메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

Anti-LRP/LR specific antibodies and shRNAs impede amyloid beta shedding in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; LAMININ RECEPTOR; MONOCLONAL ANTIBODY; SECRETASE; SMALL INTERFERING RNA;

EID: 84884656967     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02699     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • DOI 10.1038/nm0706-780, PII NM0706780
    • Mount, C. & Downton, C. Alzheimer disease: progress or profit? Nat Med 12, 780-784 (2006) (Pubitemid 44050066)
    • (2006) Nature Medicine , vol.12 , Issue.7 , pp. 780-784
    • Mount, C.1    Downton, C.2
  • 2
    • 80053385335 scopus 로고    scopus 로고
    • The Alzheimer's amyloid beta-peptide (Abeta) binds a specific DNA Abeta-interacting domain (AbetaID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: Characterizing a new regulatory motif
    • Maloney, B. & Lahiri, D. K. The Alzheimer's amyloid beta-peptide (Abeta) binds a specific DNA Abeta-interacting domain (AbetaID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: characterizing a new regulatory motif. Gene 488, 1-12 (2011)
    • (2011) Gene , vol.488 , pp. 1-12
    • Maloney, B.1    Lahiri, D.K.2
  • 3
    • 84863504256 scopus 로고    scopus 로고
    • Apolipoprotein e and apolipoprotein e receptors: Normal biology and roles in Alzheimer disease
    • Holtzman, D. M., Herz, J. & Bu, G. Apolipoprotein e and apolipoprotein e receptors: normal biology and roles in Alzheimer disease. Cold Spring Harb Perspect Med 2, a006312, http://dx.doi.org/10.1101/cshperspect. a006312 (2012)
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Holtzman, D.M.1    Herz, J.2    Bu, G.3
  • 4
    • 33745140951 scopus 로고    scopus 로고
    • Tau phosphorylation and aggregation in Alzheimer's disease pathology
    • DOI 10.1016/j.febslet.2006.02.067, PII S0014579306002705
    • Avila, J. Tau phosphorylation and aggregation in Alzheimer's disease pathology. FEBS Lett 580, 2922-2927 (2006) (Pubitemid 44250900)
    • (2006) FEBS Letters , vol.580 , Issue.12 , pp. 2922-2927
    • Avila, J.1
  • 5
    • 84857225871 scopus 로고    scopus 로고
    • Global Alzheimer Research Summit: Basic and clinical research: Present and future Alzheimer research
    • Gonsalves, D., Jovanovic, K., Da Costa Dias, B. & Weiss, S. F. Global Alzheimer Research Summit: Basic and clinical research: Present and future Alzheimer research. Prion 6, 7-10 (2012)
    • (2012) Prion , vol.6 , pp. 7-10
    • Gonsalves, D.1    Jovanovic, K.2    Da Costa Dias, B.3    Weiss, S.F.4
  • 6
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio, J., Lorenzo, A., Yeh, J. & Yankner, B. A. beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14, 879-888 (1995)
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 8
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999)
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 9
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of gamma-secretase activity
    • Edbauer, D. et al. Reconstitution of gamma-secretase activity. Nat Cell Biol 5, 486-488, http://dx.doi.org/10.1038/ncb960 (2003)
    • (2003) Nat Cell Biol , vol.5 , pp. 486-488
    • Edbauer, D.1
  • 10
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid β-peptide in cell plasma membrane and implications for Alzheimer's disease
    • DOI 10.2174/1389203043486937
    • Verdier, Y. & Penke, B. Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Curr Protein Pept Sci 5, 19-31 (2004) (Pubitemid 38279402)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.1 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 11
    • 80052804919 scopus 로고    scopus 로고
    • Structural and mechanistic commonalities of amyloid-beta and the prion protein
    • Da Costa Dias, B., Jovanovic, K., Gonsalves, D. & Weiss, S. F. Structural and mechanistic commonalities of amyloid-beta and the prion protein. Prion 5, 126-137 (2011)
    • (2011) Prion , vol.5 , pp. 126-137
    • Da Costa Dias, B.1    Jovanovic, K.2    Gonsalves, D.3    Weiss, S.F.4
  • 12
    • 77955701756 scopus 로고    scopus 로고
    • Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property
    • Sepulveda, F. J., Parodi, J., Peoples, R. W., Opazo, C. & Aguayo, L. G. Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property. PLoS One 5, e11820, http://dx.doi.org/10.1371/journal. pone.0011820 (2010)
    • (2010) PLoS One , vol.5
    • Sepulveda, F.J.1    Parodi, J.2    Peoples, R.W.3    Opazo, C.4    Aguayo, L.G.5
  • 14
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W. & Strittmatter, S. M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457, 1128-1132 (2009)
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 15
    • 84863011560 scopus 로고    scopus 로고
    • Cellular prion protein is essential for oligomeric amyloid-betainduced neuronal cell death
    • Kudo, W. et al. Cellular prion protein is essential for oligomeric amyloid-betainduced neuronal cell death. Hum Mol Genet 21, 1138-1144 (2012)
    • (2012) Hum Mol Genet , vol.21 , pp. 1138-1144
    • Kudo, W.1
  • 16
    • 84860225557 scopus 로고    scopus 로고
    • Cellular prion protein mediates toxic signaling of amyloid beta
    • Resenberger, U. K.,Winklhofer, K. F. & Tatzelt, J. Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta. Neurodegener Dis 10, 298-300 (2012)
    • (2012) Neurodegener Dis , vol.10 , pp. 298-300
    • Resenberger, U.K.1    Winklhofer, K.F.2    Tatzelt, J.3
  • 17
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um, J. W. et al. Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 15, 1227-1235 (2012)
    • (2012) Nat Neurosci , vol.15 , pp. 1227-1235
    • Um, J.W.1
  • 18
    • 0034332511 scopus 로고    scopus 로고
    • Laminin inhibition of beta-amyloid protein (Abeta) fibrillogenesis and identification of an Abeta binding site localized to the globular domain repeats on the laminin a chain
    • Castillo, G. M. et al. Laminin inhibition of beta-amyloid protein (Abeta) fibrillogenesis and identification of an Abeta binding site localized to the globular domain repeats on the laminin a chain. J Neurosci Res 62, 451-462 (2000)
    • (2000) J Neurosci Res , vol.62 , pp. 451-462
    • Castillo, G.M.1
  • 19
    • 77956630769 scopus 로고    scopus 로고
    • Interactions between PrPc and other ligands with the 37-kDa/67-kDa laminin receptor
    • Mbazima, V., Da Costa Dias, B., Omar, A., Jovanovic, K. &Weiss, S. Interactions between PrPc and other ligands with the 37-kDa/67-kDa laminin receptor. Frontiers in Bioscience 15, 1150-1163 (2010)
    • (2010) Frontiers in Bioscience , vol.15 , pp. 1150-1163
    • Mbazima, V.1    Da Costa Dias, B.2    Omar, A.3    Jovanovic, K.4    Weiss, S.5
  • 20
    • 84874596593 scopus 로고    scopus 로고
    • Downregulation of the non-integrin laminin receptor reduces cellular viability by inducing apoptosis in lung and cervical cancer cells
    • Moodley, K. &Weiss, S. F. Downregulation of the non-integrin laminin receptor reduces cellular viability by inducing apoptosis in lung and cervical cancer cells. PLoS One 8, e57409, http://dx.doi.org/10.1371/journal.pone.0057409 PONE-D-12-36482 (2013)
    • (2013) PLoS One , vol.8
    • Moodley, K.1    Weiss, S.F.2
  • 21
    • 78650501836 scopus 로고    scopus 로고
    • Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor
    • Omar, A. et al. Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor. Expert Opin Ther Pat 21, 35-53, http://dx.doi.org/10.1517/13543776.2011.539203 (2011)
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 35-53
    • Omar, A.1
  • 22
    • 84874855399 scopus 로고    scopus 로고
    • In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor
    • Khusal, R. et al. In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor. PLoS One 8, e58888, http://dx.doi.org/10.1371/journal.pone.0058888 (2013)
    • (2013) PLoS One 8
    • Khusal, R.1
  • 23
    • 84879191167 scopus 로고    scopus 로고
    • Adhesion and invasion of breast and oesophageal cancer cells are impeded by Anti-LRP/LR-Specific antibody IgG1-iS18
    • Khumalo, T. et al. Adhesion and Invasion of Breast and Oesophageal Cancer Cells Are Impeded by Anti-LRP/LR-Specific Antibody IgG1-iS18. PLoS One 8, e66297, http://dx.doi.org/10.1371/journal.pone.0066297 PONE-D-13-07741 (2013)
    • (2013) PLoS One , vol.8
    • Khumalo, T.1
  • 24
    • 84860295356 scopus 로고    scopus 로고
    • Anti-LRP/LRspecific antibody IgG1-iS18 significantly reduces adhesion and invasion of metastatic lung, cervix, colon and prostate cancer cells
    • Omar, A., Reusch, U., Knackmuss, S., Little, M. & Weiss, S. F. Anti-LRP/LRspecific antibody IgG1-iS18 significantly reduces adhesion and invasion of metastatic lung, cervix, colon and prostate cancer cells. J Mol Biol 419, 102-109 (2012)
    • (2012) J Mol Biol , vol.419 , pp. 102-109
    • Omar, A.1    Reusch, U.2    Knackmuss, S.3    Little, M.4    Weiss, S.F.5
  • 27
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • DOI 10.1038/nm1297-1383
    • Rieger, R., Edenhofer, F., Lasmezas, C. I. &Weiss, S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. NatMed 3, 1383-1388 (1997) (Pubitemid 28011039)
    • (1997) Nature Medicine , vol.3 , Issue.12 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmezas, C.I.3    Weiss, S.4
  • 29
    • 26244466387 scopus 로고    scopus 로고
    • Bovine prion is endocytosed by human enterocytes via the 37 kDa/67 kDa laminin receptor
    • [pii]
    • Morel, E. et al. Bovine prion is endocytosed by human enterocytes via the 37 kDa/67 kDa laminin receptor. Am J Pathol 167, 1033-1042 [pii] (2005)
    • (2005) Am J Pathol , vol.167 , pp. 1033-1042
    • Morel, E.1
  • 30
    • 0242585507 scopus 로고    scopus 로고
    • Sc propagation in scrapie-infected neuronal cells
    • DOI 10.1038/sj.embor.embor768
    • Leucht, C. et al. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep 4, 290-295, http://dx.doi.org/10.1038/sj.embor.embor768 (2003) (Pubitemid 36511726)
    • (2003) EMBO Reports , vol.4 , Issue.3 , pp. 290-295
    • Leucht, C.1    Simoneau, S.2    Rey, C.3    Vana, K.4    Rieger, R.5    Lasmezas, C.I.6    Weiss, S.7
  • 31
    • 79955163875 scopus 로고    scopus 로고
    • A practical guide to evaluating colocalization in biological microscopy
    • Dunn, K.W., Kamocka, M. M. &McDonald, J. H. A practical guide to evaluating colocalization in biological microscopy. Am J Physiol Cell Physiol 300, C723-742 (2011)
    • (2011) Am J Physiol Cell Physiol , vol.300
    • Dunn, K.W.1    Kamocka, M.M.2    McDonald, J.H.3
  • 32
    • 42449160941 scopus 로고    scopus 로고
    • Invasion of tumorigenic HT1080 cells is impeded by blocking or downregulating the 37-kDa/67-kDa laminin receptor
    • Zuber, C. et al. Invasion of tumorigenic HT1080 cells is impeded by blocking or downregulating the 37-kDa/67-kDa laminin receptor. J Mol Biol 378, 530-539 (2008)
    • (2008) J Mol Biol , vol.378 , pp. 530-539
    • Zuber, C.1
  • 33
    • 0028027047 scopus 로고
    • Cell localization and redistribution of the 67 kD laminin receptor and α6β1 integrin subunits in response to laminin stimulation: An immunogold electron microscopy study
    • Romanov, V., Sobel, M. E., pinto da Silva, P., Menard, S. & Castronovo, V. Cell localization and redistribution of the 67 kD laminin receptor and alpha 6 beta 1 integrin subunits in response to laminin stimulation: an immunogold electron microscopy study. Cell Adhes Commun 2, 201-209 (1994) (Pubitemid 24282667)
    • (1994) Cell Adhesion and Communication , vol.2 , Issue.3 , pp. 201-209
    • Romanov, V.1    Sobel, M.E.2    Pinto Da Silva, P.3    Menard, S.4    Castronovo, V.5
  • 34
    • 64049093215 scopus 로고    scopus 로고
    • Molecular targets of (2)-epigallocatechin-3-gallate (EGCG): Specificity and interaction with membrane lipid rafts
    • Patra, S. K., Rizzi, F., Silva, A., Rugina, D. O. & Bettuzzi, S. Molecular targets of (2)-epigallocatechin-3-gallate (EGCG): specificity and interaction with membrane lipid rafts. J Physiol Pharmacol 59 Suppl 9, 217-235 (2008)
    • (2008) J Physiol Pharmacol , vol.59 , Issue.SUPPL. 9 , pp. 217-235
    • Patra, S.K.1    Rizzi, F.2    Silva, A.3    Rugina, D.O.4    Bettuzzi, S.5
  • 36
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • Ehehalt, R., Keller, P., Haass, C., Thiele, C. & Simons, K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160, 113-123, http://dx.doi.org/10.1083/jcb. 200207113 (2003) (Pubitemid 36091721)
    • (2003) Journal of Cell Biology , vol.160 , Issue.1 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 37
    • 0042887148 scopus 로고    scopus 로고
    • Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes
    • DOI 10.1242/jcs.00643
    • Kinoshita, A. et al.Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes. J Cell Sci 116, 3339-3346 (2003) (Pubitemid 37038982)
    • (2003) Journal of Cell Science , vol.116 , Issue.16 , pp. 3339-3346
    • Kinoshita, A.1    Fukumoto, H.2    Shah, T.3    Whelan, C.M.4    Irizarry, M.C.5    Hyman, B.T.6
  • 38
    • 80052149544 scopus 로고    scopus 로고
    • ADP ribosylation factor 6 (ARF6) controls amyloid precursor protein (APP) processing by mediating the endosomal sorting of BACE1
    • Sannerud, R. et al. ADP ribosylation factor 6 (ARF6) controls amyloid precursor protein (APP) processing by mediating the endosomal sorting of BACE1. Proc Natl Acad Sci U S A 108, E559-568 (2011)
    • (2011) Proc Natl Acad Sci U S A , vol.108
    • Sannerud, R.1
  • 39
    • 14244268498 scopus 로고    scopus 로고
    • γ-Secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • DOI 10.1074/jbc.M409272200
    • Chyung, J. H., Raper, D. M. & Selkoe, D. J. Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem 280, 4383-4392 (2005) (Pubitemid 40288602)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 41
    • 80052979854 scopus 로고    scopus 로고
    • Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein
    • Griffiths, H. H. et al. Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein. J Biol Chem 286, 33489-33500 (2011)
    • (2011) J Biol Chem , vol.286 , pp. 33489-33500
    • Griffiths, H.H.1
  • 42
    • 1842532328 scopus 로고    scopus 로고
    • The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
    • Pasternak, S. H., Callahan, J. W. & Mahuran, D. J. The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective. J Alzheimers Dis 6, 53-65 (2004) (Pubitemid 38418558)
    • (2004) Journal of Alzheimer's Disease , vol.6 , Issue.1 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 43
    • 84869070324 scopus 로고    scopus 로고
    • Beta-Site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1)-deficient mice exhibit a close homolog of L1 (CHL1) loss-of-function phenotype involving axon guidance defects
    • Hitt, B. et al. beta-Site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1)-deficient mice exhibit a close homolog of L1 (CHL1) loss-of-function phenotype involving axon guidance defects. J Biol Chem 287, 38408-38425 (2012)
    • (2012) J Biol Chem , vol.287 , pp. 38408-38425
    • Hitt, B.1
  • 44
    • 84884646966 scopus 로고    scopus 로고
    • Anti-LRP/LR specific antibody IgG1-iS18 and knockdown of LRP/LR by shRNAs rescue cells from Ab42 induced cytotoxicity
    • Da Costa Dias, B. et al. Anti-LRP/LR specific antibody IgG1-iS18 and knockdown of LRP/LR by shRNAs rescue cells from Ab42 induced cytotoxicity. Sci. Rep. 3, 2702; http://dx.doi.org/10.1038/srep02702 (2013)
    • (2013) Sci. Rep , vol.3 , pp. 2702
    • Da Costa Dias, B.1
  • 45
    • 33645100082 scopus 로고    scopus 로고
    • A trans-dominant negative 37 kDa/67 kDa laminin receptor mutant impairs PrP(Sc) propagation in scrapie-infected neuronal cells
    • Vana, K. &Weiss, S. A trans-dominant negative 37 kDa/67 kDa laminin receptor mutant impairs PrP(Sc) propagation in scrapie-infected neuronal cells. JMol Biol 358, 57-66 (2006)
    • (2006) J Mol Biol , vol.358 , pp. 57-66
    • Vana, K.1    Weiss, S.2
  • 46
    • 42749095169 scopus 로고    scopus 로고
    • Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins
    • Nikles, D. et al. Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins. Biochim Biophys Acta 1782, 335-340 (2008)
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 335-340
    • Nikles, D.1
  • 47
    • 9444282652 scopus 로고    scopus 로고
    • Demonstration of BACE (beta-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy
    • von Arnim, C. A. et al. Demonstration of BACE (beta-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy. J Cell Sci 117, 5437-5445 (2004)
    • (2004) J Cell Sci , vol.117 , pp. 5437-5445
    • Von Arnim, C.A.1
  • 48
    • 70849116652 scopus 로고    scopus 로고
    • Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio
    • Uemura, K. et al. Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio. PLoS One 4, e7893, http://dx.doi.org/10.1371/journal.pone.0007893 (2009).
    • (2009) PLoS One , vol.4
    • Uemura, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.