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Volumn 30, Issue 10, 2001, Pages 1137-1144

Imbalance of antioxidant defense in mice lacking cellular prion protein

Author keywords

Catalase; Free radicals; Lipid peroxidation; Ornithine decarboxylase; Oxidative stress; Prion diseases; Protein oxidation; PrPC; Superoxide dismutase

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; ORNITHINE DECARBOXYLASE; PRION PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 0035873869     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(01)00512-3     Document Type: Article
Times cited : (222)

References (39)
  • 1
    • 0030856847 scopus 로고    scopus 로고
    • Bovine spongiform encephalopathy and early onset variant Creutzfeldt-Jakob disease
    • Weissmann C., Aguzzi A. Bovine spongiform encephalopathy and early onset variant Creutzfeldt-Jakob disease. Curr. Opin. Neurobiol. 7:1997;695-700.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 695-700
    • Weissmann, C.1    Aguzzi, A.2
  • 5
    • 0032058920 scopus 로고    scopus 로고
    • A new mechanism broadening the role of prion proteins in neurodegeneration
    • Doyle D., Rogers M. A new mechanism broadening the role of prion proteins in neurodegeneration. TIG. 14:(5):1998;171-173.
    • (1998) TIG , vol.14 , Issue.5 , pp. 171-173
    • Doyle, D.1    Rogers, M.2
  • 6
    • 0027252644 scopus 로고
    • Localization of the mRNA for a chicken prion protein by in situ hybridization
    • Harris D.A., Lele P., Snider W.D. Localization of the mRNA for a chicken prion protein by in situ hybridization. Proc. Natl. Acad. Sci. USA. 90:1993;4309-4313.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4309-4313
    • Harris, D.A.1    Lele, P.2    Snider, W.D.3
  • 9
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P.C., Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:(50):1998;33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , Issue.50 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 10
    • 0032103431 scopus 로고    scopus 로고
    • Prions are copper-binding proteins
    • Prince R.C., Gunson D.E. Prions are copper-binding proteins. TIBS. 23:1998;197-198.
    • (1998) TIBS , vol.23 , pp. 197-198
    • Prince, R.C.1    Gunson, D.E.2
  • 11
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown D.R., Schulz-Schaeffer W.J., Schmidt B., Kretzschmar H.A. Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146:1997;104-112.
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 12
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown D.R., Besinger A. Prion protein expression and superoxide dismutase activity. Biochem. J. 334:1998;423-429.
    • (1998) Biochem. J. , vol.334 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 15
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris A. Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Meth. Enzymol. 105:1984;429-435.
    • (1984) Meth. Enzymol. , vol.105 , pp. 429-435
    • Boveris, A.1
  • 16
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Meth. Enzymol. 105:1984;121-126.
    • (1984) Meth. Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 17
    • 0033920575 scopus 로고    scopus 로고
    • Retinol-induced elevation of ornithine decarboxylase activity in cultured rat Sertoli cells is attenuated by free radical scavenger and by iron chelator
    • Klamt F., Dal-Pizzol F., Ribeiro N.C., Bernard E.A., Benfato M.S., Moreira J.C.F. Retinol-induced elevation of ornithine decarboxylase activity in cultured rat Sertoli cells is attenuated by free radical scavenger and by iron chelator. Mol. Cell. Biochem. 208:2000;71-76.
    • (2000) Mol. Cell. Biochem. , vol.208 , pp. 71-76
    • Klamt, F.1    Dal-Pizzol, F.2    Ribeiro, N.C.3    Bernard, E.A.4    Benfato, M.S.5    Moreira, J.C.F.6
  • 18
  • 21
    • 0030757114 scopus 로고    scopus 로고
    • Free radical induced elevation of ornithine decarboxylase activity in developing rat brain slices
    • Saito K., Packianathan S., Longo L.D. Free radical induced elevation of ornithine decarboxylase activity in developing rat brain slices. Brain Res. 763:1997;232-238.
    • (1997) Brain Res. , vol.763 , pp. 232-238
    • Saito, K.1    Packianathan, S.2    Longo, L.D.3
  • 22
    • 0029080133 scopus 로고
    • Hypothesis: Spermine may be an important epidermal antioxidant
    • Løvaas E. Hypothesis spermine may be an important epidermal antioxidant . Med. Hypothesis. 45:1995;59-67.
    • (1995) Med. Hypothesis , vol.45 , pp. 59-67
    • Løvaas, E.1
  • 28
    • 0033429672 scopus 로고    scopus 로고
    • Redox-regulation of intrinsic prion expression in multicellular prostate tumor spheroids
    • Sauer H., Dagdanova A., Hescheler J., Wartenberg M. Redox-regulation of intrinsic prion expression in multicellular prostate tumor spheroids. Free Radic. Biol. Med. 27:(11/12):1999;1276-1283.
    • (1999) Free Radic. Biol. Med. , vol.27 , Issue.11-12 , pp. 1276-1283
    • Sauer, H.1    Dagdanova, A.2    Hescheler, J.3    Wartenberg, M.4
  • 29
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • Bush A.I. Metals and neuroscience. Curr. Opin. Chem. Biol. 4:2000;184-191.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 31
    • 0032240291 scopus 로고    scopus 로고
    • Biochemistry of free radicals: From electron to tissue
    • Boveris A. Biochemistry of free radicals from electron to tissue . Medicine (Buenos Aires). 58:1998;350-356.
    • (1998) Medicine (Buenos Aires) , vol.58 , pp. 350-356
    • Boveris, A.1
  • 32
    • 0033963704 scopus 로고    scopus 로고
    • Oxidative stress and gene regulation
    • Allen R.G., Tresini M. Oxidative stress and gene regulation. Free Radic. Biol. Med. 28:(3):2000;463-499.
    • (2000) Free Radic. Biol. Med. , vol.28 , Issue.3 , pp. 463-499
    • Allen, R.G.1    Tresini, M.2
  • 33
    • 0034117954 scopus 로고    scopus 로고
    • Protein oxidation and degradation during proliferative senescence of human mrc-5 fibroblasts
    • Sitte N., Merker K., Zglinicki T., Grune T. Protein oxidation and degradation during proliferative senescence of human mrc-5 fibroblasts. Free Radic. Biol. Med. 28:(5):2000;701-708.
    • (2000) Free Radic. Biol. Med. , vol.28 , Issue.5 , pp. 701-708
    • Sitte, N.1    Merker, K.2    Zglinicki, T.3    Grune, T.4
  • 34
    • 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
  • 35
    • 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:(5):1995;2344-2351.
    • (1995) J. Biol. Chem. , vol.270 , Issue.5 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 36
    • 0343491668 scopus 로고    scopus 로고
    • Protein precipitation: A common etiology in neurodegenerative disorders?
    • Kakinusa A. Protein precipitation a common etiology in neurodegenerative disorders? TIG. 14:(10):1998;369-402.
    • (1998) TIG , vol.14 , Issue.10 , pp. 369-402
    • Kakinusa, A.1
  • 37
    • 0030007699 scopus 로고    scopus 로고
    • Impairment of DNA replication within one cell cycle after seeding of cells in the presence of polyamine-biosynthesis inhibitor
    • Fredlund J.K., Oredsson S.M. Impairment of DNA replication within one cell cycle after seeding of cells in the presence of polyamine-biosynthesis inhibitor. Eur. J. Biochem. 237:1996;539-544.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 539-544
    • Fredlund, J.K.1    Oredsson, S.M.2
  • 38
    • 0025873423 scopus 로고
    • Polyamines: From molecular biology to clinical applications
    • Jänne J., Alhonen L., Leinonen P. Polyamines from molecular biology to clinical applications . Ann. Med. 23:1991;241-259.
    • (1991) Ann. Med. , vol.23 , pp. 241-259
    • Jänne, J.1    Alhonen, L.2    Leinonen, P.3
  • 39
    • 0029131039 scopus 로고
    • Ornithine decarboxylase activity in vitro in response to acute hypoxia: A novel use to newborn rat brain slices
    • Packianathan S., Cain C.D., Liwnicz B.H., Longo L.D. Ornithine decarboxylase activity in vitro in response to acute hypoxia a novel use to newborn rat brain slices . Brain Res. 688:1995;61-71.
    • (1995) Brain Res. , vol.688 , pp. 61-71
    • Packianathan, S.1    Cain, C.D.2    Liwnicz, B.H.3    Longo, L.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.