메뉴 건너뛰기




Volumn 71, Issue 5, 1998, Pages 2041-2048

Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis

Author keywords

Carbonyl content; Dinitrophenylhydrazine; Familial amyotrophic lateral sclerosis; Protein oxidation; Transgenic mouse; Western immunoblot

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL EXPERIMENT; ARTICLE; IMMUNOBLOTTING; LIPID PEROXIDATION; MOUSE; NONHUMAN; OXIDATIVE STRESS; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; SPINAL CORD MOTONEURON; TRANSGENIC MOUSE;

EID: 0031784348     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71052041.x     Document Type: Article
Times cited : (242)

References (40)
  • 1
    • 0030632815 scopus 로고    scopus 로고
    • Conenzyme Q10 in the central nervous system and its potential usefulness in the treatment of neurodegenerative diseases
    • Beal M. F. and Mathews R. T. (1997) Conenzyme Q10 in the central nervous system and its potential usefulness in the treatment of neurodegenerative diseases. Mol. Aspects Med. 18 (Suppl.), 169-179.
    • (1997) Mol. Aspects Med. , vol.18 , Issue.SUPPL. , pp. 169-179
    • Beal, M.F.1    Mathews, R.T.2
  • 2
    • 0029682870 scopus 로고    scopus 로고
    • Oxidative damage and tyrosine nitration from peroxynitrite
    • Beckman J. S. (1996) Oxidative damage and tyrosine nitration from peroxynitrite. Chem. Res. Toxicol. 9, 836-844.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 836-844
    • Beckman, J.S.1
  • 3
    • 0028885558 scopus 로고
    • Diquat-dependent protein carbonyl formation: Identification of lipid-dependent and lipid-independent pathways
    • Blakeman D. P., Ryan T. P., Jolly R. A., and Petry T. W. (1995) Diquat-dependent protein carbonyl formation: identification of lipid-dependent and lipid-independent pathways. Biochem. Pharmacol. 50, 929-935.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 929-935
    • Blakeman, D.P.1    Ryan, T.P.2    Jolly, R.A.3    Petry, T.W.4
  • 4
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A. C., Schulz J. B., Brown R. H. Jr., and Beal M. F. (1993) Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61, 2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown Jr., R.H.3    Beal, M.F.4
  • 5
    • 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-α-phenylnitrone
    • Carney J. M., Starke-Reed P. E., Oliver C. N., Landum R. W., Cheng M. S., Wu J. F., and Floyd R. A. (1991) 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-α-phenylnitrone. Proc. Natl. Acad. Sci. USA 88, 3633-3636.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3633-3636
    • Carney, J.M.1    Starke-Reed, P.E.2    Oliver, C.N.3    Landum, R.W.4    Cheng, M.S.5    Wu, J.F.6    Floyd, R.A.7
  • 7
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J. P., Sampson J. B., Zhuang Y., Thompson J. A., and Beckman J. S. (1997) Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69, 1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 8
    • 0019268092 scopus 로고
    • The free radical pathology and the microcirculation in the major central nervous system disorders
    • Demopoulos H. B., Flamm E. S., Pietronigro D. D., and Seligman M. L. (1980) The free radical pathology and the microcirculation in the major central nervous system disorders. Acta Physiol. Scand. Suppl. 492, 91-119.
    • (1980) Acta Physiol. Scand. Suppl. , vol.492 , pp. 91-119
    • Demopoulos, H.B.1    Flamm, E.S.2    Pietronigro, D.D.3    Seligman, M.L.4
  • 9
    • 0024468045 scopus 로고
    • Methods of determination of aldehydic lipid peroxidation products
    • Esterbauer H. and Zollner H. (1989) Methods of determination of aldehydic lipid peroxidation products. Free Radic. Biol. Med. 7, 197-203.
    • (1989) Free Radic. Biol. Med. , vol.7 , pp. 197-203
    • Esterbauer, H.1    Zollner, H.2
  • 10
    • 0025778702 scopus 로고
    • Age influence on oxidative events during brain ischemia/reperfusion
    • Floyd R. A. and Carney J. M. (1991) Age influence on oxidative events during brain ischemia/reperfusion. Arch. Gerontol. Geriatr. 12, 155-177.
    • (1991) Arch. Gerontol. Geriatr. , vol.12 , pp. 155-177
    • Floyd, R.A.1    Carney, J.M.2
  • 12
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E. riluzole and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney M. E., Cutting F. B., Zhai P., Doble A., Taylor C. P., Andrus P. D., and Hall E. D. (1996) Benefit of vitamin E. riluzole and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol. 39, 147-157.
    • (1996) Ann. Neurol. , vol.39 , pp. 147-157
    • Gurney, M.E.1    Cutting, F.B.2    Zhai, P.3    Doble, A.4    Taylor, C.P.5    Andrus, P.D.6    Hall, E.D.7
  • 13
    • 0345513784 scopus 로고    scopus 로고
    • Mutant Cu/Zn SOD gene in motor neuron disease
    • Gurney M. E., Liu R., Althaus J. S., and Hall E. D. (1998) Mutant Cu/Zn SOD gene in motor neuron disease. Age 21, 41-45.
    • (1998) Age , vol.21 , pp. 41-45
    • Gurney, M.E.1    Liu, R.2    Althaus, J.S.3    Hall, E.D.4
  • 14
    • 0032127330 scopus 로고    scopus 로고
    • Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS
    • Hall E. D., Andrus P. K., Oostveen J. A., Fleck T. J., and Gurney M. E. (1998) Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS. J. Neurosci. Res. 53, 66-77.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 66-77
    • Hall, E.D.1    Andrus, P.K.2    Oostveen, J.A.3    Fleck, T.J.4    Gurney, M.E.5
  • 15
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triagers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong J. and Xu Z. (1998) Massive mitochondrial degeneration in motor neurons triagers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci. 18, 3241-3250.
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0021100174 scopus 로고
    • Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of histidine residue
    • Levine R. L. (1983) Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of histidine residue. J. Biol. Chem. 258, 11823-11827.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11823-11827
    • Levine, R.L.1
  • 18
    • 0019555585 scopus 로고
    • Turnover of bacterial glutamine synthetase: Oxidative inactivation precedes proteolysis
    • Levine R. L., Oliver C. N., Fulks R. M., and Stadtman E. R. (1981) Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis. Proc. Natl. Acad. Sci. USA 78, 2120-2124.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2120-2124
    • Levine, R.L.1    Oliver, C.N.2    Fulks, R.M.3    Stadtman, E.R.4
  • 20
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R. L., Williams J. A., Stadtman E. R., and Shacter L. (1994) Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233, 346-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, L.4
  • 21
    • 0029894681 scopus 로고    scopus 로고
    • Oxidative damage and motor neuron disease: Difficulties in the measurement of protein carbonyl in human tissues
    • Lyras L., Evans P. J., Shaw P. J., Nice P. G., and Halliwell B. (1996) Oxidative damage and motor neuron disease: difficulties in the measurement of protein carbonyl in human tissues. Free Radic. Res. 24, 397-406.
    • (1996) Free Radic. Res. , vol.24 , pp. 397-406
    • Lyras, L.1    Evans, P.J.2    Shaw, P.J.3    Nice, P.G.4    Halliwell, B.5
  • 22
    • 0022532466 scopus 로고
    • Regional distributions of thiobarbituric acid-reactive products, activities of enzymes regulating the metabolism of oxygen free radicals, and some of the related enzymes of adult and age rat brains
    • Mizuno Y. and Ohta K. (1986) Regional distributions of thiobarbituric acid-reactive products, activities of enzymes regulating the metabolism of oxygen free radicals, and some of the related enzymes of adult and age rat brains. J. Neurochem. 46, 1344-1352.
    • (1986) J. Neurochem. , vol.46 , pp. 1344-1352
    • Mizuno, Y.1    Ohta, K.2
  • 23
    • 0022443737 scopus 로고
    • Familial adult motor neuron disease: Amyotrophic lateral sclerosis
    • Mulder D. W., Kurland L. T., Offord K. P., and Beard C. M. (1986) Familial adult motor neuron disease: amyotrophic lateral sclerosis. Neurology 36, 511-517.
    • (1986) Neurology , vol.36 , pp. 511-517
    • Mulder, D.W.1    Kurland, L.T.2    Offord, K.P.3    Beard, C.M.4
  • 24
    • 0025309904 scopus 로고
    • Oxidative damage to brain proteins, loss of glutamine synthetase activity and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain
    • Oliver C. N., Starke-Reed P. E., Stadtman E. R., Liu G. J., Carney J. M., and Floyd R. A. (1990) Oxidative damage to brain proteins, loss of glutamine synthetase activity and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain. Proc. Natl. Acad. Sci. USA 87, 5144-5147.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5144-5147
    • Oliver, C.N.1    Starke-Reed, P.E.2    Stadtman, E.R.3    Liu, G.J.4    Carney, J.M.5    Floyd, R.A.6
  • 25
    • 0027487229 scopus 로고
    • AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition Ad Hoc Writing Committee on the reformulation of the AIN-76A rodent diet
    • Reeves E. D., Nielsen F. H., and Fahey G. C. Jr. (1993) AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition Ad Hoc Writing Committee on the reformulation of the AIN-76A rodent diet. J. Nutr. 123, 1939-1951.
    • (1993) J. Nutr. , vol.123 , pp. 1939-1951
    • Reeves, E.D.1    Nielsen, F.H.2    Fahey Jr., G.C.3
  • 26
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase provide an animal model of amyotrophic lateral sclerosis
    • Ripps M. E., Huntley G. W., Hof P. R., Morrison J. H., and Gordon J. W. (1995) Transgenic mice expressing an altered murine superoxide dismutase provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 92, 689-693.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 27
    • 0028864842 scopus 로고
    • Changes in the histidine residues ot Cu/Zn superoxide dismutase during aging
    • Santa Maria C., Revilla E., Ayala A., de la Cruz C. P., and Machado A. (1995) Changes in the histidine residues ot Cu/Zn superoxide dismutase during aging. FEBS Lett. 34, 85-88.
    • (1995) FEBS Lett. , vol.34 , pp. 85-88
    • Santa Maria, C.1    Revilla, E.2    Ayala, A.3    De La Cruz, C.P.4    Machado, A.5
  • 28
    • 0029082389 scopus 로고
    • Oxidative damage to protein in sporadic motor neuron disease spinal cord
    • Shaw P. J., Ince P. G., Falkous G., and Mantle D. (1995) Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann. Neurol. 38, 691-695.
    • (1995) Ann. Neurol. , vol.38 , pp. 691-695
    • Shaw, P.J.1    Ince, P.G.2    Falkous, G.3    Mantle, D.4
  • 30
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman E. R. (1992) Protein oxidation and aging. Science 257, 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 31
    • 0344651501 scopus 로고    scopus 로고
    • Forum on free radical mechanisms of neurotoxicity: Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E. R. and Berlett B. S. (1997) Forum on free radical mechanisms of neurotoxicity: reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10, 483-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 483-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 33
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenol to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction
    • Uchida K. and Stadtman E. R. (1993) Covalent attachment of 4-hydroxynonenol to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction. J. Biol. Chem. 268, 6388-6393.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 34
    • 0021255413 scopus 로고
    • Effect of age on vitamin E concentrations in various brain regions of the brain and a few selected peripheral tissues of the rat, and on the uptake of radioactive vitamin E by various regions of rat brain
    • Vatassery G. T., Angerhofer C. K., and Knox C. A. (1984) Effect of age on vitamin E concentrations in various brain regions of the brain and a few selected peripheral tissues of the rat, and on the uptake of radioactive vitamin E by various regions of rat brain. J. Neurochem. 43, 409-412.
    • (1984) J. Neurochem. , vol.43 , pp. 409-412
    • Vatassery, G.T.1    Angerhofer, C.K.2    Knox, C.A.3
  • 36
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P. C., Pardo C. A., Borchelt D. R., Lee M. K., Copeland N. G., Jenkins N. A., Sisodia S. S., Cleveland D. W., and Price D. L. (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 39
    • 0027489345 scopus 로고
    • Age-related changes in hydroxyl radical stress and antioxidants in gerbil brain
    • Zhang J.-R., Andrus P. K., and Hall E. D. (1993) Age-related changes in hydroxyl radical stress and antioxidants in gerbil brain. J. Neurochem. 61, 1640-1647.
    • (1993) J. Neurochem. , vol.61 , pp. 1640-1647
    • Zhang, J.-R.1    Andrus, P.K.2    Hall, E.D.3
  • 40
    • 0024350070 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase specific activity in tissues of rats of different age and comparison with other glutathione peroxidases
    • Zhang L., Maiorino M., Roveri A., and Ursini F. (1989) Phospholipid hydroperoxide glutathione peroxidase specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim. Biophys. Acta 1006, 140-143.
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 140-143
    • Zhang, L.1    Maiorino, M.2    Roveri, A.3    Ursini, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.