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Volumn 28, Issue 1, 2000, Pages 129-140

Differential oxidation of apolipoprotein E isoforms and interaction with phospholipids

Author keywords

Alzheimer's disease; Apolipoprotein E; Free radicals; Myeloperoxidase; Oxidation; Phospholipids; Thrombin proteolysis

Indexed keywords

APOLIPOPROTEIN E; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; FREE RADICAL; ISOPROTEIN; MYELOPEROXIDASE; PHOSPHOLIPID; THROMBIN;

EID: 0033954735     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00232-4     Document Type: Article
Times cited : (72)

References (57)
  • 1
    • 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;1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 2
    • 0029266603 scopus 로고
    • Free radical mechanisms in dementia of Alzheimer type and the potential for antioxidative treatment
    • Frölich L., Riederer P. Free radical mechanisms in dementia of Alzheimer type and the potential for antioxidative treatment. Drug. Res. 45:1995;443-446.
    • (1995) Drug. Res. , vol.45 , pp. 443-446
    • Frölich, L.1    Riederer, P.2
  • 3
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease and oxidative stress. J. Biol. Chem. 272:1997;20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 5
    • 0028019080 scopus 로고
    • Role of protein oxidation in aging and in age-associated neurodegenerative diseases
    • Carney J.M., Carney A.M. Role of protein oxidation in aging and in age-associated neurodegenerative diseases. Life Sci. 55:1994;2097-2103.
    • (1994) Life Sci. , vol.55 , pp. 2097-2103
    • Carney, J.M.1    Carney, A.M.2
  • 6
    • 0024299370 scopus 로고
    • Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
    • Mahley R.W. Apolipoprotein E cholesterol transport protein with expanding role in cell biology . Science. 240:1988;622-630.
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 7
    • 0028172930 scopus 로고
    • Apolipoprotein E in animal models of brain injury and in Alzheimer's disease
    • Poirier J. Apolipoprotein E in animal models of brain injury and in Alzheimer's disease. Trends Neurosci. 12:1994;525-530.
    • (1994) Trends Neurosci. , vol.12 , pp. 525-530
    • Poirier, J.1
  • 9
    • 0028282762 scopus 로고
    • Frequency of the apolipoprotein E epsilon 2 allele is diminished in sporadic Alzheimer disease
    • West H.L., Rebeck G.W., Hyman B.T. Frequency of the apolipoprotein E epsilon 2 allele is diminished in sporadic Alzheimer disease. Neurosci. Lett. 175:1994;46-48.
    • (1994) Neurosci. Lett. , vol.175 , pp. 46-48
    • West, H.L.1    Rebeck, G.W.2    Hyman, B.T.3
  • 12
    • 0028303072 scopus 로고
    • Apolipoprotein E: Structure-function relationships
    • Weisgraber K.H. Apolipoprotein E structure-function relationships . Adv. Protein Chem. 45:1994;249-302.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 249-302
    • Weisgraber, K.H.1
  • 13
    • 0029119753 scopus 로고
    • Association of apolipoprotein E genotype with brain levels of apolipoprotein E and apolipoprotein J (clusterin) in Alzheimer disease
    • Bertrand P., Poirier J., Oda T., Finch C.E., Pasinetti G.M. Association of apolipoprotein E genotype with brain levels of apolipoprotein E and apolipoprotein J (clusterin) in Alzheimer disease. Mol. Brain Res. 33:1995;174-178.
    • (1995) Mol. Brain Res. , vol.33 , pp. 174-178
    • Bertrand, P.1    Poirier, J.2    Oda, T.3    Finch, C.E.4    Pasinetti, G.M.5
  • 14
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies K.J.A. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262:1987;9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 15
    • 0029151238 scopus 로고
    • Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease
    • Castano E.M., Prelli F., Pras M., Frangione B. Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease. J. Biol. Chem. 270:1995;17610-17615.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17610-17615
    • Castano, E.M.1    Prelli, F.2    Pras, M.3    Frangione, B.4
  • 16
    • 0029832616 scopus 로고    scopus 로고
    • A thrombin cleavage fragment of apolipoprotein E exhibits isoform-specific neurotoxicity
    • Marques M.A., Tolar M., Harmony J.A.K., Crutcher K.A. A thrombin cleavage fragment of apolipoprotein E exhibits isoform-specific neurotoxicity. Neuroreport. 7:1996;2529-2532.
    • (1996) Neuroreport , vol.7 , pp. 2529-2532
    • Marques, M.A.1    Tolar, M.2    Harmony, J.A.K.3    Crutcher, K.A.4
  • 19
    • 0029765553 scopus 로고    scopus 로고
    • Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and β-amyloid peptides
    • Miyata M., Smith J.D. Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and β-amyloid peptides. Nature Genet. 14:1996;55-61.
    • (1996) Nature Genet. , vol.14 , pp. 55-61
    • Miyata, M.1    Smith, J.D.2
  • 21
    • 0027933937 scopus 로고
    • Apolipoprotein oxidation in the absence of lipid peroxidation enhances LDL uptake by macrophage
    • Hunt J.V., Bailey J.R., Schultz D.L., McKay A.G., Michinson M.J. Apolipoprotein oxidation in the absence of lipid peroxidation enhances LDL uptake by macrophage. FEBS Lett. 349:1994;375-379.
    • (1994) FEBS Lett. , vol.349 , pp. 375-379
    • Hunt, J.V.1    Bailey, J.R.2    Schultz, D.L.3    McKay, A.G.4    Michinson, M.J.5
  • 22
    • 0028335529 scopus 로고
    • Effects of ebselen and probucol on oxidative modifications of lipid and protein of low density lipoprotein induced by free radicals
    • Noguchi N., Gotoh N., Niki E. Effects of ebselen and probucol on oxidative modifications of lipid and protein of low density lipoprotein induced by free radicals. Biochim. Biophys. Acta. 1213:1994;176-182.
    • (1994) Biochim. Biophys. Acta , vol.1213 , pp. 176-182
    • Noguchi, N.1    Gotoh, N.2    Niki, E.3
  • 26
    • 0024234923 scopus 로고
    • Action of myeloperoxidase-hydrogen peroxide-chloride system on the egg white lysozyme
    • Drozdz R., Naskalski J.W. Action of myeloperoxidase-hydrogen peroxide-chloride system on the egg white lysozyme. Acta Biochim. Pol. 35:1988;277-286.
    • (1988) Acta Biochim. Pol. , vol.35 , pp. 277-286
    • Drozdz, R.1    Naskalski, J.W.2
  • 27
    • 0030729868 scopus 로고    scopus 로고
    • Mechanisms of oxidative damage of low density lipoprotein in human atherosclerosis
    • Heineke J.W. Mechanisms of oxidative damage of low density lipoprotein in human atherosclerosis. Curr. Opin. Lipidol. 8:1997;268-274.
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 268-274
    • Heineke, J.W.1
  • 28
    • 0028379203 scopus 로고
    • Inflammation-associated amyloidogenesis. Lessons for Alzheimer's amyloidogenesis
    • Kisilevsky R. Inflammation-associated amyloidogenesis. Lessons for Alzheimer's amyloidogenesis. Mol. Neurobiol. 8:1993;65-66.
    • (1993) Mol. Neurobiol. , vol.8 , pp. 65-66
    • Kisilevsky, R.1
  • 29
    • 0029947089 scopus 로고    scopus 로고
    • Apolipoprotein E is highly susceptible to oxidation by myeloperoxidase, an enzyme present in the brain
    • Jolivalt C., Leininger Muller B., Drozdz R., Naskalski J.W., Siest G. Apolipoprotein E is highly susceptible to oxidation by myeloperoxidase, an enzyme present in the brain. Neurosci. Lett. 210:1996;61-64.
    • (1996) Neurosci. Lett. , vol.210 , pp. 61-64
    • Jolivalt, C.1    Leininger Muller, B.2    Drozdz, R.3    Naskalski, J.W.4    Siest, G.5
  • 30
    • 0023280054 scopus 로고
    • Lipoproteins and their receptors in the central nervous system. Characterization of the lipoproteins in cerebrospinal fluid and identification of apolipoprotein B, E (LDL) receptors in the brain
    • Pitas R.E., Boyles J.K., Lee S.H., Hui D., Weisgraber K.H. Lipoproteins and their receptors in the central nervous system. Characterization of the lipoproteins in cerebrospinal fluid and identification of apolipoprotein B, E (LDL) receptors in the brain. J. Biol. Chem. 262:1987;14352-14360.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14352-14360
    • Pitas, R.E.1    Boyles, J.K.2    Lee, S.H.3    Hui, D.4    Weisgraber, K.H.5
  • 33
    • 0025962686 scopus 로고
    • Large-scale isolation and purification of human apolipoproteins A-I and A-II
    • Sigalov A., Alexandrovitch O., Strizevskaya E. Large-scale isolation and purification of human apolipoproteins A-I and A-II. J. Chromatogr. 537:1991;464-468.
    • (1991) J. Chromatogr. , vol.537 , pp. 464-468
    • Sigalov, A.1    Alexandrovitch, O.2    Strizevskaya, E.3
  • 34
    • 0019125282 scopus 로고
    • Simple procedure of isolation of myeloperoxidase from leukocytes, pus and bone marrow cells
    • Naskalski J.W. Simple procedure of isolation of myeloperoxidase from leukocytes, pus and bone marrow cells. Acta Med. Pol. 21:1980;129-137.
    • (1980) Acta Med. Pol. , vol.21 , pp. 129-137
    • Naskalski, J.W.1
  • 37
    • 0021224520 scopus 로고
    • A review of plasma apolipoprotein A-I interaction with phosphatidylcholines
    • Jonas A. A review of plasma apolipoprotein A-I interaction with phosphatidylcholines. Exp. Lung Res. 6:1984;255-270.
    • (1984) Exp. Lung Res. , vol.6 , pp. 255-270
    • Jonas, A.1
  • 38
    • 0028352550 scopus 로고
    • Paradoxical enhancement of atherosclerosis by probucol treatment in apolipoprotein E-deficient mice
    • Zhuang Z., Huang X., Costa M. Paradoxical enhancement of atherosclerosis by probucol treatment in apolipoprotein E-deficient mice. Toxicol. Appl. Pharmacol. 126:1994;319-325.
    • (1994) Toxicol. Appl. Pharmacol. , vol.126 , pp. 319-325
    • Zhuang, Z.1    Huang, X.2    Costa, M.3
  • 39
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davies K.J.A., Delsignore M.E. Protein damage and degradation by oxygen radicals. J. Biol. Chem. 262:1987;9908-9913.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 41
    • 0022262772 scopus 로고
    • Activation of lecithin cholesterol acyltransferase by human apolipoprotein E in discoidal complexes with lipids
    • Zorich N., Jonas A., Pownall H.J. Activation of lecithin cholesterol acyltransferase by human apolipoprotein E in discoidal complexes with lipids. J. Biol. Chem. 260:1985;8831-8837.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8831-8837
    • Zorich, N.1    Jonas, A.2    Pownall, H.J.3
  • 43
    • 0027292790 scopus 로고
    • Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins
    • Heinecke J.W., Li W., Francis G.A., Golstein J.A. Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins. J. Clin. Invest. 91:1993;2866-2872.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2866-2872
    • Heinecke, J.W.1    Li, W.2    Francis, G.A.3    Golstein, J.A.4
  • 46
    • 0032513108 scopus 로고    scopus 로고
    • Oxidation of high density lipoproteins. II. Evidence for direct reduction of lipid hydroperoxides by methionine residues of apolipoproteins AI and AII
    • Garner B., Waldeck A.R., Witting P.K., Rye K.A., Stocker R. Oxidation of high density lipoproteins. II. Evidence for direct reduction of lipid hydroperoxides by methionine residues of apolipoproteins AI and AII. J. Biol. Chem. 273:1998;6088-6095.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6088-6095
    • Garner, B.1    Waldeck, A.R.2    Witting, P.K.3    Rye, K.A.4    Stocker, R.5
  • 49
    • 0027358327 scopus 로고
    • Inefficient degradation of oxidized regions of protein molecules
    • Grant A.J., Jessup W., Dean R.T. Inefficient degradation of oxidized regions of protein molecules. Free Radic. Res. Commun. 18:1993;259-267.
    • (1993) Free Radic. Res. Commun. , vol.18 , pp. 259-267
    • Grant, A.J.1    Jessup, W.2    Dean, R.T.3
  • 50
    • 0026502543 scopus 로고
    • Choline metabolism as a basis for selective vulnerability of cholinergique neurons
    • Wurtman R.J. Choline metabolism as a basis for selective vulnerability of cholinergique neurons. Trends Neurosci. 15:1992;117-122.
    • (1992) Trends Neurosci. , vol.15 , pp. 117-122
    • Wurtman, R.J.1
  • 51
    • 0027351531 scopus 로고
    • Regeneration in Alzheimer disease and aging
    • Terry R.D. Regeneration in Alzheimer disease and aging. Adv. Neurol. 59:1993;1-4.
    • (1993) Adv. Neurol. , vol.59 , pp. 1-4
    • Terry, R.D.1
  • 54
    • 0029894681 scopus 로고    scopus 로고
    • Oxidative damage and motor neurone disease difficulties in the measurement of protein carbonyls in human brain tissue
    • Lyras L., Evans P.J., Shaw P.J., Ince P.G., Halliwell B. Oxidative damage and motor neurone disease difficulties in the measurement of protein carbonyls in human brain tissue. Free Radic. Res. Commun. 24:1996;397-406.
    • (1996) Free Radic. Res. Commun. , vol.24 , pp. 397-406
    • Lyras, L.1    Evans, P.J.2    Shaw, P.J.3    Ince, P.G.4    Halliwell, B.5
  • 55
    • 0030805622 scopus 로고    scopus 로고
    • A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease
    • Alam Z.I., Daniel S.E., Lees A.J., Marsden D.C., Jenner P., Halliwell B. A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem. 69:1997;1326-1329.
    • (1997) J. Neurochem. , vol.69 , pp. 1326-1329
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Marsden, D.C.4    Jenner, P.5    Halliwell, B.6
  • 57
    • 0030759072 scopus 로고    scopus 로고
    • placebo-controlled, double-bind, randomized trial of an extract of Ginkgo biloba for dementia
    • Le Bars, P. L.; Katz, M. M.; Berman, N.; Itil, T. M.; Freedman, A. M.; Schatzberg, A. F. A placebo-controlled, double-bind, randomized trial of an extract of Ginkgo biloba for dementia. JAMA 278:1327-1332; 1997.
    • (1997) JAMA , vol.278 , pp. 1327-1332
    • Le Bars, P.L.1    Katz, M.M.2    Berman, N.3    Itil, T.M.4    Freedman, A.M.5    Schatzberg, A.F.A.6


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