williams, and T.C. Squier Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase Biochemistry 37 1998 9536 9548
    • (1998) Biochemistry , vol.37 , pp. 9536-9548
    • Gao, J.1    Yin, D.2    Yao, Y.3    Williams, T.D.4    Squier, T.C.5
  • 37
    • 0842346324 scopus 로고    scopus 로고
    • The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts
    • C.R. Picot, M. Perichon, J.C. Cintrat, B. Friguet, and I. Petropoulos The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts FEBS Lett. 558 2004 74 78
    • (2004) FEBS Lett. , vol.558 , pp. 74-78
    • Picot, C.R.1    Perichon, M.2    Cintrat, J.C.3    Friguet, B.4    Petropoulos, I.5
  • 38
    • 0032561328 scopus 로고    scopus 로고
    • Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
    • M.D. Williams, H. Van Remmen, C.C. Conrad, T.T. Huang, C.J. Epstein, and A. Richardson Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice J. Biol. Chem. 273 1998 28510 28515
    • (1998) J. Biol. Chem. , vol.273 , pp. 28510-28515
    • Williams, M.D.1    Van Remmen, H.2    Conrad, C.C.3    Huang, T.T.4    Epstein, C.J.5    Richardson, A.6
  • 39
    • 0029912239 scopus 로고    scopus 로고
    • Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues
    • J. Moskovitz, N.A. Jenkins, D.J. Gilbert, N.G. Copeland, F. Jursky, H. Weissbach, and N. Brot Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues Proc. Natl. Acad. Sci. U. S. A. 93 1996 3205 3208
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3205-3208
    • Moskovitz, J.1    Jenkins, N.A.2    Gilbert, D.J.3    Copeland, N.G.4    Jursky, F.5    Weissbach, H.6    Brot, N.7
  • 40
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • C.C. Chao, Y.S. Ma, and E.R. Stadtman Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems Proc. Natl. Acad. Sci. U. S. A. 94 1997 2969 2974
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2969-2974
    • Chao, C.C.1    Ma, Y.S.2    Stadtman, E.R.3
  • 42
    • 0025832844 scopus 로고
    • Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-a-phenylnitrone
    • J.M. Carney, P.E. Starke-Reed, C.N. Oliver, R.W. Landrum, M.S. Cheng, J.F. Wu, and R.A. Floyd Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-a- phenylnitrone Proc. Natl. Acad. Sci. U. S. A. 88 1991 3633 3636
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3633-3636
    • Carney, J.M.1    Starke-Reed, P.E.2    Oliver, C.N.3    Landrum, R.W.4    Cheng, M.S.5    Wu, J.F.6    Floyd, R.A.7
  • 43
    • 0024788456 scopus 로고
    • Protein oxidation and proteolysis during aging and oxidative stress
    • P.E. Starke-Reed, and C.N. Oliver Protein oxidation and proteolysis during aging and oxidative stress Arch. Biochem. Biophys. 275 1989 559 567
    • (1989) Arch. Biochem. Biophys. , vol.275 , pp. 559-567
    • Starke-Reed, P.E.1    Oliver, C.N.2
  • 46
    • 0021021424 scopus 로고
    • Oxidation of methionine residues in proteins of activated human neutrophils
    • H. Fliss, H. Weissbach, and N. Brot Oxidation of methionine residues in proteins of activated human neutrophils Proc. Natl. Acad. Sci. U. S. A. 80 1983 7160 7164
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 7160-7164
    • Fliss, H.1    Weissbach, H.2    Brot, N.3
  • 47
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity
    • C. Taggart, D. Cervantes-Laurean, G. Kim, N.G. McElvaney, N. Wehr, J. Moss, and R.L. Levine Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity J. Biol. Chem. 275 2000 27258 27265
    • (2000) J. Biol. Chem. , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3    McElvaney, N.G.4    Wehr, N.5    Moss, J.6    Levine, R.L.7


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