메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

Anti-LRP/LR specific antibody IgG1-iS18 and knock-down of LRP/LR by shRNAs rescue cells from Aβ 42 induced cytotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

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

EID: 84884646966     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02702     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 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
  • 3
    • 84857225871 scopus 로고    scopus 로고
    • Global Alzheimer Research Summit: Basic and clinical research: Present and future Alzheimer research
    • doi:10.4161/pri.6.1.18854
    • 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, doi:10.4161/pri.6.1.18854 (2012)
    • (2012) Prion , vol.6 , pp. 7-10
    • Gonsalves, D.1    Jovanovic, K.2    Da Costa Dias, B.3    Weiss, S.F.4
  • 4
    • 84865457490 scopus 로고    scopus 로고
    • Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogenactivated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a
    • doi:10.1074/jbc.M112.340372
    • Kakiya, N. et al. Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogenactivated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a. J Biol Chem 287, 29362-29372, doi:10.1074/jbc.M112.340372 (2012)
    • (2012) J Biol Chem , vol.287 , pp. 29362-29372
    • Kakiya, N.1
  • 5
    • 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
    • DOI 10.1021/bi00069a001
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T., Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (1993) (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 6
    • 0031969223 scopus 로고    scopus 로고
    • Alzheimer's disease as proteolytic disorders: Anabolism and catabolism of β-amyloid
    • DOI 10.1016/S0197-4580(98)00033-5, PII S0197458098000335
    • Saido, T. C. Alzheimer's disease as proteolytic disorders: anabolism and catabolism of beta-amyloid. Neurobiol Aging 19, S69-75 (1998) (Pubitemid 28178942)
    • (1998) Neurobiology of Aging , vol.19 , Issue.SUPPL. 1
    • Saido, T.C.1
  • 8
    • 62649174753 scopus 로고    scopus 로고
    • Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
    • doi:10.1073/pnas.0811698106
    • Koffie, R. M. et al. Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. Proc Natl Acad Sci U S A 106, 4012-4017, doi:10.1073/pnas.0811698106 (2009)
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4012-4017
    • Koffie, R.M.1
  • 9
    • 0028899724 scopus 로고
    • Quantitative analysis of senile plaques in Alzheimer disease: Observation of log-normal size distribution and molecular epidemiology of differences associated with apolipoprotein e genotype and trisomy 21 (Down syndrome
    • Hyman, B. T. et al. Quantitative analysis of senile plaques in Alzheimer disease: observation of log-normal size distribution and molecular epidemiology of differences associated with apolipoprotein E genotype and trisomy 21 (Down syndrome) Proc Natl Acad Sci U S A 92, 3586-3590 (1995)
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3586-3590
    • Hyman, B.T.1
  • 10
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of Amyloid beta-Protein: Synaptic and Network Dysfunction
    • doi:10.1101/cshperspect.a006338
    • Mucke, L. & Selkoe, D. J. Neurotoxicity of Amyloid beta-Protein: Synaptic and Network Dysfunction. Cold Spring Harb Perspect Med 2, a006338, doi:10.1101/cshperspect.a006338 (2012)
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Mucke, L.1    Selkoe, D.J.2
  • 11
    • 78049290389 scopus 로고    scopus 로고
    • Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    • doi:10.1111/j.1742-4658.2010.07889.x
    • Stefani, M. Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity. FEBS J 277, 4602-4613, doi:10.1111/j.1742-4658.2010.07889.x (2010)
    • (2010) FEBS J , vol.277 , pp. 4602-4613
    • Stefani, M.1
  • 12
    • 77955701756 scopus 로고    scopus 로고
    • Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property
    • doi:10.1371/journal.pone.0011820
    • 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, doi: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
  • 13
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DOI 10.1074/jbc.M500997200
    • Demuro, A. et al. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280, 17294-17300, doi:10.1074/jbc.M500997200 (2005) (Pubitemid 41389198)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 14
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • DOI 10.1096/fj.01-0377com
    • Lin, H., Bhatia, R. & Lal, R. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J 15, 2433-2444, doi:10.1096/fj.01-0377com (2001) (Pubitemid 33063171)
    • (2001) FASEB Journal , vol.15 , Issue.13 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 15
    • 79251544549 scopus 로고    scopus 로고
    • Alzheimer's dementia begins as a disease of small blood vessels, damaged by oxidative-induced inflammation and dysregulated amyloid metabolism: Implications for early detection and therapy
    • doi:10.1096/fj.11-0102ufm
    • Marchesi, V. T. Alzheimer's dementia begins as a disease of small blood vessels, damaged by oxidative-induced inflammation and dysregulated amyloid metabolism: implications for early detection and therapy. FASEB J 25, 5-13, doi:10.1096/fj.11-0102ufm (2011)
    • (2011) FASEB J , vol.25 , pp. 5-13
    • Marchesi, V.T.1
  • 16
    • 79959599177 scopus 로고    scopus 로고
    • Alzheimer's disease as homeostatic responses to age-related myelin breakdown
    • doi:10.1016/j.neurobiolaging. 2009.08.007
    • Bartzokis, G. Alzheimer's disease as homeostatic responses to age-related myelin breakdown. Neurobiol Aging 32, 1341-1371, doi:10.1016/j.neurobiolaging. 2009.08.007 (2011)
    • (2011) Neurobiol Aging , vol.32 , pp. 1341-1371
    • Bartzokis, G.1
  • 17
    • 80052804919 scopus 로고    scopus 로고
    • Structural and mechanistic commonalities of amyloid-beta and the prion protein
    • doi:10.4161/pri.5.3.17025
    • 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, doi:10.4161/pri.5.3.17025 (2011)
    • (2011) Prion , vol.5 , pp. 126-137
    • Da Costa Dias, B.1    Jovanovic, K.2    Gonsalves, D.3    Weiss, S.F.4
  • 18
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid Beta protein facilitate hippocampal longterm depression by disrupting neuronal glutamate uptake
    • doi:10.1016/j.neuron.2009.05.012
    • Li, S. et al. Soluble oligomers of amyloid Beta protein facilitate hippocampal longterm depression by disrupting neuronal glutamate uptake. Neuron 62, 788-801, doi:10.1016/j.neuron.2009.05.012 (2009)
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.1
  • 19
    • 84863011560 scopus 로고    scopus 로고
    • Cellular prion protein is essential for oligomeric amyloid-betainduced neuronal cell death
    • doi:10.1093/hmg/ddr542
    • Kudo, W. et al. Cellular prion protein is essential for oligomeric amyloid-betainduced neuronal cell death. Hum Mol Genet 21, 1138-1144, doi:10.1093/hmg/ddr542 (2012)
    • (2012) Hum Mol Genet , vol.21 , pp. 1138-1144
    • Kudo, W.1
  • 20
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication
    • doi:10.1038/emboj.2011.86
    • Resenberger, U. K. et al. The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. EMBO J 30, 2057-2070, doi:10.1038/emboj.2011.86 (2011)
    • (2011) EMBO J , vol.30 , pp. 2057-2070
    • Resenberger, U.K.1
  • 22
    • 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, 290295-, doi: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
  • 23
    • 77956630769 scopus 로고    scopus 로고
    • Interactions between PrP(c) and other ligands with the 37-kDa/67-kDa laminin receptor
    • Mbazima, V., Da Costa Dias, B., Omar, A., Jovanovic, K. & Weiss, S. F. Interactions between PrP(c) and other ligands with the 37-kDa/67-kDa laminin receptor. Front Biosci 15, 1150-1163 (2010)
    • (2010) Front Biosci , vol.15 , pp. 1150-1163
    • Mbazima, V.1    Da Costa Dias, B.2    Omar, A.3    Jovanovic, K.4    Weiss, S.F.5
  • 24
    • 78650501836 scopus 로고    scopus 로고
    • Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor
    • doi:10.1517/13543776.2011.539203
    • 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, doi:10.1517/13543776.2011.539203 (2011)
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 35-53
    • Omar, A.1
  • 28
    • 42449160941 scopus 로고    scopus 로고
    • Invasion of tumorigenic HT1080 cells is impeded by blocking or downregulating the 37-kDa/67-kDa laminin receptor
    • doi:10.1016/j.jmb.2008.02.004
    • 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, doi:10.1016/j.jmb.2008.02.004 (2008)
    • (2008) J Mol Biol , vol.378 , pp. 530-539
    • Zuber, C.1
  • 29
    • 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
    • doi:10.1016/j.jmb.2012.02.035
    • 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, doi:10.1016/j.jmb.2012.02.035 (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
  • 30
    • 84879191167 scopus 로고    scopus 로고
    • Adhesion and invasion of breast and oesophageal cancer cells are impeded by anti-LRP/LR-specific antibody IgG1-iS18
    • doi:10.1371/journal.pone.0066297
    • 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, doi:10.1371/journal.pone.0066297 (2013)
    • (2013) PLoS One , vol.8
    • Khumalo, T.1
  • 31
    • 84874855399 scopus 로고    scopus 로고
    • In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor
    • doi:10.1371/journal.pone.0058888
    • Khusal, R. et al. In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor. PLoS One 8, e58888, doi:10.1371/journal.pone.0058888 (2013)
    • (2013) PLoS One , vol.8
    • Khusal, R.1
  • 34
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: Implications for neuronal damage
    • doi:10.1093/hmg/ddr139
    • Manczak,M., Calkins, M. J.&Reddy, P. H. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage. Hum Mol Genet 20, 2495-2509, doi:10.1093/hmg/ddr139 (2011)
    • (2011) Hum Mol Genet , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 35
    • 79251569266 scopus 로고    scopus 로고
    • Interactions between laminin receptor and the cytoskeleton during translation and cell motility
    • doi:10.1371/journal.pone.0015895
    • Venticinque, L., Jamieson, K. V. & Meruelo, D. Interactions between laminin receptor and the cytoskeleton during translation and cell motility. PLoS One 6, e15895, doi:10.1371/journal.pone.0015895 (2011)
    • (2011) PLoS One , vol.6
    • Venticinque, L.1    Jamieson, K.V.2    Meruelo, D.3
  • 36
    • 2442711686 scopus 로고    scopus 로고
    • r 67,000 laminin receptor
    • DOI 10.1158/0008-5472.CAN-03-3424
    • Givant-Horwitz, V.,Davidson, B.&Reich, R. Laminin-induced signaling in tumor cells: the role of the M(r) 67,000 laminin receptor. Cancer Res 64, 3572-3579, doi:10.1158/0008-5472.CAN-03-3424 (2004) (Pubitemid 38657934)
    • (2004) Cancer Research , vol.64 , Issue.10 , pp. 3572-3579
    • Givant-Horwitz, V.1    Davidson, B.2    Reich, R.3
  • 37
    • 84884656967 scopus 로고    scopus 로고
    • Anti-LRP/LR specific antibodies and shRNAs impede amyloid beta shedding in Alzheimer's disease
    • doi:10.1038/srep02699
    • Jovanovic, J. et al. Anti-LRP/LR specific antibodies and shRNAs impede amyloid beta shedding in Alzheimer's disease. Sci. Rep. 3, 2699; doi:10.1038/srep02699 (2013).
    • (2013) Sci. Rep , vol.3 , pp. 2699
    • Jovanovic, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.