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Volumn 126, Issue 1, 2016, Pages 123-136

Endothelial LRP1 transports amyloid-β1-42 across the blood-brain barrier

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; CD11B ANTIGEN; CRE RECOMBINASE; GLIAL FIBRILLARY ACIDIC PROTEIN; IMMUNOGLOBULIN G; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; TAMOXIFEN; AMYLOID BETA-PROTEIN (1-42); LOW DENSITY LIPOPROTEIN RECEPTOR; LRP1 PROTEIN, MOUSE; PEPTIDE FRAGMENT; TUMOR SUPPRESSOR PROTEIN;

EID: 84956617728     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI81108     Document Type: Article
Times cited : (315)

References (66)
  • 1
    • 78650678688 scopus 로고    scopus 로고
    • Decreased clearance of CNS β-amyloid in Alzheimer's disease
    • Mawuenyega KG, et al. Decreased clearance of CNS β-amyloid in Alzheimer's disease. Science. 2010;330(6012):1774.
    • (2010) Science. , vol.330 , Issue.6012 , pp. 1774
    • Mawuenyega, K.G.1
  • 2
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging
    • Naslund J, et al. Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging. Proc Natl Acad Sci U S A. 1994;91(18):8378-8382.
    • (1994) Proc Natl Acad Sci U S A. , vol.91 , Issue.18 , pp. 8378-8382
    • Naslund, J.1
  • 3
    • 13544268809 scopus 로고    scopus 로고
    • Neurovascular mechanisms of Alzheimer's neurodegeneration
    • Zlokovic BV. Neurovascular mechanisms of Alzheimer's neurodegeneration. Trends Neurosci. 2005;28(4):202-208.
    • (2005) Trends Neurosci. , vol.28 , Issue.4 , pp. 202-208
    • Zlokovic, B.V.1
  • 4
    • 84938949776 scopus 로고    scopus 로고
    • Clearance systems in the brain-implications for Alzheimer disease
    • Tarasoff-Conway JM, et al. Clearance systems in the brain-implications for Alzheimer disease. Nat Rev Neurol. 2015;11(8):457-470.
    • (2015) Nat Rev Neurol. , vol.11 , Issue.8 , pp. 457-470
    • Tarasoff-Conway, J.M.1
  • 5
    • 40849102300 scopus 로고    scopus 로고
    • LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-β peptide in a blood-brain barrier in vitro model
    • Nazer B, Hong S, Selkoe DJ. LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-β peptide in a blood-brain barrier in vitro model. Neurobiol Dis. 2008;30(1):94-102.
    • (2008) Neurobiol Dis. , vol.30 , Issue.1 , pp. 94-102
    • Nazer, B.1    Hong, S.2    Selkoe, D.J.3
  • 6
    • 84889041948 scopus 로고    scopus 로고
    • Neuronal clearance of amyloid-β by endocytic receptor LRP1
    • Kanekiyo T, et al. Neuronal clearance of amyloid-β by endocytic receptor LRP1. J Neurosci. 2013;33(49):19276-19283.
    • (2013) J Neurosci. , vol.33 , Issue.49 , pp. 19276-19283
    • Kanekiyo, T.1
  • 7
    • 84869037441 scopus 로고    scopus 로고
    • LRP1 in brain vascular smooth muscle cells mediates local clearance of Alzheimer's amyloid-β
    • Kanekiyo T, Liu CC, Shinohara M, Li J, Bu G. LRP1 in brain vascular smooth muscle cells mediates local clearance of Alzheimer's amyloid-β. J Neurosci. 2012;32(46):16458-16465.
    • (2012) J Neurosci. , vol.32 , Issue.46 , pp. 16458-16465
    • Kanekiyo, T.1    Liu, C.C.2    Shinohara, M.3    Li, J.4    Bu, G.5
  • 8
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-ss(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata M, et al. Clearance of Alzheimer's amyloid-ss(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J Clin Invest. 2000;106(12):1489-1499.
    • (2000) J Clin Invest. , vol.106 , Issue.12 , pp. 1489-1499
    • Shibata, M.1
  • 9
    • 77957963537 scopus 로고    scopus 로고
    • Amyloid efflux transporter expression at the blood-brain barrier declines in normal aging
    • Silverberg GD, et al. Amyloid efflux transporter expression at the blood-brain barrier declines in normal aging. J Neuropathol Exp Neurol. 2010;69(10):1034-1043.
    • (2010) J Neuropathol Exp Neurol. , vol.69 , Issue.10 , pp. 1034-1043
    • Silverberg, G.D.1
  • 10
    • 0033762062 scopus 로고    scopus 로고
    • Modulation of amyloid β-protein clearance and Alzheimer's disease susceptibility by the LDL receptor-related protein pathway
    • Kang DE, et al. Modulation of amyloid β-protein clearance and Alzheimer's disease susceptibility by the LDL receptor-related protein pathway. J Clin Invest. 2000;106(9):1159-1166.
    • (2000) J Clin Invest. , vol.106 , Issue.9 , pp. 1159-1166
    • Kang, D.E.1
  • 11
    • 34247506244 scopus 로고    scopus 로고
    • Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins e and J in the mouse central nervous system
    • Bell RD, et al. Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system. J Cereb Blood Flow Metab. 2007;27(5):909-918.
    • (2007) J Cereb Blood Flow Metab. , vol.27 , Issue.5 , pp. 909-918
    • Bell, R.D.1
  • 12
    • 57449084208 scopus 로고    scopus 로고
    • ApoE Isoform-specific disruption of amyloid β peptide clearance from mouse brain
    • Deane R, et al. apoE Isoform-specific disruption of amyloid β peptide clearance from mouse brain. J Clin Invest. 2008;118(12):4002-4013.
    • (2008) J Clin Invest. , vol.118 , Issue.12 , pp. 4002-4013
    • Deane, R.1
  • 13
    • 84933277693 scopus 로고    scopus 로고
    • Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance
    • Zhao Z, et al. Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance. Nat Neurosci. 2015;18(7):978-987.
    • (2015) Nat Neurosci. , vol.18 , Issue.7 , pp. 978-987
    • Zhao, Z.1
  • 14
    • 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 GW, Harr SD, Strickland DK, Hyman BT. 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. 1995;37(2):211-217.
    • (1995) Ann Neurol. , vol.37 , Issue.2 , pp. 211-217
    • Rebeck, G.W.1    Harr, S.D.2    Strickland, D.K.3    Hyman, B.T.4
  • 15
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (yin) versus LRP (yang) balance regulates Alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier
    • Deane R, Wu Z, Zlokovic BV. RAGE (yin) versus LRP (yang) balance regulates alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier. Stroke. 2004;35(11 suppl 1):2628-2631.
    • (2004) Stroke. , vol.35 , Issue.11 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3
  • 16
    • 84913553780 scopus 로고    scopus 로고
    • Amyloid-β efflux from the CNS into the plasma
    • Roberts KF, et al. Amyloid-β efflux from the CNS into the plasma. Ann Neurol. 2014;76(6):837-844.
    • (2014) Ann Neurol. , vol.76 , Issue.6 , pp. 837-844
    • Roberts, K.F.1
  • 17
    • 77951934845 scopus 로고    scopus 로고
    • Lack of brainto-blood efflux transport activity of low-density lipoprotein receptor-related protein-1 (LRP-1) for amyloid-β peptide(1-40) in mouse: Involvement of an LRP-1-independent pathway
    • Ito S, Ueno T, Ohtsuki S, Terasaki T. Lack of brainto-blood efflux transport activity of low-density lipoprotein receptor-related protein-1 (LRP-1) for amyloid-β peptide(1-40) in mouse: involvement of an LRP-1-independent pathway. J Neurochem. 2010;113(5):1356-1363.
    • (2010) J Neurochem. , vol.113 , Issue.5 , pp. 1356-1363
    • Ito, S.1    Ueno, T.2    Ohtsuki, S.3    Terasaki, T.4
  • 18
    • 36448976927 scopus 로고    scopus 로고
    • Cerebral clearance of human amyloid-beta peptide (1-40) across the blood-brain barrier is reduced by self-aggregation and formation of low-density lipoprotein receptor-related protein-1 ligand complexes
    • Ito S, Ohtsuki S, Kamiie J, Nezu Y, Terasaki T. Cerebral clearance of human amyloid-beta peptide (1-40) across the blood-brain barrier is reduced by self-aggregation and formation of low-density lipoprotein receptor-related protein-1 ligand complexes. J Neurochem. 2007;103(6):2482-2490.
    • (2007) J Neurochem. , vol.103 , Issue.6 , pp. 2482-2490
    • Ito, S.1    Ohtsuki, S.2    Kamiie, J.3    Nezu, Y.4    Terasaki, T.5
  • 19
    • 58049199498 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein 1 mediates uptake of amyloid β peptides in an in vitro model of the blood-brain barrier cells
    • Yamada K, et al. The low density lipoprotein receptor-related protein 1 mediates uptake of amyloid β peptides in an in vitro model of the blood-brain barrier cells. J Biol Chem. 2008;283(50):34554-34562.
    • (2008) J Biol Chem. , vol.283 , Issue.50 , pp. 34554-34562
    • Yamada, K.1
  • 20
    • 84919632560 scopus 로고    scopus 로고
    • In vitro discrimination of the role of LRP1 at the BBB cellular level: Focus on brain capillary endothelial cells and brain pericytes
    • Candela P, et al. In vitro discrimination of the role of LRP1 at the BBB cellular level: focus on brain capillary endothelial cells and brain pericytes. Brain Res. 2015;1594:15-26.
    • (2015) Brain Res. , vol.1594 , pp. 15-26
    • Candela, P.1
  • 21
    • 84893833082 scopus 로고    scopus 로고
    • Differences in amyloid-β clearance across mouse and human blood-brain barrier models: Kinetic analysis and mechanistic modeling
    • Qosa H, et al. Differences in amyloid-β clearance across mouse and human blood-brain barrier models: kinetic analysis and mechanistic modeling. Neuropharmacology. 2014;79:668-678.
    • (2014) Neuropharmacology. , vol.79 , pp. 668-678
    • Qosa, H.1
  • 22
    • 0026439778 scopus 로고
    • LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • Herz J, Clouthier DE, Hammer RE. LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell. 1992;71(3):411-421.
    • (1992) Cell. , vol.71 , Issue.3 , pp. 411-421
    • Herz, J.1    Clouthier, D.E.2    Hammer, R.E.3
  • 23
    • 0027229924 scopus 로고
    • Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • Herz J, Couthier DE, Hammer RE. Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell. 1993;73(3):428.
    • (1993) Cell. , vol.73 , Issue.3 , pp. 428
    • Herz, J.1    Couthier, D.E.2    Hammer, R.E.3
  • 24
    • 84855483251 scopus 로고    scopus 로고
    • TAK1 in brain endothelial cells mediates fever and lethargy
    • Ridder DA, et al. TAK1 in brain endothelial cells mediates fever and lethargy. J Exp Med. 2011;208(13):2615-2623.
    • (2011) J Exp Med. , vol.208 , Issue.13 , pp. 2615-2623
    • Ridder, D.A.1
  • 25
    • 0032004972 scopus 로고    scopus 로고
    • Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants
    • Rohlmann A, Gotthardt M, Hammer RE, Herz J. Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants. J Clin Invest. 1998;101(3):689-695.
    • (1998) J Clin Invest. , vol.101 , Issue.3 , pp. 689-695
    • Rohlmann, A.1    Gotthardt, M.2    Hammer, R.E.3    Herz, J.4
  • 26
    • 0035168814 scopus 로고    scopus 로고
    • Genotyping of Cre-lox mice and detection of tissue-specific recombination by multiplex PCR
    • Leneuve P, Zaoui R, Monget P, Le Bouc Y, Holzenberger M. Genotyping of Cre-lox mice and detection of tissue-specific recombination by multiplex PCR. Biotechniques. 2001;31(5):1156-1160.
    • (2001) Biotechniques. , vol.31 , Issue.5 , pp. 1156-1160
    • Leneuve, P.1    Zaoui, R.2    Monget, P.3    Le Bouc, Y.4    Holzenberger, M.5
  • 27
    • 0028298886 scopus 로고
    • Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons
    • Bu G, Maksymovitch EA, Nerbonne JM, Schwartz AL. Expression and function of the low density lipoprotein receptor-related protein (LRP) in mammalian central neurons. J Biol Chem. 1994;269(28):18521-18528.
    • (1994) J Biol Chem. , vol.269 , Issue.28 , pp. 18521-18528
    • Bu, G.1    Maksymovitch, E.A.2    Nerbonne, J.M.3    Schwartz, A.L.4
  • 28
    • 50349092250 scopus 로고    scopus 로고
    • LDL receptor-related protein 1: Unique tissue-specific functions revealed by selective gene knockout studies
    • Lillis AP, Van Duyn LB, Murphy-Ullrich JE, Strickland DK. LDL receptor-related protein 1: unique tissue-specific functions revealed by selective gene knockout studies. Physiol Rev. 2008;88(3):887-918.
    • (2008) Physiol Rev. , vol.88 , Issue.3 , pp. 887-918
    • Lillis, A.P.1    Van Duyn, L.B.2    Murphy-Ullrich, J.E.3    Strickland, D.K.4
  • 29
    • 0026693345 scopus 로고
    • Characterization and immunohistochemical localization of α2-macroglobulin receptor (low-density lipoprotein receptorrelated protein) in human brain
    • Wolf BB, Lopes MB, VandenBerg SR, Gonias SL. Characterization and immunohistochemical localization of α2-macroglobulin receptor (low-density lipoprotein receptorrelated protein) in human brain. Am J Pathol. 1992;141(1):37-42.
    • (1992) Am J Pathol. , vol.141 , Issue.1 , pp. 37-42
    • Wolf, B.B.1    Lopes, M.B.2    VandenBerg, S.R.3    Gonias, S.L.4
  • 30
    • 0029094357 scopus 로고
    • Subcellular localization of the low density lipoprotein receptor-related protein (α2-macroglobulin receptor) in human brain
    • Tooyama I, et al. Subcellular localization of the low density lipoprotein receptor-related protein (α2-macroglobulin receptor) in human brain. Brain Res. 1995;691(1-2):235-238.
    • (1995) Brain Res. , vol.691 , Issue.1-2 , pp. 235-238
    • Tooyama, I.1
  • 31
    • 0027263617 scopus 로고
    • Immunohistochemical study of α2 macroglobulin receptor in Alzheimer and control postmortem human brain
    • Tooyama I, Kawamata T, Akiyama H, Moestrup SK, Gliemann J, McGeer PL. Immunohistochemical study of α2 macroglobulin receptor in Alzheimer and control postmortem human brain. Mol Chem Neuropathol. 1993;18(1-2):153-160.
    • (1993) Mol Chem Neuropathol. , vol.18 , Issue.1-2 , pp. 153-160
    • Tooyama, I.1    Kawamata, T.2    Akiyama, H.3    Moestrup, S.K.4    Gliemann, J.5    McGeer, P.L.6
  • 32
    • 80053652475 scopus 로고    scopus 로고
    • LRP1 mediates bidirectional transcytosis of amyloid-β across the blood-brain barrier
    • Pflanzner T, et al. LRP1 mediates bidirectional transcytosis of amyloid-β across the blood-brain barrier. Neurobiol Aging. 2011;32(12):2323 e1-2323 11.
    • (2011) Neurobiol Aging. , vol.32 , Issue.12 , pp. 2323e1-2323e11
    • Pflanzner, T.1
  • 33
    • 84863895905 scopus 로고    scopus 로고
    • Enhanced brain amyloid-β clearance by rifampicin and caffeine as a possible protective mechanism against Alzheimer's disease
    • Qosa H, Abuznait AH, Hill RA, Kaddoumi A. Enhanced brain amyloid-β clearance by rifampicin and caffeine as a possible protective mechanism against Alzheimer's disease. J Alzheimers Dis. 2012;31(1):151-165.
    • (2012) J Alzheimers Dis. , vol.31 , Issue.1 , pp. 151-165
    • Qosa, H.1    Abuznait, A.H.2    Hill, R.A.3    Kaddoumi, A.4
  • 34
    • 84859425248 scopus 로고    scopus 로고
    • Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier
    • Pflanzner T, et al. Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier. J Cereb Blood Flow Metab. 2012;32(4):628-632.
    • (2012) J Cereb Blood Flow Metab. , vol.32 , Issue.4 , pp. 628-632
    • Pflanzner, T.1
  • 35
    • 0035947646 scopus 로고    scopus 로고
    • Differential functions of members of the low density lipoprotein receptor family suggested by their distinct endocytosis rates
    • Li Y, Lu W, Marzolo MP, Bu G. Differential functions of members of the low density lipoprotein receptor family suggested by their distinct endocytosis rates. J Biol Chem. 2001;276(21):18000-18006.
    • (2001) J Biol Chem. , vol.276 , Issue.21 , pp. 18000-18006
    • Li, Y.1    Lu, W.2    Marzolo, M.P.3    Bu, G.4
  • 36
    • 2442594971 scopus 로고    scopus 로고
    • Early-onset and robust cerebral microvascular accumulation of amyloid β-protein in transgenic mice expressing low levels of a vasculotropic Dutch/Iowa mutant form of amyloid β-protein precursor
    • Davis J, et al. Early-onset and robust cerebral microvascular accumulation of amyloid β-protein in transgenic mice expressing low levels of a vasculotropic Dutch/Iowa mutant form of amyloid β-protein precursor. J Biol Chem. 2004;279(19):20296-20306.
    • (2004) J Biol Chem. , vol.279 , Issue.19 , pp. 20296-20306
    • Davis, J.1
  • 37
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • Oakley H, et al. Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J Neurosci. 2006;26(40):10129-10140.
    • (2006) J Neurosci. , vol.26 , Issue.40 , pp. 10129-10140
    • Oakley, H.1
  • 38
    • 0034744296 scopus 로고    scopus 로고
    • TGF-β1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice
    • Wyss-Coray T, et al. TGF-β1 promotes microglial amyloid-beta clearance and reduces plaque burden in transgenic mice. Nat Med. 2001;7(5):612-618.
    • (2001) Nat Med. , vol.7 , Issue.5 , pp. 612-618
    • Wyss-Coray, T.1
  • 39
    • 0037394788 scopus 로고    scopus 로고
    • Adult mouse astrocytes degrade amyloid-beta in vitro and in situ
    • Wyss-Coray T, et al. Adult mouse astrocytes degrade amyloid-beta in vitro and in situ. Nat Med. 2003;9(4):453-457.
    • (2003) Nat Med. , vol.9 , Issue.4 , pp. 453-457
    • Wyss-Coray, T.1
  • 40
    • 0021173996 scopus 로고
    • Developments of a water-maze procedure for studying spatial learning in the rat
    • Morris R. Developments of a water-maze procedure for studying spatial learning in the rat. J Neurosci Methods. 1984;11(1):47-60.
    • (1984) J Neurosci Methods. , vol.11 , Issue.1 , pp. 47-60
    • Morris, R.1
  • 41
    • 84881099652 scopus 로고    scopus 로고
    • N-truncated amyloid beta (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits
    • Bouter Y, et al. N-truncated amyloid beta (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits. Acta Neuropathol. 2013;126(2):189-205.
    • (2013) Acta Neuropathol. , vol.126 , Issue.2 , pp. 189-205
    • Bouter, Y.1
  • 42
    • 43149089590 scopus 로고    scopus 로고
    • Assessment of developmental milestones in rodents
    • Chapter 8:Unit 8.18
    • Heyser CJ. Assessment of developmental milestones in rodents. Curr Protoc Neurosci. 2004;Chapter 8:Unit 8.18.
    • (2004) Curr Protoc Neurosci.
    • Heyser, C.J.1
  • 43
    • 84901378800 scopus 로고    scopus 로고
    • Deciphering the molecular profile of plaques, memory decline and neuron loss in two mouse models for Alzheimer's disease by deep sequencing
    • Bouter Y, et al. Deciphering the molecular profile of plaques, memory decline and neuron loss in two mouse models for Alzheimer's disease by deep sequencing. Front Aging Neurosci. 2014;6:75.
    • (2014) Front Aging Neurosci. , vol.6 , pp. 75
    • Bouter, Y.1
  • 44
    • 0036218738 scopus 로고    scopus 로고
    • Alzheimer disease as a vascular disorder: Nosological evidence
    • de la Torre JC. Alzheimer disease as a vascular disorder: nosological evidence. Stroke. 2002;33(4):1152-1162.
    • (2002) Stroke. , vol.33 , Issue.4 , pp. 1152-1162
    • De La Torre, J.C.1
  • 45
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola C. Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat Rev Neurosci. 2004;5(5):347-360.
    • (2004) Nat Rev Neurosci. , vol.5 , Issue.5 , pp. 347-360
    • Iadecola, C.1
  • 46
    • 84865485770 scopus 로고    scopus 로고
    • LRP1-dependent endocytic mechanism governs the signaling output of the bmp system in endothelial cells and in angiogenesis
    • Pi X, et al. LRP1-dependent endocytic mechanism governs the signaling output of the bmp system in endothelial cells and in angiogenesis. Circ Res. 2012;111(5):564-574.
    • (2012) Circ Res. , vol.111 , Issue.5 , pp. 564-574
    • Pi, X.1
  • 47
    • 80053523669 scopus 로고    scopus 로고
    • Bloodbrain-barrier models for the investigation of transporter-and receptor-mediated amyloid-β clearance in Alzheimer's disease
    • Pflanzner T, Kuhlmann CR, Pietrzik CU. Bloodbrain-barrier models for the investigation of transporter-and receptor-mediated amyloid-β clearance in Alzheimer's disease. Curr Alzheimer Res. 2010;7(7):578-590.
    • (2010) Curr Alzheimer Res. , vol.7 , Issue.7 , pp. 578-590
    • Pflanzner, T.1    Kuhlmann, C.R.2    Pietrzik, C.U.3
  • 48
    • 0142137232 scopus 로고    scopus 로고
    • Lipoprotein receptor-mediated induction of matrix metalloproteinase by tissue plasminogen activator
    • Wang X, et al. Lipoprotein receptor-mediated induction of matrix metalloproteinase by tissue plasminogen activator. Nat Med. 2003;9(10):1313-1317.
    • (2003) Nat Med. , vol.9 , Issue.10 , pp. 1313-1317
    • Wang, X.1
  • 49
    • 84901341240 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor-related protein 1 and amyloid-β clearance in Alzheimer's disease
    • Kanekiyo T, Bu G. The low-density lipoprotein receptor-related protein 1 and amyloid-β clearance in Alzheimer's disease. Front Aging Neurosci. 2014;6:93.
    • (2014) Front Aging Neurosci. , vol.6 , pp. 93
    • Kanekiyo, T.1    Bu, G.2
  • 50
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms
    • Deane R, et al. LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms. Neuron. 2004;43(3):333-344.
    • (2004) Neuron. , vol.43 , Issue.3 , pp. 333-344
    • Deane, R.1
  • 51
    • 34948888151 scopus 로고    scopus 로고
    • Clearance of amyloid-β by circulating lipoprotein receptors
    • Sagare A, et al. Clearance of amyloid-β by circulating lipoprotein receptors. Nat Med. 2007;13(9):1029-1031.
    • (2007) Nat Med. , vol.13 , Issue.9 , pp. 1029-1031
    • Sagare, A.1
  • 52
    • 33750017850 scopus 로고    scopus 로고
    • Functional characterization of the brain-to-blood efflux clearance of human amyloid-β peptide (1-40) across the rat blood-brain barrier
    • Ito S, Ohtsuki S, Terasaki T. Functional characterization of the brain-to-blood efflux clearance of human amyloid-β peptide (1-40) across the rat blood-brain barrier. Neurosci Res. 2006;56(3):246-252.
    • (2006) Neurosci Res. , vol.56 , Issue.3 , pp. 246-252
    • Ito, S.1    Ohtsuki, S.2    Terasaki, T.3
  • 53
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: Crossing cellular barriers
    • Tuma P, Hubbard AL. Transcytosis: crossing cellular barriers. Physiol Rev. 2003;83(3):871-932.
    • (2003) Physiol Rev. , vol.83 , Issue.3 , pp. 871-932
    • Tuma, P.1    Hubbard, A.L.2
  • 54
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
    • Dodart JC, et al. Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model. Nat Neurosci. 2002;5(5):452-457.
    • (2002) Nat Neurosci. , vol.5 , Issue.5 , pp. 452-457
    • Dodart, J.C.1
  • 55
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol. 1999;46(6):860-866.
    • (1999) Ann Neurol. , vol.46 , Issue.6 , pp. 860-866
    • McLean, C.A.1
  • 56
    • 77951928742 scopus 로고    scopus 로고
    • The presence of sodium dodecyl sulphate-stable Aβ dimers is strongly associated with Alzheimer-type dementia
    • Mc Donald JM, et al. The presence of sodium dodecyl sulphate-stable Aβ dimers is strongly associated with Alzheimer-type dementia. Brain. 2010;133(pt 5):1328-1341.
    • (2010) Brain. , vol.133 , pp. 1328-1341
    • Mc Donald, J.M.1
  • 57
    • 0034629292 scopus 로고    scopus 로고
    • Modulation of β-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease
    • Ulery PG, et al. Modulation of β-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease. J Biol Chem. 2000;275(10):7410-7415.
    • (2000) J Biol Chem. , vol.275 , Issue.10 , pp. 7410-7415
    • Ulery, P.G.1
  • 59
    • 84859723641 scopus 로고    scopus 로고
    • A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer disease
    • Deane R, et al. A multimodal RAGE-specific inhibitor reduces amyloid β-mediated brain disorder in a mouse model of Alzheimer disease. J Clin Invest. 2012;122(4):1377-1392.
    • (2012) J Clin Invest. , vol.122 , Issue.4 , pp. 1377-1392
    • Deane, R.1
  • 60
    • 1042301280 scopus 로고    scopus 로고
    • Brain capillary endothelium and choroid plexus epithelium regulate transport of transferrin-bound and free iron into the rat brain
    • Deane R, Zheng W, Zlokovic BV. Brain capillary endothelium and choroid plexus epithelium regulate transport of transferrin-bound and free iron into the rat brain. J Neurochem. 2004;88(4):813-820.
    • (2004) J Neurochem. , vol.88 , Issue.4 , pp. 813-820
    • Deane, R.1    Zheng, W.2    Zlokovic, B.V.3
  • 61
    • 27644489474 scopus 로고    scopus 로고
    • P-glycoprotein deficiency at the blood-brain barrier increases amyloid-β deposition in an Alzheimer disease mouse model
    • Cirrito JR, et al. P-glycoprotein deficiency at the blood-brain barrier increases amyloid-β deposition in an Alzheimer disease mouse model. J Clin Invest. 2005;115(11):3285-3290.
    • (2005) J Clin Invest. , vol.115 , Issue.11 , pp. 3285-3290
    • Cirrito, J.R.1
  • 62
    • 84863919429 scopus 로고    scopus 로고
    • Matrix metalloprotease 8-dependent extracellular matrix cleavage at the blood-CSF barrier contributes to lethality during systemic inflammatory diseases
    • Vandenbroucke RE, et al. Matrix metalloprotease 8-dependent extracellular matrix cleavage at the blood-CSF barrier contributes to lethality during systemic inflammatory diseases. J Neurosci. 2012;32(29):9805-9816.
    • (2012) J Neurosci. , vol.32 , Issue.29 , pp. 9805-9816
    • Vandenbroucke, R.E.1
  • 63
    • 78651316278 scopus 로고    scopus 로고
    • Presenilin-1 but not amyloid precursor protein mutations present in mouse models of Alzheimer's disease attenuate the response of cultured cells to γ-secretase modulators regardless of their potency and structure
    • Hahn S, et al. Presenilin-1 but not amyloid precursor protein mutations present in mouse models of Alzheimer's disease attenuate the response of cultured cells to γ-secretase modulators regardless of their potency and structure. J Neurochem. 2011;116(3):385-395.
    • (2011) J Neurochem. , vol.116 , Issue.3 , pp. 385-395
    • Hahn, S.1
  • 64
    • 76949102099 scopus 로고    scopus 로고
    • Pyroglutamate Aβ pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases
    • Wirths O, et al. Pyroglutamate Aβ pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases. J Neural Transm. 2010;117(1):85-96.
    • (2010) J Neural Transm. , vol.117 , Issue.1 , pp. 85-96
    • Wirths, O.1
  • 65
    • 84858040971 scopus 로고    scopus 로고
    • Pyroglutamate amyloid beta (Aβ) aggravates behavioral deficits in transgenic amyloid mouse model for Alzheimer disease
    • Wittnam JL, et al. Pyroglutamate amyloid beta (Aβ) aggravates behavioral deficits in transgenic amyloid mouse model for Alzheimer disease. J Biol Chem. 2012;287(11):8154-8162.
    • (2012) J Biol Chem. , vol.287 , Issue.11 , pp. 8154-8162
    • Wittnam, J.L.1
  • 66
    • 0032847543 scopus 로고    scopus 로고
    • Monoclonal antibodies specific for the native, disease-associated isoform of the prion protein
    • Korth C, Streit P, Oesch B. Monoclonal antibodies specific for the native, disease-associated isoform of the prion protein. Methods Enzymol. 1999;309:106-122.
    • (1999) Methods Enzymol. , vol.309 , pp. 106-122
    • Korth, C.1    Streit, P.2    Oesch, B.3


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