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Volumn 44, Issue 2, 2009, Pages 101-106

Liposome membrane can act like molecular and metal chaperones for oxidized and fragmented superoxide dismutase

Author keywords

Chaperones; Enzymatic activity; Hydrogen peroxide; Liposomes; Superoxide dismutase

Indexed keywords

COPPER; HYDROGEN; HYDROGEN PEROXIDE; OXIDATION; OXYGEN; PHOSPHOLIPIDS; ZINC;

EID: 57549085702     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.10.012     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 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 (1969) 6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 2
    • 0032699972 scopus 로고    scopus 로고
    • Fragmentation of human ceruloplasmin induced by hydrogen peroxide
    • Choi S.Y., Kwon H.Y., Kwon O.B., and Kang J.W. Fragmentation of human ceruloplasmin induced by hydrogen peroxide. Biochim Biophys Acta 1472 (1999) 651-657
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 651-657
    • Choi, S.Y.1    Kwon, H.Y.2    Kwon, O.B.3    Kang, J.W.4
  • 3
    • 0031592750 scopus 로고    scopus 로고
    • Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction
    • Kang J.H., and Kim S.M. Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction. Mol Cell 7 (1997) 553-558
    • (1997) Mol Cell , vol.7 , pp. 553-558
    • Kang, J.H.1    Kim, S.M.2
  • 4
    • 0025358959 scopus 로고
    • Undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo D.C., Pacifici R.E., Lin S.W., Giulivi C., and Davies K.J.A. Undergoes proteolysis and fragmentation following oxidative modification and inactivation. J Biol Chem 265 (1990) 11919-11927
    • (1990) J Biol Chem , vol.265 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Lin, S.W.3    Giulivi, C.4    Davies, K.J.A.5
  • 5
    • 0027980816 scopus 로고
    • 2. Selective generation of 2-oxo-histidine at the histidine 118
    • 2. Selective generation of 2-oxo-histidine at the histidine 118. J Biol Chem 269 (1994) 2405-2410
    • (1994) J Biol Chem , vol.269 , pp. 2405-2410
    • Uchida, K.1    Kawakishi, S.2
  • 7
    • 0033555968 scopus 로고    scopus 로고
    • Bicarbonate is required for the peroxidase function of Cu,Zn-superoxide dismutase at physicological pH
    • Sankarapandi S., and Zweier J.L. Bicarbonate is required for the peroxidase function of Cu,Zn-superoxide dismutase at physicological pH. J Biol Chem 257 (1999) 1226-1232
    • (1999) J Biol Chem , vol.257 , pp. 1226-1232
    • Sankarapandi, S.1    Zweier, J.L.2
  • 8
  • 9
    • 10644225292 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immuno-spin trapping: role of copper- and carbonate radical anion-mediated oxidations
    • Ramirez D.C., Mejiba S.E.G., and Mason R.P. Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immuno-spin trapping: role of copper- and carbonate radical anion-mediated oxidations. Free Radic Biol Med 38 (2005) 201-214
    • (2005) Free Radic Biol Med , vol.38 , pp. 201-214
    • Ramirez, D.C.1    Mejiba, S.E.G.2    Mason, R.P.3
  • 10
    • 0034144361 scopus 로고    scopus 로고
    • Fragmentation of human ceruloplasmin induced by hydrogen peroxide
    • Choi S.Y., Kwon H.Y., Kwon O.B., Eum W.S., and Kang J.H. Fragmentation of human ceruloplasmin induced by hydrogen peroxide. Biochimie 82 (2000) 175-180
    • (2000) Biochimie , vol.82 , pp. 175-180
    • Choi, S.Y.1    Kwon, H.Y.2    Kwon, O.B.3    Eum, W.S.4    Kang, J.H.5
  • 11
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies K.T.A. Protein damage and degradation by oxygen radicals. I. General aspects. J Biol Chem 262 (1987) 9895-9901
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.T.A.1
  • 12
    • 0021104498 scopus 로고
    • -2, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: modification of one histidine per subunit
    • -2, is an affinity reagent for the inactivation of yeast Cu,Zn superoxide dismutase: modification of one histidine per subunit. Arch Biochem Biophys 224 (1983) 579-586
    • (1983) Arch Biochem Biophys , vol.224 , pp. 579-586
    • Blech, D.M.1    Borders Jr., C.L.2
  • 13
    • 0037088291 scopus 로고    scopus 로고
    • Protective effects of carnosine, homocarnosine and anserine against peroxyl radical-mediated Cu,Zn-superoxide dismutase modification
    • Kang J.H., Kim K.S., Choi S.Y., Kwon H.Y., Won M.H., and Kang T.C. Protective effects of carnosine, homocarnosine and anserine against peroxyl radical-mediated Cu,Zn-superoxide dismutase modification. Biochim Biophys Acta 1570 (2002) 89-96
    • (2002) Biochim Biophys Acta , vol.1570 , pp. 89-96
    • Kang, J.H.1    Kim, K.S.2    Choi, S.Y.3    Kwon, H.Y.4    Won, M.H.5    Kang, T.C.6
  • 14
    • 38749088302 scopus 로고    scopus 로고
    • Liposome-recruited activity of oxidized and fragmented superoxide dismutase
    • Tuan L.Q., Umakoshi H., Shimanouchi T., and Kuboi R. Liposome-recruited activity of oxidized and fragmented superoxide dismutase. Langmuir 24 (2008) 350-354
    • (2008) Langmuir , vol.24 , pp. 350-354
    • Tuan, L.Q.1    Umakoshi, H.2    Shimanouchi, T.3    Kuboi, R.4
  • 15
    • 0026732669 scopus 로고
    • Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species
    • Ookawara T., Kawamura N., Kitagawas Y., and Taniguchi N. Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J Biol Chem 267 (1992) 18505-18510
    • (1992) J Biol Chem , vol.267 , pp. 18505-18510
    • Ookawara, T.1    Kawamura, N.2    Kitagawas, Y.3    Taniguchi, N.4
  • 16
    • 0035955156 scopus 로고    scopus 로고
    • 2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS,MS/MS for the determination of the copper-binding site
    • 2-treated Cu,Zn-SOD protein with LC-ESI-Q-TOF-MS,MS/MS for the determination of the copper-binding site. J Am Chem Soc 123 (2001) 9268-9278
    • (2001) J Am Chem Soc , vol.123 , pp. 9268-9278
    • Kurahashi, T.1    Miyazaki, A.2    Suwan, S.3    Isobe, M.4
  • 17
    • 0033006157 scopus 로고    scopus 로고
    • Oxidative refolding of denatured/reduced lyzozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography
    • Yoshimoto M., and Kuboi R. Oxidative refolding of denatured/reduced lyzozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography. Biotechnol Prog 15 (1999) 480-487
    • (1999) Biotechnol Prog , vol.15 , pp. 480-487
    • Yoshimoto, M.1    Kuboi, R.2
  • 18
    • 0034705747 scopus 로고    scopus 로고
    • Immobilized liposome chromatography for refolding and purification of protein
    • Yoshimoto M., Shimanouchi T., Umakoshi H., and Kuboi R. Immobilized liposome chromatography for refolding and purification of protein. J Chromatogr B 743 (2000) 93-99
    • (2000) J Chromatogr B , vol.743 , pp. 93-99
    • Yoshimoto, M.1    Shimanouchi, T.2    Umakoshi, H.3    Kuboi, R.4
  • 19
    • 0034233061 scopus 로고    scopus 로고
    • Oxidative refolding of lysozyme assisted by negatively charged liposomes: relationship with lysozyme-mediated fusion of liposomes
    • Kuboi K., Mawatari T., and Yoshimoto M. Oxidative refolding of lysozyme assisted by negatively charged liposomes: relationship with lysozyme-mediated fusion of liposomes. J Biosci Bioeng 90 (2000) 14-19
    • (2000) J Biosci Bioeng , vol.90 , pp. 14-19
    • Kuboi, K.1    Mawatari, T.2    Yoshimoto, M.3
  • 20
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen Y.H., Yang J.T., and Chau K.H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13 (1974) 3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 21
    • 0033950664 scopus 로고    scopus 로고
    • A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1)
    • Peskin A.V., and Winterbourn C.C. A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1). Clin Chim Acta 293 (2000) 157-166
    • (2000) Clin Chim Acta , vol.293 , pp. 157-166
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 22
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals. Modification of secondary and tertiary structure
    • Davis K.J.A., and Delsignore M.E. Protein damage and degradation by oxygen radicals. Modification of secondary and tertiary structure. J Biol Chem 262 (1987) 9908-9913
    • (1987) J Biol Chem , vol.262 , pp. 9908-9913
    • Davis, K.J.A.1    Delsignore, M.E.2
  • 23
    • 0344255607 scopus 로고    scopus 로고
    • Copper (II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region
    • Brown D.R., Guantieri V., Grasso G., Impellizzeri G., Pappalardo G., and Rizzarelli E. Copper (II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region. J Inorg Biochem 98 (2004) 133-143
    • (2004) J Inorg Biochem , vol.98 , pp. 133-143
    • Brown, D.R.1    Guantieri, V.2    Grasso, G.3    Impellizzeri, G.4    Pappalardo, G.5    Rizzarelli, E.6
  • 25
    • 0020710017 scopus 로고
    • Coordination modes of histidine. 4. Coordination structures in the copper(II)-l-Histidine (1:2) system
    • Casella L., and Gullotti M. Coordination modes of histidine. 4. Coordination structures in the copper(II)-l-Histidine (1:2) system. J Inorg Biochem 18 (1983) 19-31
    • (1983) J Inorg Biochem , vol.18 , pp. 19-31
    • Casella, L.1    Gullotti, M.2
  • 26
    • 0037687921 scopus 로고    scopus 로고
    • A green fluorescent chemosensor for amino acids provides a versatile high-throughput screening (HTS) assay for proteases
    • Dean K.E.S., Klein G., Renaudet O., and Reymond J.L. A green fluorescent chemosensor for amino acids provides a versatile high-throughput screening (HTS) assay for proteases. Bioorg Med Chem Lett 13 (2003) 1653-1656
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 1653-1656
    • Dean, K.E.S.1    Klein, G.2    Renaudet, O.3    Reymond, J.L.4
  • 27
    • 24644493661 scopus 로고    scopus 로고
    • An organometallic chemosensor for the sequence-selective detection of histidine- and methionine-containing peptides in water at neutral pH
    • Buryak A., and Severin K. An organometallic chemosensor for the sequence-selective detection of histidine- and methionine-containing peptides in water at neutral pH. Angew Chem 116 (2004) 4875-4878
    • (2004) Angew Chem , vol.116 , pp. 4875-4878
    • Buryak, A.1    Severin, K.2
  • 29
    • 0028880110 scopus 로고
    • Determination of 2-oxohistidine by amino acid analysis
    • Lewisch S.A., and Levine R.L. Determination of 2-oxohistidine by amino acid analysis. Anal Biochem 231 (1995) 440-446
    • (1995) Anal Biochem , vol.231 , pp. 440-446
    • Lewisch, S.A.1    Levine, R.L.2
  • 30
    • 33750534538 scopus 로고    scopus 로고
    • Multiple forms of copper(II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4
    • Wells M.A., Jelinska C., Hosszu L.L.P., Craven C.J., Clarke A.R., Collinge J., et al. Multiple forms of copper(II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4. Biochemistry 400 (2006) 501-510
    • (2006) Biochemistry , vol.400 , pp. 501-510
    • Wells, M.A.1    Jelinska, C.2    Hosszu, L.L.P.3    Craven, C.J.4    Clarke, A.R.5    Collinge, J.6
  • 32
    • 37549056246 scopus 로고    scopus 로고
    • Copper binding and conformation of the N-terminal octarepeats of the prion protein in the presence of DPC micelles as membrane mimetic
    • Dong S.L., Cadamuro S.A., Fiorino F., Bertsch U., Moroder L., and Renner C. Copper binding and conformation of the N-terminal octarepeats of the prion protein in the presence of DPC micelles as membrane mimetic. Biopolymers 88 (2007) 840-847
    • (2007) Biopolymers , vol.88 , pp. 840-847
    • Dong, S.L.1    Cadamuro, S.A.2    Fiorino, F.3    Bertsch, U.4    Moroder, L.5    Renner, C.6
  • 33
    • 57549086798 scopus 로고    scopus 로고
    • Characterization of oxidized and fragmented superoxide dismutase recruited on liposome surface
    • Tuan L.Q., Umakoshi H., Shimanouchi T., and Kuboi R. Characterization of oxidized and fragmented superoxide dismutase recruited on liposome surface. Membrane 33 (2008) 173-179
    • (2008) Membrane , vol.33 , pp. 173-179
    • Tuan, L.Q.1    Umakoshi, H.2    Shimanouchi, T.3    Kuboi, R.4
  • 36
    • 35948936850 scopus 로고    scopus 로고
    • Three histidine residues of amyloid-β peptide control the redox activity of copper and iron
    • Nakamura M., Shishido N., Nunomura A., Smith M.A., Perry G., Hayashi Y., et al. Three histidine residues of amyloid-β peptide control the redox activity of copper and iron. Biochemistry 46 (2007) 12737-12743
    • (2007) Biochemistry , vol.46 , pp. 12737-12743
    • Nakamura, M.1    Shishido, N.2    Nunomura, A.3    Smith, M.A.4    Perry, G.5    Hayashi, Y.6
  • 37
    • 0242521579 scopus 로고    scopus 로고
    • Activation of protein-bound copper ions during early glycation: study on two proteins
    • Argirova M.D., and Ortwerth B. Activation of protein-bound copper ions during early glycation: study on two proteins. Arch Biochem Biophys 420 (2003) 176-184
    • (2003) Arch Biochem Biophys , vol.420 , pp. 176-184
    • Argirova, M.D.1    Ortwerth, B.2
  • 38
    • 33751536847 scopus 로고    scopus 로고
    • The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase
    • Hörnberg A., Logan D.T., Marklund S.L., and Oliveberg M. The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J Mol Biol 365 (2007) 333-342
    • (2007) J Mol Biol , vol.365 , pp. 333-342
    • Hörnberg, A.1    Logan, D.T.2    Marklund, S.L.3    Oliveberg, M.4
  • 39
    • 1942437507 scopus 로고    scopus 로고
    • Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone
    • Carroll M.C., Girouard J.B., Ulloa J.L., Subramaniam J.R., Wong P.C., Valentine J.S., et al. Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone. PNAS 101 (2004) 5964-5969
    • (2004) PNAS , vol.101 , pp. 5964-5969
    • Carroll, M.C.1    Girouard, J.B.2    Ulloa, J.L.3    Subramaniam, J.R.4    Wong, P.C.5    Valentine, J.S.6


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