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Volumn 84, Issue 6, 2003, Pages 1442-1451

Apolipoprotein E enhances uptake of soluble but not aggregated amyloid-β protein into synaptic terminals

Author keywords

Alzheimer's disease; Amyloid; Apolipoprotein E; Flow cytometry; Lipoprotein receptor related protein; Synaptosomes

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; APOLIPOPROTEIN E; DODECYL SULFATE SODIUM; HEPARIN LYASE; LIPOPROTEIN RECEPTOR RELATED PROTEIN; RECEPTOR ASSOCIATED PROTEIN; RECEPTOR PROTEIN; TRYPSIN; UNCLASSIFIED DRUG;

EID: 0037343967     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01643.x     Document Type: Article
Times cited : (72)

References (52)
  • 2
    • 0031882562 scopus 로고    scopus 로고
    • β-amyloid peptides increase the binding and internalization of apolipoprotein E to hippocampal neurons
    • Beffert U., Aumont N., Dea D., Lussier-Cacan S., Davignon J. and Poirer J. (1998) β-Amyloid peptides increase the binding and internalization of apolipoprotein E to hippocampal neurons. J. Neurochem. 70, 1458-1466.
    • (1998) J. Neurochem. , vol.70 , pp. 1458-1466
    • Beffert, U.1    Aumont, N.2    Dea, D.3    Lussier-Cacan, S.4    Davignon, J.5    Poirer, J.6
  • 4
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide Aβ1-42, in differentiated PC 12 cells
    • Burdick D., Kosmoski J., Knauer M. F. and Glabe C. G. (1997) Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide Aβ1-42, in differentiated PC 12 cells. Brain Res. 746, 275-284.
    • (1997) Brain Res. , vol.746 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 5
    • 0029905421 scopus 로고    scopus 로고
    • Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ
    • Chan W., Fornwald J., Brawner M. and Wetzel R. (1996) Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ. Biochemistry 35, 7123-7130.
    • (1996) Biochemistry , vol.35 , pp. 7123-7130
    • Chan, W.1    Fornwald, J.2    Brawner, M.3    Wetzel, R.4
  • 9
    • 0022531676 scopus 로고
    • A rapid method for isolation of synaptosomes on percoll gradients
    • Dunkley P. R., Jarvie P. E., Heath J. W., Kidd G. J. and Rostas J. A. (1986) A rapid method for isolation of synaptosomes on percoll gradients. Brain Res. 372, 115-129.
    • (1986) Brain Res. , vol.372 , pp. 115-129
    • Dunkley, P.R.1    Jarvie, P.E.2    Heath, J.W.3    Kidd, G.J.4    Rostas, J.A.5
  • 11
    • 0031693494 scopus 로고    scopus 로고
    • Receptors of the low density lipoprotein (LDL) receptor family in Man. Multiple functions of the large family members via interaction with complex ligands
    • Gliemann J. (1998) Receptors of the low density lipoprotein (LDL) receptor family in Man. Multiple functions of the large family members via interaction with complex ligands. Biol. Chem. 379, 951-964.
    • (1998) Biol. Chem. , vol.379 , pp. 951-964
    • Gliemann, J.1
  • 12
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein E and Alzheimer's amyloid-b peptide is dependent on b-peptide conformation
    • Golabek A. A., Soto C., Vogel T. and Wisniewski T. (1996) The interaction between apolipoprotein E and Alzheimer's amyloid-b peptide is dependent on b-peptide conformation. J. Biol. Chem. 271, 10602-10606.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4
  • 13
    • 0034661731 scopus 로고    scopus 로고
    • Quantitative characterization of crude synaptosomal fraction (P-2) components by flow cytometry
    • Gylys K. H., Fein J. A. and Cole G. M. (2000) Quantitative characterization of crude synaptosomal fraction (P-2) components by flow cytometry. J. Neurosci. Res. 61, 186-192.
    • (2000) J. Neurosci. Res. , vol.61 , pp. 186-192
    • Gylys, K.H.1    Fein, J.A.2    Cole, G.M.3
  • 14
    • 0036591530 scopus 로고    scopus 로고
    • Caspase inhibition protects nerve terminals from in vitro degradation
    • Gylys K. H., Fein J. A. and Cole G. M. (2002) Caspase inhibition protects nerve terminals from in vitro degradation. Neurochem. Res. 27, 465-472.
    • (2002) Neurochem. Res. , vol.27 , pp. 465-472
    • Gylys, K.H.1    Fein, J.A.2    Cole, G.M.3
  • 15
    • 0025786502 scopus 로고
    • 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
    • Herz J., Goldstein J. L., Strickland D. K., Ho Y. K. and Brown M. S. (1991) 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. J. Biol. Chem. 266, 21232-21238.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21232-21238
    • Herz, J.1    Goldstein, J.L.2    Strickland, D.K.3    Ho, Y.K.4    Brown, M.S.5
  • 18
    • 0031452443 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans participate in hepatic lipase- and apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins
    • Ji Z. S., Dichek H. L., Miranda R. D. and Mahley R. W. (1997) Heparan sulfate proteoglycans participate in hepatic lipase- and apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins. J. Biol. Chem. 272, 31285-31292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31285-31292
    • Ji, Z.S.1    Dichek, H.L.2    Miranda, R.D.3    Mahley, R.W.4
  • 19
    • 0032577695 scopus 로고    scopus 로고
    • Differential cellular accumulation/retention of apolipoprotein E mediated by cell surface heparan sulfate proteoglycans
    • Ji Z. S., Pitas R. E. and Mahley R. W. (1998) Differential cellular accumulation/retention of apolipoprotein E mediated by cell surface heparan sulfate proteoglycans. J. Biol. Chem. 273, 13452-13460.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13452-13460
    • Ji, Z.S.1    Pitas, R.E.2    Mahley, R.W.3
  • 20
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein W. L., Krafft G. A. and Finch C. E. (2001) Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24, 219-224.
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 21
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein
    • Knauer M. F., Soreghan B., Burdick D., Kosmoski J. and Glabe C. G. (1992) Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein. Proc. Natl Acad. Sci. USA 89, 7437-7441.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 23
    • 0030748833 scopus 로고    scopus 로고
    • Association of human, rat, and rabbit apolipoprotein E with β-amyloid
    • LaDu M. J., Lukens J., Reardon C. A. and Getz G. S. (1997) Association of human, rat, and rabbit apolipoprotein E with β-amyloid. J. Neurosci. Res. 49, 9-18.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 9-18
    • LaDu, M.J.1    Lukens, J.2    Reardon, C.A.3    Getz, G.S.4
  • 25
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A. and Yankner B. A. (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl Acad. Sci. USA 91, 12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 27
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-chymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J., Yee A., Brewer H. B. Jr, Das S. and Potter H. (1994) Amyloid-associated proteins alpha 1-chymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372, 92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer H.B., Jr.3    Das, S.4    Potter, H.5
  • 29
    • 0027727915 scopus 로고
    • Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: Differences revealed using aminooxyacetate
    • McKenna M. C., Tildon J. T., Stevenson J. H., Boatright R. and Huang S. (1993) Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: differences revealed using aminooxyacetate. Dev. Neurosci. 15, 320-329.
    • (1993) Dev. Neurosci. , vol.15 , pp. 320-329
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Boatright, R.4    Huang, S.5
  • 31
    • 0035884905 scopus 로고    scopus 로고
    • A novel action of Alzheimer's amyloid β-protein (Aβ): Oligomeric Aβ promotes lipid release
    • Michikawa M., Gong J. S., Fan Q. W., Sawamura N. and Yanagisawa K. (2001) A novel action of Alzheimer's amyloid β-protein (Aβ): oligomeric Aβ promotes lipid release. J. Neurosci. 21, 7226-7235.
    • (2001) J. Neurosci. , vol.21 , pp. 7226-7235
    • Michikawa, M.1    Gong, J.S.2    Fan, Q.W.3    Sawamura, N.4    Yanagisawa, K.5
  • 33
    • 0021219280 scopus 로고
    • Rapid preparation of synaptosomes from mammalian brain using nontoxic isoosmotic gradient material (Percoll)
    • Nagy A. and Delgado-Escueta A. V. (1984) Rapid preparation of synaptosomes from mammalian brain using nontoxic isoosmotic gradient material (Percoll). J. Neurochem. 43, 1114-1123.
    • (1984) J. Neurochem. , vol.43 , pp. 1114-1123
    • Nagy, A.1    Delgado-Escueta, A.V.2
  • 34
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid b-protein via a scavenger receptor
    • Paresce D. M., Ghosh R. N. and Maxfield F. R. (1996) Microglial cells internalize aggregates of the Alzheimer's disease amyloid b-protein via a scavenger receptor. Neuron 17, 553-565.
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 35
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures
    • Pike C. J., Walencewica A. J., Glabe C. G. and Cotman C. W. (1991a) Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207, 367-368.
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewica, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 36
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike C. J., Walencewica A. J., Glabe C. G. and Cotman C. W. (1991b) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563, 311-314.
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewica, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 37
    • 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. and Cotman C. W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 38
    • 0028894661 scopus 로고
    • Multiple, diverse senile plaque-associated proteins are ligands of an apolipoprotein E receptor, the α2-macroglobulin receptor/low-density-lipoprotein receptor-related protein
    • Rebeck G. W., Harr S. D., Strickland D. K. and Hyman B. T. (1995) Multiple, diverse senile plaque-associated proteins are ligands of an apolipoprotein E receptor, the α2-macroglobulin receptor/low-density-lipoprotein receptor-related protein. Ann. Neurol. 37, 211-217.
    • (1995) Ann. Neurol. , vol.37 , pp. 211-217
    • Rebeck, G.W.1    Harr, S.D.2    Strickland, D.K.3    Hyman, B.T.4
  • 39
    • 0027332081 scopus 로고
    • Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher A. E., Lowenson J. D., Clarke S., Woods A. S., Cotter R. J., Gowing E. and Ball M. J. (1993) Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl Acad. Sci. USA 90, 10836-10840.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 41
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D. et al. (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2, 864-870.
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 42
    • 0026061995 scopus 로고
    • A gentle fixation and permeabilization method for combined cell surface and intra-cellular staining with improved precision in DNA quantitation
    • Schmid I., Uttenbogaart C. H. and Giorgi J. V. (1991) A gentle fixation and permeabilization method for combined cell surface and intra-cellular staining with improved precision in DNA quantitation. Cytometry 12, 279-285.
    • (1991) Cytometry , vol.12 , pp. 279-285
    • Schmid, I.1    Uttenbogaart, C.H.2    Giorgi, J.V.3
  • 43
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D. J. (1999) Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399, A23-A31.
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 46
    • 0002080057 scopus 로고    scopus 로고
    • The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations
    • Terry R. D. et al., eds, Lippincott Williams & Wilkins, Philadelphia
    • Terry R. D. (1999) The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations, in Alzheimer Disease (Terry R. D. et al., eds), pp. 187-206, Lippincott Williams & Wilkins, Philadelphia.
    • (1999) Alzheimer Disease , pp. 187-206
    • Terry, R.D.1
  • 47
    • 0000731820 scopus 로고
    • Choline uptake and acetylcholine synthesis in synaptosomes: Investigations using two different labeled variants of choline
    • Weiler M. H., Gundersen C. B. and Jenden D. J. (1981) Choline uptake and acetylcholine synthesis in synaptosomes: investigations using two different labeled variants of choline. J. Neurochem. 31, 789-796.
    • (1981) J. Neurochem. , vol.31 , pp. 789-796
    • Weiler, M.H.1    Gundersen, C.B.2    Jenden, D.J.3
  • 49
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castano E. M., Golabek A., Vogel T. and Frangione B. (1994) Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am. J. Pathol. 145, 1030-1035.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 50
    • 0024578637 scopus 로고
    • Flow cytometric analysis of rat striatal nerve terminals
    • Wolf M. E. and Kapatos G. (1989) Flow cytometric analysis of rat striatal nerve terminals. J. Neurosc. 9, 94-105.
    • (1989) J. Neurosc. , vol.9 , pp. 94-105
    • Wolf, M.E.1    Kapatos, G.2
  • 51
    • 0032903412 scopus 로고    scopus 로고
    • Apolipoprotein E promotes the binding and uptake of β-amyloid into Chinese hamster ovary cells in an isoform-specific manner
    • Yang A. J., Small D. H., Seydel U., Smith J. D., Hallmayer J., Gandy S. E. and Martins R. N. (1999) Apolipoprotein E promotes the binding and uptake of β-amyloid into Chinese hamster ovary cells in an isoform-specific manner. Neuroscience 90, 1217-1226.
    • (1999) Neuroscience , vol.90 , pp. 1217-1226
    • Yang, A.J.1    Small, D.H.2    Seydel, U.3    Smith, J.D.4    Hallmayer, J.5    Gandy, S.E.6    Martins, R.N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.