메뉴 건너뛰기




Volumn 27, Issue 3, 1997, Pages 267-281

Oxidative modification of glutamine synthetase by amyloid beta peptide

Author keywords

Amyloid peptide; Glutamine synthetase; Inactivation; Protein carbonyls

Indexed keywords

AMYLOID BETA PROTEIN; CELL PROTEIN; FREE RADICAL; GLUTAMATE AMMONIA LIGASE; IRON; PEROXIDE;

EID: 0030657456     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.3109/10715769709065765     Document Type: Article
Times cited : (73)

References (48)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D. J. (1991). The molecular pathology of Alzheimer's disease. Neuron, 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0030064140 scopus 로고    scopus 로고
    • Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of Aβ42(43) and association of Aβ40 with cored plaques
    • Fukumoto, H., Asami-Odaka, A., Suzuki, N., Shimada, H., Ihara, Y., Iwatsubo, T. (1996). Amyloid β protein deposition in normal aging has the same characteristics as that in Alzheimer's disease. Predominance of Aβ42(43) and association of Aβ40 with cored plaques. American Journal of Pathology, 148, 259-265.
    • (1996) American Journal of Pathology , vol.148 , pp. 259-265
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Shimada, H.4    Ihara, Y.5    Iwatsubo, T.6
  • 7
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G., Cotman, C. W. (1993). Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. Journal of Neuroscience, 13, 1676-1687.
    • (1993) Journal of Neuroscience , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 9
  • 10
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons
    • Harris, M. E., Hensley, K., Butterfield, D. A., Leedle, R. A., Carney, J. M. (1995). Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons. Experimental Neurology, 131, 193-202.
    • (1995) Experimental Neurology , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 11
  • 13
    • 0028985210 scopus 로고
    • Amyloid β-peptide spin trapping 1: Peptide enzyme toxicity is related to free radical spin trap reactivity
    • Hensley, K., Aksenova, M., Carney, J. M., Harris, M., Butterfield, D. A. (1995). Amyloid β-peptide spin trapping 1: peptide enzyme toxicity is related to free radical spin trap reactivity. Neuroreport, 6, 489-492.
    • (1995) Neuroreport , vol.6 , pp. 489-492
    • Hensley, K.1    Aksenova, M.2    Carney, J.M.3    Harris, M.4    Butterfield, D.A.5
  • 14
    • 0028985209 scopus 로고
    • Amyloid β-peptide spin trapping II: Evidence for decomposition of the PBN spin adduct
    • Hensley, K., Aksenova, M., Carney, J. M., Harris, M., Butterfield, D. A. (1995). Amyloid β-peptide spin trapping II: evidence for decomposition of the PBN spin adduct. Neuroreport, 6, 489-492.
    • (1995) Neuroreport , vol.6 , pp. 489-492
    • Hensley, K.1    Aksenova, M.2    Carney, J.M.3    Harris, M.4    Butterfield, D.A.5
  • 15
    • 0029878108 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis
    • Mason, R. P., Estermyer, J. D., Kelly, J. F., Mason, P. E. (1996). Alzheimer's disease amyloid β peptide 25-35 is localized in the membrane hydrocarbon core: X-ray diffraction analysis. Biochemical and Biophysical Research Communications, 222, 78-82.
    • (1996) Biochemical and Biophysical Research Communications , vol.222 , pp. 78-82
    • Mason, R.P.1    Estermyer, J.D.2    Kelly, J.F.3    Mason, P.E.4
  • 16
    • 0028178837 scopus 로고
    • β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence specific fashion: Implications to Alzheimer's disease
    • Butterfield, D. A., Hensley, K., Harris, M., Mattson, M., Carney, J. M. (1994). β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence specific fashion: implications to Alzheimer's disease. Biochemical and Biophysical Research Communications, 200, 710-715.
    • (1994) Biochemical and Biophysical Research Communications , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.M.5
  • 17
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., Rydel, R. E. (1992). β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. Journal of Neuroscience, 12, 376-389.
    • (1992) Journal of Neuroscience , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 18
    • 0028981159 scopus 로고
    • Amyloid β-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Cahomeostasis and cell death
    • Mark, R., Hensley, K., Butterfield, D. A., Mattson, M. (1995). Amyloid β-peptide impairs ion-motive ATPase activities: evidence for a role in loss of neuronal Cahomeostasis and cell death. Journal of Neuroscience, 15, 6239-6249.
    • (1995) Journal of Neuroscience , vol.15 , pp. 6239-6249
    • Mark, R.1    Hensley, K.2    Butterfield, D.A.3    Mattson, M.4
  • 19
    • 0029889640 scopus 로고    scopus 로고
    • Amyloid β peptide (25-35) inhibits Na-dependent glutamate uptake in rat hippocampal astrocyte cultures
    • Harris, M. E., Wang, Y., Pedigo, N. W., Hensley, K., Butterfield, D. A., Carney, J. M. (1996). Amyloid β peptide (25-35) inhibits Na-dependent glutamate uptake in rat hippocampal astrocyte cultures, Journal of Neurochemistry, 67, 277-286.
    • (1996) Journal of Neurochemistry , vol.67 , pp. 277-286
    • Harris, M.E.1    Wang, Y.2    Pedigo, N.W.3    Hensley, K.4    Butterfield, D.A.5    Carney, J.M.6
  • 23
    • 0017579832 scopus 로고
    • Glutamine synthetase: Glial localization in brain
    • Martinez-Hernandez, A., Bell, K. P., Norenberg, M. D. (1976). Glutamine synthetase: glial localization in brain. Science, 195, 1356-1358.
    • (1976) Science , vol.195 , pp. 1356-1358
    • Martinez-Hernandez, A.1    Bell, K.P.2    Norenberg, M.D.3
  • 25
    • 0025309904 scopus 로고
    • Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbril brain
    • Oliver, C. N., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M., 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 gerbril brain. Proceedings of the National Academy of Science of the USA, 87, 5144-5147.
    • (1990) Proceedings of the National Academy of Science of the 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
  • 27
    • 0026622911 scopus 로고
    • Reaction of astrocytes in the gerbil hippocampus following transient ischemia: Immunohistochemical observations with antibodies against glial fibrillary acidic protein, glutamine synthetase, and S-100 protein
    • Tanaka, H., Araki, M., Masuzawa, T. (1992). Reaction of astrocytes in the gerbil hippocampus following transient ischemia: immunohistochemical observations with antibodies against glial fibrillary acidic protein, glutamine synthetase, and S-100 protein. Experimental Neurology, 116, 264-274.
    • (1992) Experimental Neurology , vol.116 , pp. 264-274
    • Tanaka, H.1    Araki, M.2    Masuzawa, T.3
  • 30
    • 0026597286 scopus 로고
    • Oxidative modification of Escherichia coli glutamine synthetase
    • Fisher, M. T. and Stadtman, E. R. (1992). Oxidative modification of Escherichia coli glutamine synthetase. Journal of Biological Chemistry, 267, 1872-1880.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 1872-1880
    • Fisher, M.T.1    Stadtman, E.R.2
  • 32
    • 0342319174 scopus 로고
    • Regulation of glutamine synthetase in cultured 3T3-L1 cells by insulin, hydrocortisone, and dibutyryl cyclic AMP
    • Miller, R. E., Hadenberg, R., Gersham, H. (1978). Regulation of glutamine synthetase in cultured 3T3-L1 cells by insulin, hydrocortisone, and dibutyryl cyclic AMP. Proceedings of the National Academy of Science of the USA, 75, 1418-1422.
    • (1978) Proceedings of the National Academy of Science of the USA , vol.75 , pp. 1418-1422
    • Miller, R.E.1    Hadenberg, R.2    Gersham, H.3
  • 34
    • 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.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 35
    • 0022764985 scopus 로고
    • Antibody probing on Western blots have been stained with India ink
    • Glenney, J. R. (1986). Antibody probing on Western blots have been stained with India ink. Analytical Biochemistry, 156, 315-318.
    • (1986) Analytical Biochemistry , vol.156 , pp. 315-318
    • Glenney, J.R.1
  • 36
    • 0030921729 scopus 로고    scopus 로고
    • Oxidatively-induced structural alterations of glutamine synthetase assessed by analysis of spin label incorporation kinetics: Relevance to Alzheimer's disease
    • Butterfield, D. A., Hensley, K., Cole, P., Aksenov, M., Aksenova, M., Bummer, P. M., Carney, J. M., Haley, B. E. (1997). Oxidatively-induced structural alterations of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer's disease. Journal of Neurochemistry, 68, 2451-2457.
    • (1997) Journal of Neurochemistry , vol.68 , pp. 2451-2457
    • Butterfield, D.A.1    Hensley, K.2    Cole, P.3    Aksenov, M.4    Aksenova, M.5    Bummer, P.M.6    Carney, J.M.7    Haley, B.E.8
  • 37
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of β-Amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation
    • Aksenov, M. Y., Aksenova, M. V., Butterfield, D. A., Hensley, K., Vigo-Pelfrey, C., Carney, J. M. (1996). Glutamine synthetase-induced enhancement of β-Amyloid peptide Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and Aβ fragmentation. Journal of Neurochemistry, 66, 2050-2056.
    • (1996) Journal of Neurochemistry , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 38
    • 0025305991 scopus 로고
    • Metal-catalyzed oxidation of Esclu'richia call glutamine synthetase: Correlation of structural and functional changes
    • Rivett, A. J. and Levine, R. L. (1990). Metal-catalyzed oxidation of Esclu'richia call glutamine synthetase: correlation of structural and functional changes. Archives of Biochemistry and Biophysics, 278, 26-34.
    • (1990) Archives of Biochemistry and Biophysics , vol.278 , pp. 26-34
    • Rivett, A.J.1    Levine, R.L.2
  • 40
    • 0028890715 scopus 로고
    • Protein hydroperoxides can give rise to reactive free radicals
    • Davies, M. J., Fu, S., Dean, R. T. (1995). Protein hydroperoxides can give rise to reactive free radicals. Biochemical Journal, 305, 643-649.
    • (1995) Biochemical Journal , vol.305 , pp. 643-649
    • Davies, M.J.1    Fu, S.2    Dean, R.T.3
  • 42
    • 0024514390 scopus 로고
    • Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivates by metal-catalyzed oxidation reactions
    • Amici, A., Levine, R. L., Tsai, L., Stadtman, E. R. (1989). Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivates by metal-catalyzed oxidation reactions. Journal of Biological Chemistry, 264, 3341-3346.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 3341-3346
    • Amici, A.1    Levine, R.L.2    Tsai, L.3    Stadtman, E.R.4
  • 44
    • 0029568017 scopus 로고
    • Purification and immunocharacterization of human brain glutamine synthetase and its detection in cerebrospinal fluid and serum by a sandwich enzyme immunoassay
    • Tumani, H., Shen, G. Q., Peter, J. B. (1995). Purification and immunocharacterization of human brain glutamine synthetase and its detection in cerebrospinal fluid and serum by a sandwich enzyme immunoassay. Journal of Immunological Methods, 188, 155-163.
    • (1995) Journal of Immunological Methods , vol.188 , pp. 155-163
    • Tumani, H.1    Shen, G.Q.2    Peter, J.B.3
  • 45
    • 0027080730 scopus 로고
    • Detection of glutamine synthetase in the cerebrospinal fluid of Alzheimer diseases patients: A potential diagnostic marker
    • Gunnersen, D. and Haley, B. (1992). Detection of glutamine synthetase in the cerebrospinal fluid of Alzheimer diseases patients: a potential diagnostic marker. Proceedings of the National Academy of Science of the USA, 89, 11949-11953.
    • (1992) Proceedings of the National Academy of Science of the USA , vol.89 , pp. 11949-11953
    • Gunnersen, D.1    Haley, B.2
  • 46
    • 0028064502 scopus 로고
    • Involvement of free oxygen radicals in β-amyloidosis: An hypothesis
    • Friedlich, A. and Butcher, L. (1994). Involvement of free oxygen radicals in β-amyloidosis: an hypothesis. Neurobiology of Aging, 15, 443-455.
    • (1994) Neurobiology of Aging , vol.15 , pp. 443-455
    • Friedlich, A.1    Butcher, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.