메뉴 건너뛰기




Volumn 96, Issue 3, 1998, Pages 279-286

Mitochondrial dysfunction induced by oxidative stress in the brains of hamsters infected with the 263 K scrapie agent

Author keywords

Mitochondrial dysfunction; Neurodegeneration; Oxidative stress; Scrapie

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C OXIDASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL ENZYME;

EID: 0031710192     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004010050895     Document Type: Article
Times cited : (139)

References (31)
  • 1
    • 0028129137 scopus 로고
    • Evidence of an oxidative challenge in the Alzheimer's brain
    • Balazs L, Leon M (1994) Evidence of an oxidative challenge in the Alzheimer's brain. Neurochem Res 19: 1131-1137
    • (1994) Neurochem Res , vol.19 , pp. 1131-1137
    • Balazs, L.1    Leon, M.2
  • 2
    • 0023463279 scopus 로고
    • Aspects of the structure, function, and applications of superoxide dismutase
    • Bannister JV, Bannister WH, Rotilio G (1987) Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit Rev Biochem 22: 111-180
    • (1987) CRC Crit Rev Biochem , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 3
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal MF (1995) Aging, energy, and oxidative stress in neurodegenerative diseases. Ann Neurol 38: 357-366
    • (1995) Ann Neurol , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 4
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beer RF Jr, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133-140
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beer Jr., R.F.1    Sizer, I.W.2
  • 5
    • 0028145462 scopus 로고
    • Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes
    • Bolanos P, Peuchen S, Heales SJ, Land JM, Clark JB (1994) Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes. J Neurochem 63: 910-916
    • (1994) J Neurochem , vol.63 , pp. 910-916
    • Bolanos, P.1    Peuchen, S.2    Heales, S.J.3    Land, J.M.4    Clark, J.B.5
  • 6
    • 0030071721 scopus 로고    scopus 로고
    • Downregulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrate pathway
    • Troy CM, Derossi D, Prochiantz A, Greene LA, Shelanski ML (1996) Downregulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrate pathway. J Neurosci 16: 253-261
    • (1996) J Neurosci , vol.16 , pp. 253-261
    • Troy, C.M.1    Derossi, D.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5
  • 7
    • 0028238249 scopus 로고
    • The nature of the scrapie agent: Scrapie strain-host combinations
    • Carp RI, Ye X, Kascsak RJ, Rubenstein R (1994) The nature of the scrapie agent: scrapie strain-host combinations. Ann NY Acad Sci 724: 221-234
    • (1994) Ann NY Acad Sci , vol.724 , pp. 221-234
    • Carp, R.I.1    Ye, X.2    Kascsak, R.J.3    Rubenstein, R.4
  • 8
    • 0028922696 scopus 로고
    • Etiology and pathogenesis of prion diseases
    • DeArmond SJ, Prusiner SB (1995) Etiology and pathogenesis of prion diseases. Am J Pathol 146: 785-811
    • (1995) Am J Pathol , vol.146 , pp. 785-811
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 9
    • 0017643758 scopus 로고
    • Unconventional viruses and origin and disappearance of kuru
    • Gajdusek DC (1977) Unconventional viruses and origin and disappearance of kuru. Science 197: 943-960
    • (1977) Science , vol.197 , pp. 943-960
    • Gajdusek, D.C.1
  • 10
    • 0029012812 scopus 로고
    • Age- and peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system
    • Benzi G, Moretti A (1995) Age-and peroxidative stress-related modifications of the cerebral enzymatic activities linked to mitochondria and the glutathione system. Free Radic Biol Med 19: 77-101
    • (1995) Free Radic Biol Med , vol.19 , pp. 77-101
    • Benzi, G.1    Moretti, A.2
  • 11
    • 0021351203 scopus 로고
    • Oxygen toxicity, transition metals and disease
    • Halliwell B, Gutteridge JM (1984) Oxygen toxicity, transition metals and disease. Biochem J 219: 1-14
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 12
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B, Gutteridge JM (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol 186: 1-88
    • (1990) Methods Enzymol , vol.186 , pp. 1-88
    • Halliwell, B.1    Gutteridge, J.M.2
  • 13
    • 0000645311 scopus 로고
    • Methods for studying the genetics of mitochondria
    • Darley-Usmar VM, Rickwood D, Wilson MT (eds) IRL Press, Oxford
    • Hauswirth WW, Lim LOL, Dujon B, Turner G (1987) Methods for studying the genetics of mitochondria. In: Darley-Usmar VM, Rickwood D, Wilson MT (eds) Mitochondria: a practical approach. IRL Press, Oxford, pp 171-173
    • (1987) Mitochondria: A Practical Approach , pp. 171-173
    • Hauswirth, W.W.1    Lim, L.O.L.2    Dujon, B.3    Turner, G.4
  • 14
    • 0014664079 scopus 로고
    • On the tissue and subcellular distribution of multiple forms of catalase in the rat
    • Holmes RS, Masters CJ (1969) On the tissue and subcellular distribution of multiple forms of catalase in the rat. Biochim Biophys Acta 191: 488-490
    • (1969) Biochim Biophys Acta , vol.191 , pp. 488-490
    • Holmes, R.S.1    Masters, C.J.2
  • 15
    • 0004251221 scopus 로고
    • Methods of enzymatic analysis
    • Bergmeyer HU (ed) Academic Press, New York
    • Horn HD (1963) Methods of enzymatic analysis. In: Bergmeyer HU (ed) Glutathione reductase. Academic Press, New York, pp 875-879
    • (1963) Glutathione Reductase , pp. 875-879
    • Horn, H.D.1
  • 17
    • 0025073809 scopus 로고
    • Incubation periods and histopathological changes in mice injected stereotaxically in different brain areas with the 87V scrapie strain
    • Kim YS, Carp RI, Callahan SM, Wisniewski HM (1990) Incubation periods and histopathological changes in mice injected stereotaxically in different brain areas with the 87V scrapie strain. Acta Neuropathol 80: 388-392
    • (1990) Acta Neuropathol , vol.80 , pp. 388-392
    • Kim, Y.S.1    Carp, R.I.2    Callahan, S.M.3    Wisniewski, H.M.4
  • 18
    • 0017336439 scopus 로고
    • Characteristics of a short incubation model of scrapie in the golden hamster
    • Kimberlin RH, Walker CA (1977) Characteristics of a short incubation model of scrapie in the golden hamster. J Gen Virol 34: 295-304
    • (1977) J Gen Virol , vol.34 , pp. 295-304
    • Kimberlin, R.H.1    Walker, C.A.2
  • 19
    • 0030916006 scopus 로고    scopus 로고
    • Two pathways of nitric oxide production through glutamate receptors in the rat cerebellum in vivo
    • Yamada K, Nabeshima T (1997) Two pathways of nitric oxide production through glutamate receptors in the rat cerebellum in vivo. Neurosci Res 28: 93-102
    • (1997) Neurosci Res , vol.28 , pp. 93-102
    • Yamada, K.1    Nabeshima, T.2
  • 20
    • 0026688148 scopus 로고
    • Nitric oxide, a novel biologic messenger
    • Lowenstein CJ, Snyder SH (1992) Nitric oxide, a novel biologic messenger. Cell 70: 705-707
    • (1992) Cell , vol.70 , pp. 705-707
    • Lowenstein, C.J.1    Snyder, S.H.2
  • 21
    • 77957013023 scopus 로고
    • Micromethods tor the assay of enzymes
    • Lowry OH (1957) Micromethods tor the assay of enzymes. Methods Enzymol, pp 366-381
    • (1957) Methods Enzymol , pp. 366-381
    • Lowry, O.H.1
  • 22
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • Marletta MA (1993) Nitric oxide synthase structure and mechanism. J Biol Chem 26: 12231-12234
    • (1993) J Biol Chem , vol.26 , pp. 12231-12234
    • Marletta, M.A.1
  • 23
    • 0014691242 scopus 로고
    • Superoxide dismutase an enzymatic function for erythrocuprein
    • McCord J, Fridovich I (1969) Superoxide dismutase an enzymatic function for erythrocuprein. J Biol Chem 244: 6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.1    Fridovich, I.2
  • 24
    • 0029924622 scopus 로고    scopus 로고
    • In vivo expression of inducible nitric oxide synthase in cerebellar neurons
    • Minc-Golomb D, Yadid G, Tsarfaty I, Resau JH, Schwartz JP (1996) In vivo expression of inducible nitric oxide synthase in cerebellar neurons. J Neurochem 66: 1504-1509
    • (1996) J Neurochem , vol.66 , pp. 1504-1509
    • Minc-Golomb, D.1    Yadid, G.2    Tsarfaty, I.3    Resau, J.H.4    Schwartz, J.P.5
  • 25
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathology, and pharmacology
    • Moncada S, Palmer RM, Higgs EA (1991) Nitric oxide: physiology, pathology, and pharmacology. Pharmacol Rev 43: 109-142
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 26
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan C (1992) Nitric oxide as a secretory product of mammalian cells. FASEB J 6: 3051-3064
    • (1992) FASEB J , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 27
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95: 351-358
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 28
    • 0014108436 scopus 로고
    • Studies on the quantitative characterization of erythrocyte glutathione peroxidase
    • Paglia DE, Valentine WN (1967) Studies on the quantitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70: 158-169
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 29
    • 0017278865 scopus 로고
    • Studies on cytochrome c oxidase
    • Phan SM, Mahler HR (1976) Studies on cytochrome c oxidase. J Biol Chem 251: 257-269
    • (1976) J Biol Chem , vol.251 , pp. 257-269
    • Phan, S.M.1    Mahler, H.R.2
  • 30
    • 0028235036 scopus 로고
    • Amyloidosis in prion diseases and cells involved in PrP fibrinogenesis
    • Wisniewski HM, Wegiel J, Kozielski R (1994) Amyloidosis in prion diseases and cells involved in PrP fibrinogenesis. Ann NY Acad Sci 724: 191-209
    • (1994) Ann NY Acad Sci , vol.724 , pp. 191-209
    • Wisniewski, H.M.1    Wegiel, J.2    Kozielski, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.