메뉴 건너뛰기




Volumn 122, Issue 2, 2004, Pages 126-132

Protein oxidation and the degradation of oxidized proteins in the rat oligodendrocyte cell line OLN 93-antioxidative effect of the intracellular spin trapping agent PBN

Author keywords

phenyl N tert butylnitrone; Cellular and molecular biology; FCS; Fetal calf serum; Neuroglia and myelin; Oligodendrocytes; Oxidative stress; PBN; Proteasome; Protein oxidation; Protein turnover

Indexed keywords

ANTIOXIDANT; HYDROGEN PEROXIDE; N TERT BUTYL ALPHA PHENYLNITRONE; OXIDIZING AGENT; PARAQUAT; PROTEASOME;

EID: 1542268910     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2003.12.005     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 17344390525 scopus 로고    scopus 로고
    • N-t-butyl hydroxylamine, a hydrolysis product of α-phenyl-N-t- butyl nitrone, is more potent in delaying senescence in human lung fibroblasts
    • Atamna H., Paler-Martinez A., Ames B.N. N-t-butyl hydroxylamine, a hydrolysis product of α-phenyl-N-t-butyl nitrone, is more potent in delaying senescence in human lung fibroblasts. J. Biol. Chem. 275:2000;6741-6748.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6741-6748
    • Atamna, H.1    Paler-Martinez, A.2    Ames, B.N.3
  • 2
    • 0021990499 scopus 로고
    • Toxicity determination in vitro by morphological alterations and neutral red absorption
    • Borenfreund E., Puerner J.A. Toxicity determination in vitro by morphological alterations and neutral red absorption. Toxicol. Lett. 24:1985;119-124.
    • (1985) Toxicol. Lett. , vol.24 , pp. 119-124
    • Borenfreund, E.1    Puerner, J.A.2
  • 3
    • 0016153291 scopus 로고
    • Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity
    • Bus J.S., Aust S.D., Gibson J.E. Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochem. Biophys. Res. Commun. 58:1974;749-755.
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 6
    • 0031029393 scopus 로고    scopus 로고
    • Free radical oxidation of brain proteins in accelerated senescence and its modulation by N-ter-butyl-α-phenylnitrone
    • Butterfield D.A., Howard B.J., Yatin S., Allen K.L., Carney J.M. Free radical oxidation of brain proteins in accelerated senescence and its modulation by N-ter-butyl-α-phenylnitrone. Proc. Natl. Acad. Sci. U. S. A. 94:1997;674-678.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 674-678
    • Butterfield, D.A.1    Howard, B.J.2    Yatin, S.3    Allen, K.L.4    Carney, J.M.5
  • 7
    • 0025932511 scopus 로고
    • Protection against oxidative damage to CNS by α-phenyl-tert-butyl- nitrone (PBN) and other spin-trapping agents: A novel series of non-lipid free radical scavengers
    • Carney J.M., Floyd R.A. Protection against oxidative damage to CNS by α-phenyl-tert-butyl-nitrone (PBN) and other spin-trapping agents: a novel series of non-lipid free radical scavengers. J. Mol. Neurosci. 3:1991;47-57.
    • (1991) J. Mol. Neurosci. , vol.3 , pp. 47-57
    • Carney, J.M.1    Floyd, R.A.2
  • 8
    • 0018776894 scopus 로고
    • Hydrogen peroxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydrogen peroxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-593.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-593
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 9
    • 0027400449 scopus 로고
    • Distribution of spin-trapping compounds in rat blood and brain: In vivo microdialysis determination
    • Cheng H.Y., Liu T., Feuerstein G., Barone F.C. Distribution of spin-trapping compounds in rat blood and brain: in vivo microdialysis determination. Free Radic. Biol. Med. 14:1993;243-250.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 243-250
    • Cheng, H.Y.1    Liu, T.2    Feuerstein, G.3    Barone, F.C.4
  • 10
    • 0030174825 scopus 로고    scopus 로고
    • Relationship of iron to oligodendrocytes and myelination
    • Connor J.R., Menzeis S.L. Relationship of iron to oligodendrocytes and myelination. Glia. 17:1996;83-93.
    • (1996) Glia , vol.17 , pp. 83-93
    • Connor, J.R.1    Menzeis, S.L.2
  • 11
    • 0025648166 scopus 로고
    • Cellular distribution of transferrin, ferritin and iron in normal and aged brains
    • Connor J.R., Menzeis S.L., St. Martin S.M., Mufson E.J. Cellular distribution of transferrin, ferritin and iron in normal and aged brains. J. Neurosci. Res. 27:1990;595-611.
    • (1990) J. Neurosci. Res. , vol.27 , pp. 595-611
    • Connor, J.R.1    Menzeis, S.L.2    St. Martin, S.M.3    Mufson, E.J.4
  • 12
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. General aspects
    • Davies K.J.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.J.A.1
  • 13
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1997;1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 15
    • 0035938294 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis in RAW264.7 macrophages: Effects of PMA activation
    • Gieche J., Mehlhase J., Licht A., Zacke T., Sitte N., Grune T. Protein oxidation and proteolysis in RAW264.7 macrophages: effects of PMA activation. Biochim. Biophys. Acta. 1538:2001;321-328.
    • (2001) Biochim. Biophys. Acta , vol.1538 , pp. 321-328
    • Gieche, J.1    Mehlhase, J.2    Licht, A.3    Zacke, T.4    Sitte, N.5    Grune, T.6
  • 16
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress
    • Grune T., Reinheckel T., Joshi M., Davies K.J.A. Proteolysis in cultured liver epithelial cells during oxidative stress. J. Biol. Chem. 270:1995;2344-2351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 17
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T., Reinheckel T., Davies K.J.A. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem. 271:1996;15504-15509.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 18
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T., Reinheckel T., Davies K.J.A. Degradation of oxidized proteins in mammalian cells. FASEB J. 11:1997;526-534.
    • (1997) FASEB J. , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 19
    • 0032080117 scopus 로고    scopus 로고
    • Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome
    • Grune T., Blasig I.E., Sitte N., Roloff B., Haseloff R., Davies K.J.A. Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome. J. Biol. Chem. 273:1998;10857-10862.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10857-10862
    • Grune, T.1    Blasig, I.E.2    Sitte, N.3    Roloff, B.4    Haseloff, R.5    Davies, K.J.A.6
  • 20
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59:1992;1609-1632.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1632
    • Halliwell, B.1
  • 22
    • 0032054439 scopus 로고    scopus 로고
    • Peroxide-scavenging deficit underlies oligodendrocyte susceptibility to oxidative stress
    • Juurlink B.J.H., Thorburne S., Hertz L. Peroxide-scavenging deficit underlies oligodendrocyte susceptibility to oxidative stress. Glia. 22:1998;371-378.
    • (1998) Glia , vol.22 , pp. 371-378
    • Juurlink, B.J.H.1    Thorburne, S.2    Hertz, L.3
  • 24
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R.L., Stadtman E.R., Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233:1994;346-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Stadtman, E.R.2    Shacter, E.3
  • 25
    • 0034456958 scopus 로고    scopus 로고
    • LPS-induced protein oxidation and proteolysis in BV-2 microglial cells
    • Mehlhase J., Gieche J., Ullrich O., Sitte N., Grune T. LPS-induced protein oxidation and proteolysis in BV-2 microglial cells. IUBMB Life. 50:2000;331-335.
    • (2000) IUBMB Life , vol.50 , pp. 331-335
    • Mehlhase, J.1    Gieche, J.2    Ullrich, O.3    Sitte, N.4    Grune, T.5
  • 26
    • 0001521560 scopus 로고
    • Molecular organization of myelin
    • P. Morrell. New York: Plenum
    • Brown P.E. Molecular organization of myelin. Morrell P. Myelin. 1984;97-116 Plenum, New York.
    • (1984) Myelin , pp. 97-116
    • Brown, P.E.1
  • 27
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski P.J. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron. 35:2002;9-12.
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 28
    • 0030017964 scopus 로고    scopus 로고
    • OLN-93: A new permanent oligodenroglia cell line derived from primary rat brain glial cultures
    • Richter-Landsberg C., Heinrich M. OLN-93: a new permanent oligodenroglia cell line derived from primary rat brain glial cultures. J. Neurosci. Res. 45:1996;161-173.
    • (1996) J. Neurosci. Res. , vol.45 , pp. 161-173
    • Richter-Landsberg, C.1    Heinrich, M.2
  • 29
    • 0028872327 scopus 로고
    • Reactive oxygen species are involved in the pathogenesis of experimental allergic encephalomyelitis in Lewis rats
    • Ruuls S.R., Bauer J., Sontrop K., Huitinga I., Hart B.A., Dijkstra C.D. Reactive oxygen species are involved in the pathogenesis of experimental allergic encephalomyelitis in Lewis rats. J. Neuroimmunol. 56:1995;207-217.
    • (1995) J. Neuroimmunol. , vol.56 , pp. 207-217
    • Ruuls, S.R.1    Bauer, J.2    Sontrop, K.3    Huitinga, I.4    Hart, B.A.5    Dijkstra, C.D.6
  • 30
    • 0035542983 scopus 로고    scopus 로고
    • Oligodendrocytes use lactate as a source of energy and as a precursor of lipids
    • Sanchez-Abarca L.I., Tabernero A., Medina J.M. Oligodendrocytes use lactate as a source of energy and as a precursor of lipids. Glia. 36:2001;321-329.
    • (2001) Glia , vol.36 , pp. 321-329
    • Sanchez-Abarca, L.I.1    Tabernero, A.2    Medina, J.M.3
  • 31
    • 0032438035 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts
    • Sitte N., Merker K., Grune T. Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts. FEBS Lett. 440:1998;399-402.
    • (1998) FEBS Lett. , vol.440 , pp. 399-402
    • Sitte, N.1    Merker, K.2    Grune, T.3
  • 33
    • 0033673408 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I. Effects of proliferative senescence
    • Sitte N., Merker K., von Zglinicki T., Grune T., Davies K.J.A. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I. Effects of proliferative senescence. FASEB J. 14:2000;2495-2502.
    • (2000) FASEB J. , vol.14 , pp. 2495-2502
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4    Davies, K.J.A.5
  • 34
    • 0033674181 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II. Aging of nondividing cells
    • Sitte N., Merker K., von Zglinicki T., Davies K.J.A., Grune T. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II. Aging of nondividing cells. FASEB J. 14:2000;2502-2510.
    • (2000) FASEB J. , vol.14 , pp. 2502-2510
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Davies, K.J.A.4    Grune, T.5
  • 35
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalysed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalysed reactions. Ann. Rev. Biochem. 62:1993;797-821.
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 36
    • 0029952689 scopus 로고    scopus 로고
    • Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure
    • Strack P.R., Waxman L., Fagan J.M. Activation of the multicatalytic endopeptidase by oxidants. Effects on enzyme structure. Biochemistry. 35:1996;7142-7149.
    • (1996) Biochemistry , vol.35 , pp. 7142-7149
    • Strack, P.R.1    Waxman, L.2    Fagan, J.M.3
  • 37
    • 0029799756 scopus 로고    scopus 로고
    • Low glutathione and high iron govern the susceptibility of oligodendroglial precursors to oxidative stress
    • Thorburne S.K., Juurlink H.J. Low glutathione and high iron govern the susceptibility of oligodendroglial precursors to oxidative stress. J. Neurochem. 67:1996;1014-1022.
    • (1996) J. Neurochem. , vol.67 , pp. 1014-1022
    • Thorburne, S.K.1    Juurlink, H.J.2
  • 38
    • 0026500136 scopus 로고
    • Evidence for increased lipid peroxidation in multiple sclerosis
    • Toshdiwal P.K., Zarling E.J. Evidence for increased lipid peroxidation in multiple sclerosis. Neurochem. Res. 17:1992;205-207.
    • (1992) Neurochem. Res. , vol.17 , pp. 205-207
    • Toshdiwal, P.K.1    Zarling, E.J.2
  • 39
    • 0034846386 scopus 로고    scopus 로고
    • Proteolysis of oxidized proteins after oxygen-glucose deprivation in rat cortical neurons is mediated by the proteasome
    • Weih M., Schmitt M., Gieche J., Harms C., Ruscher K., Dirnagl U., Grune T. Proteolysis of oxidized proteins after oxygen-glucose deprivation in rat cortical neurons is mediated by the proteasome. J. Cereb. Blood Flow Metab. 21:2001;1090-1096.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 1090-1096
    • Weih, M.1    Schmitt, M.2    Gieche, J.3    Harms, C.4    Ruscher, K.5    Dirnagl, U.6    Grune, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.