메뉴 건너뛰기




Volumn 46, Issue 1, 1996, Pages 58-66

Relative efficacies of amyloid β peptide (Aβ) binding proteins in Aβ aggregation

Author keywords

1 antichymotrypsin; Alzheimer's disease; apolipoprotein E; C1q; serum amyloid P

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; AMYLOID BETA PROTEIN; AMYLOID P COMPONENT; APOLIPOPROTEIN E; BINDING PROTEIN; COMPLEMENT COMPONENT C1Q; PREALBUMIN;

EID: 0029758030     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(19961001)46:1<58::AID-JNR8>3.0.CO;2-E     Document Type: Article
Times cited : (65)

References (79)
  • 1
    • 0023838532 scopus 로고
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52: 487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 5
    • 0027158642 scopus 로고
    • Association cortex, cerebellum, and serum concentrations of C1q and factor B in Alzheimer's disease
    • Brachova L, Lue L-F, Schultz J, El Rashidy T, Rogers J (1993): Association cortex, cerebellum, and serum concentrations of C1q and factor B in Alzheimer's disease. Mol Brain Res 18: 329-334.
    • (1993) Mol Brain Res , vol.18 , pp. 329-334
    • Brachova, L.1    Lue, L.-F.2    Schultz, J.3    El Rashidy, T.4    Rogers, J.5
  • 7
    • 0028588694 scopus 로고
    • Congo Red protects against toxicity of β-amyloid peptides on rat hippocampal neurones
    • Burgevin MC, Passat M, Daniel N, Doble A (1994): Congo Red protects against toxicity of β-amyloid peptides on rat hippocampal neurones. NeuroReport 5:2429-2432.
    • (1994) NeuroReport , vol.5 , pp. 2429-2432
    • Burgevin, M.C.1    Passat, M.2    Daniel, N.3    Doble, A.4
  • 9
    • 0023899417 scopus 로고
    • Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis
    • Coria F, Castano E, Prelli F, Larrondo-Lillo M, Van Duinen S, Shelanski ML, Frangione B (1988): Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab Invest 58:454-458.
    • (1988) Lab Invest , vol.58 , pp. 454-458
    • Coria, F.1    Castano, E.2    Prelli, F.3    Larrondo-Lillo, M.4    Van Duinen, S.5    Shelanski, M.L.6    Frangione, B.7
  • 10
    • 0025951302 scopus 로고
    • Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes
    • Diedrich JF, Minnigan H, Carp RI, Whitaker JN, Race R, Frey W II, Haase AT (1991): Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes. J Virol 65: 4759-4768.
    • (1991) J Virol , vol.65 , pp. 4759-4768
    • Diedrich, J.F.1    Minnigan, H.2    Carp, R.I.3    Whitaker, J.N.4    Race, R.5    Frey II, W.6    Haase, A.T.7
  • 11
    • 0024340461 scopus 로고
    • Immunodetection of the amyloid P component in Alzheimer's disease
    • Duong T, Pommier EC, Scheibel AB (1989): Immunodetection of the amyloid P component in Alzheimer's disease. Acta Neuropathol 78:429-437.
    • (1989) Acta Neuropathol , vol.78 , pp. 429-437
    • Duong, T.1    Pommier, E.C.2    Scheibel, A.B.3
  • 14
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • Evans KC, Berger EP, Cho C-G, Weisgraber KH, Lansbury PT (1995): Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci USA 92:763-767.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.-G.3    Weisgraber, K.H.4    Lansbury, P.T.5
  • 16
    • 0027186334 scopus 로고
    • The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
    • Ghiso J, Matsubara E, Koudinov A, Choi-Miura NH, Tomita M, Wisniewski T, Frangione B (1993): The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. Biochem J 293:27-30.
    • (1993) Biochem J , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Choi-Miura, N.H.4    Tomita, M.5    Wisniewski, T.6    Frangione, B.7
  • 17
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis: The beta-fibrilloses
    • Glenner GG (1980): Amyloid deposits and amyloidosis: The beta-fibrilloses. N Engl J Med 302:1283-1292.
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 18
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984): Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 20
    • 0029075189 scopus 로고
    • Amyloid P component promotes aggregation of Alzheimer's beta-amyloid peptide
    • Hamazaki H (1995): Amyloid P component promotes aggregation of Alzheimer's beta-amyloid peptide. Biochem Biophys Res Commun 211:349-353.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 349-353
    • Hamazaki, H.1
  • 21
    • 0028246095 scopus 로고
    • Concentration of serum amyloid P component in the CSF as a possible marker of cerebral amyloid deposits in Alzheimer's disease
    • Hawkins PN, Rossor MN, Gallimore JR, Miller B, Moore EG, Pepys MB (1994): Concentration of serum amyloid P component in the CSF as a possible marker of cerebral amyloid deposits in Alzheimer's disease. Biochem Biophys Res Commun 201: 722-726.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 722-726
    • Hawkins, P.N.1    Rossor, M.N.2    Gallimore, J.R.3    Miller, B.4    Moore, E.G.5    Pepys, M.B.6
  • 23
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarret JT, Berger EP, Lansbury PT (1993): The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarret, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 24
    • 0028178458 scopus 로고
    • β-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q a chain
    • Jiang H, Burdick D, Glabe CG, Cotman CW, Tenner AJ (1994): β-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain. J Immunol 152:5050-5059.
    • (1994) J Immunol , vol.152 , pp. 5050-5059
    • Jiang, H.1    Burdick, D.2    Glabe, C.G.3    Cotman, C.W.4    Tenner, A.J.5
  • 25
    • 0025905126 scopus 로고
    • Widespread serum amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders
    • Kalaria RN, Galloway PG, Perry G (1991): Widespread serum amyloid P immunoreactivity in cortical amyloid deposits and the neurofibrillary pathology of Alzheimer's disease and other degenerative disorders. Neuropathol Appl Neurobiol 17:189-201.
    • (1991) Neuropathol Appl Neurobiol , vol.17 , pp. 189-201
    • Kalaria, R.N.1    Galloway, P.G.2    Perry, G.3
  • 26
    • 0027080695 scopus 로고
    • Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition
    • Kisilevsky R (1992): Proteoglycans, glycosaminoglycans, amyloid-enhancing factor, and amyloid deposition. J Intern Med 232: 515-516.
    • (1992) J Intern Med , vol.232 , pp. 515-516
    • Kisilevsky, R.1
  • 27
    • 0028853238 scopus 로고
    • Apolipoprotein E (apoE) polymorphism and its influence on apoE concentrations in the cerebrospinal fluid in Finnish patients with Alzheimer's disease
    • Lehtimaki T, Pirttila T, Mehta PD, Wisniewski HM, Frey H, Nikkari T (1995): Apolipoprotein E (apoE) polymorphism and its influence on apoE concentrations in the cerebrospinal fluid in Finnish patients with Alzheimer's disease. Hum Genet 95:39-42.
    • (1995) Hum Genet , vol.95 , pp. 39-42
    • Lehtimaki, T.1    Pirttila, T.2    Mehta, P.D.3    Wisniewski, H.M.4    Frey, H.5    Nikkari, T.6
  • 28
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H (1993): Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 2:404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine, H.1
  • 29
    • 0001733723 scopus 로고
    • Thioflavine T interaction with amyloid β-sheet structures Amyloid
    • LeVine H (1995): Thioflavine T interaction with amyloid β-sheet structures Amyloid. Int J Exp Clin Invest 2:1-6.
    • (1995) Int J Exp Clin Invest , vol.2 , pp. 1-6
    • LeVine, H.1
  • 32
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red
    • Lorenzo A, Yankner BA (1994): β-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
  • 33
    • 0028173205 scopus 로고
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature 372:92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 35
    • 0026493598 scopus 로고
    • Analysis for cerebrospinal fluid proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Mashige F, Shimizu T, Iijima S, Ohkubo A (1992): Analysis for cerebrospinal fluid proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Clin Chem 38:2008-2012.
    • (1992) Clin Chem , vol.38 , pp. 2008-2012
    • Mashige, F.1    Shimizu, T.2    Iijima, S.3    Ohkubo, A.4
  • 37
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's Aβ interaction
    • Matsubara E, Frangione B, Ghiso J (1995): Characterization of apolipoprotein J-Alzheimer's Aβ interaction. J Biol Chem 270: 7563-7567.
    • (1995) J Biol Chem , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3
  • 38
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson MP, Tomaselli KJ, Rydel RE (1993): Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res 621:35-49.
    • (1993) Brain Res , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 40
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • Naiki H, Higuchi K, Hosokawa M, Takeda T (1989): Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T. Anal Biochem 177:244-249.
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 41
    • 0025826915 scopus 로고
    • Kinetic analysis of amyloid fibril polymerization in vitro
    • Naiki H, Higuchi K, Nakakuki K, Takeda T (1991): Kinetic analysis of amyloid fibril polymerization in vitro. Lab Invest 65:104-110.
    • (1991) Lab Invest , vol.65 , pp. 104-110
    • Naiki, H.1    Higuchi, K.2    Nakakuki, K.3    Takeda, T.4
  • 45
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991): 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    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 46
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW (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
  • 47
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity
    • Pike CJ, Walencewicz-Wasserman AJ, Kosmoski J, Cribbs DH, Glabe CG, Cotman CW (1995): Structure-activity analyses of β-amyloid peptides: Contributions of the β25-35 region to aggregation and neurotoxicity. J Neurochem 64:253-265.
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 48
    • 10144244720 scopus 로고
    • Effect of apolipoprotein E4 allele on soluble β-amyloid protein concentrations in cerebrospinal fluid from patients with Alzheimer's disease and controls
    • Iqbal K, Mortimer JA, Winblad B, Wisniewski HM (eds): New York: John Wiley & Sons
    • Pirttila T, Mehta PD, Lehtimaki T, Kim KS, Sersen EA, Frey H, Nikkari T, Wisniewski HM (1995): Effect of apolipoprotein E4 allele on soluble β-amyloid protein concentrations in cerebrospinal fluid from patients with Alzheimer's disease and controls. In Iqbal K, Mortimer JA, Winblad B, Wisniewski HM (eds): "Research Advances in Alzheimer's Disease and Related Disorders." New York: John Wiley & Sons, pp 121-128.
    • (1995) Research Advances in Alzheimer's Disease and Related Disorders , pp. 121-128
    • Pirttila, T.1    Mehta, P.D.2    Lehtimaki, T.3    Kim, K.S.4    Sersen, E.A.5    Frey, H.6    Nikkari, T.7    Wisniewski, H.M.8
  • 49
  • 52
    • 0027374047 scopus 로고
    • Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
    • Rebeck GW, Reiter JS, Strickland DK, Hyman BT (1993): Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions. Neuron 11:575-580.
    • (1993) Neuron , vol.11 , pp. 575-580
    • Rebeck, G.W.1    Reiter, J.S.2    Strickland, D.K.3    Hyman, B.T.4
  • 54
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher A, Wolfe D, Palutke M, KuKuruga D (1986): Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Proc Natl Acad Sci USA 83: 2622-2666.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2622-2666
    • Roher, A.1    Wolfe, D.2    Palutke, M.3    Kukuruga, D.4
  • 60
    • 0026771089 scopus 로고
    • Amyloidosis
    • Sipe JD (1992): Amyloidosis. Annu Rev Biochem 61:947-975.
    • (1992) Annu Rev Biochem , vol.61 , pp. 947-975
    • Sipe, J.D.1
  • 64
    • 0029119868 scopus 로고
    • Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, Gelsolin and AA amyloids
    • Soto C, Castano EM, Prelli F, Kumar RA, Baumann M (1995): Apolipoprotein E increases the fibrillogenic potential of synthetic peptides derived from Alzheimer's, Gelsolin and AA amyloids. FEBS Lett 371:110-114.
    • (1995) FEBS Lett , vol.371 , pp. 110-114
    • Soto, C.1    Castano, E.M.2    Prelli, F.3    Kumar, R.A.4    Baumann, M.5
  • 66
    • 0027053903 scopus 로고
    • Human serum amyloid P-component (SAP) selectively binds to immobilized or bound forms of C-reactive protein (CRP)
    • Swanson SJ, Christner RB, Mortensen RF (1992): Human serum amyloid P-component (SAP) selectively binds to immobilized or bound forms of C-reactive protein (CRP). Biochim Biophys Acta 1160:309-316.
    • (1992) Biochim Biophys Acta , vol.1160 , pp. 309-316
    • Swanson, S.J.1    Christner, R.B.2    Mortensen, R.F.3
  • 67
    • 0023798449 scopus 로고
    • Preamyloid deposits in the cerebral cortex of patients with Alzheimer's disease and non-demented individuals
    • Tagliavini F, Giaccone G, Frangione B, Bugiani O (1988): Preamyloid deposits in the cerebral cortex of patients with Alzheimer's disease and non-demented individuals. Neurosci Lett 93:191-196.
    • (1988) Neurosci Lett , vol.93 , pp. 191-196
    • Tagliavini, F.1    Giaccone, G.2    Frangione, B.3    Bugiani, O.4
  • 69
    • 0028331604 scopus 로고
    • Amyloid beta protein-induced neuronal cell death: Neurotoxic properties of aggregated amyloid beta protein
    • Ueda K, Fukui Y, Kageyama H (1994): Amyloid beta protein-induced neuronal cell death: Neurotoxic properties of aggregated amyloid beta protein. Brain Res 639:240-244.
    • (1994) Brain Res , vol.639 , pp. 240-244
    • Ueda, K.1    Fukui, Y.2    Kageyama, H.3
  • 70
    • 0028135459 scopus 로고
    • Enhanced aggregation and β structure of amyloid β peptide after co-incubation with C1q
    • Webster S, O'Barr S, Rogers J (1994): Enhanced aggregation and β structure of amyloid β peptide after co-incubation with C1q. J Neurosci Res 39:448-456.
    • (1994) J Neurosci Res , vol.39 , pp. 448-456
    • Webster, S.1    O'Barr, S.2    Rogers, J.3
  • 71
    • 0029417189 scopus 로고
    • Multivalent binding of complement protein C1q to the amyloid β-peptide promotes the nucleation phase of Aβ aggregation
    • Webster S, Glabe C, Rogers J (1995): Multivalent binding of complement protein C1q to the amyloid β-peptide promotes the nucleation phase of Aβ aggregation. Biochem Biophys Res Commun 217:869-875.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 869-875
    • Webster, S.1    Glabe, C.2    Rogers, J.3
  • 72
    • 0028303072 scopus 로고
    • Apolipoprotein E: Structure-function relationships
    • Weisgraber KH (1994): Apolipoprotein E: Structure-function relationships. Adv Prot Chem 45:249-301.
    • (1994) Adv Prot Chem , vol.45 , pp. 249-301
    • Weisgraber, K.H.1
  • 73
    • 0002898753 scopus 로고
    • Reexamination of the pathogenesis of the senile plaques
    • Wisniewski HM, Terry RD (1973): Reexamination of the pathogenesis of the senile plaques. Prog Neuropathol 11:1-26.
    • (1973) Prog Neuropathol , vol.11 , pp. 1-26
    • Wisniewski, H.M.1    Terry, R.D.2
  • 74
    • 0027444955 scopus 로고
    • Cerebrospinal fluid inhibits Alzheimer β-amyloid fibril formation in vitro
    • Wisniewski T, Castano E, Ghiso J, Frangione B (1993a): Cerebrospinal fluid inhibits Alzheimer β-amyloid fibril formation in vitro. Ann Neurol 34:631-633.
    • (1993) Ann Neurol , vol.34 , pp. 631-633
    • Wisniewski, T.1    Castano, E.2    Ghiso, J.3    Frangione, B.4
  • 76
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castano EM, Golabek A, Vogel T, 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
  • 77
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood SJ, Maleeff B, Hart T, Wetzel R (1996): Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J Mol Biol 256: 870-877.
    • (1996) J Mol Biol , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.