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Volumn 9, Issue 6, 2014, Pages

High resolution imaging study of interactions between the 37 kDa/67 kDa laminin receptor and APP, beta-secretase and gamma-secretase in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GAMMA SECRETASE; LAMININ RECEPTOR; PROTEIN BINDING; SECRETASE;

EID: 84903516906     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0100373     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 33745893779 scopus 로고    scopus 로고
    • Alzheimer disease: Progress or profit?
    • DOI 10.1038/nm0706-780, PII NM0706780
    • Mount C, Downton C (2006) Alzheimer disease: progress or profit? Nat Med 12: 780-784. (Pubitemid 44050066)
    • (2006) Nature Medicine , vol.12 , Issue.7 , pp. 780-784
    • Mount, C.1    Downton, C.2
  • 4
    • 84863011560 scopus 로고    scopus 로고
    • Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death
    • Kudo W, Lee HP, Zou WQ, Wang X, Perry G, et al. (2012) Cellular prion protein is essential for oligomeric amyloid-beta-induced neuronal cell death. Hum Mol Genet 21: 1138-1144.
    • (2012) Hum Mol Genet , vol.21 , pp. 1138-1144
    • Kudo, W.1    Lee, H.P.2    Zou, W.Q.3    Wang, X.4    Perry, G.5
  • 5
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease
    • DOI 10.2174/1389203043486937
    • Verdier Y, Penke B (2004) Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Curr Protein Pept Sci 5: 19-31. (Pubitemid 38279402)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.1 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 7
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457: 1128-1132.
    • (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
  • 8
    • 79956302348 scopus 로고    scopus 로고
    • Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein
    • Barry AE, Klyubin I, Mc Donald JM, Mably AJ, Farrell MA, et al. (2011) Alzheimer's disease brain-derived amyloid-beta-mediated inhibition of LTP in vivo is prevented by immunotargeting cellular prion protein. J Neurosci 31: 7259-7263.
    • (2011) J Neurosci , vol.31 , pp. 7259-7263
    • Barry, A.E.1    Klyubin, I.2    Mc Donald, J.M.3    Mably, A.J.4    Farrell, M.A.5
  • 9
    • 84863116075 scopus 로고    scopus 로고
    • Abeta neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors
    • You H, Tsutsui S, Hameed S, Kannanayakal TJ, Chen L, et al. (2012) Abeta neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors. Proc Natl Acad Sci U S A 109: 1737-1742.
    • (2012) Proc Natl Acad Sci U S a , vol.109 , pp. 1737-1742
    • You, H.1    Tsutsui, S.2    Hameed, S.3    Kannanayakal, T.J.4    Chen, L.5
  • 10
    • 84874585213 scopus 로고    scopus 로고
    • Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
    • Um JW, Strittmatter SM (2013) Amyloid-beta induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease. Prion 7: 37-41.
    • (2013) Prion , vol.7 , pp. 37-41
    • Um, J.W.1    Strittmatter, S.M.2
  • 11
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um JW, Nygaard HB, Heiss JK, Kostylev MA, Stagi M, et al. (2012) Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 15: 1227-1235.
    • (2012) Nat Neurosci , vol.15 , pp. 1227-1235
    • Um, J.W.1    Nygaard, H.B.2    Heiss, J.K.3    Kostylev, M.A.4    Stagi, M.5
  • 15
    • 78650501836 scopus 로고    scopus 로고
    • Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor
    • Omar A, Jovanovic K, Da Costa Dias B, Gonsalves D, Moodley K, et al. (2011) Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor. Expert Opin Ther Pat 21: 35-53.
    • (2011) Expert Opin Ther Pat , vol.21 , pp. 35-53
    • Omar, A.1    Jovanovic, K.2    Da Costa Dias, B.3    Gonsalves, D.4    Moodley, K.5
  • 16
    • 84900464448 scopus 로고    scopus 로고
    • Anti-LRP/LR Specific Antibody IgG1-iS18 Impedes Adhesion and Invasion of Liver Cancer Cells
    • Chetty C, Khumalo T, Da Costa Dias B, Reusch U, Knackmuss S, et al. (2014) Anti-LRP/LR Specific Antibody IgG1-iS18 Impedes Adhesion and Invasion of Liver Cancer Cells. PLoS One 9: e96268.
    • (2014) PLoS One , vol.9
    • Chetty, C.1    Khumalo, T.2    Da Costa Dias, B.3    Reusch, U.4    Knackmuss, S.5
  • 17
    • 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, Knackmuss S, Zemora G, Reusch U, Vlasova E, et al. (2008) 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) J Mol Biol , vol.378 , pp. 530-539
    • Zuber, C.1    Knackmuss, S.2    Zemora, G.3    Reusch, U.4    Vlasova, E.5
  • 18
    • 84860295356 scopus 로고    scopus 로고
    • Anti-LRP/LR-specific 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 SF (2012) Anti-LRP/LR-specific antibody IgG1-iS18 significantly reduces adhesion and invasion of metastatic lung, cervix, colon and prostate cancer cells. J Mol Biol 419: 102-109.
    • (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
  • 19
    • 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, Reusch U, Knackmuss S, Little M, Veale RB, et al. (2013) Adhesion and Invasion of Breast and Oesophageal Cancer Cells Are Impeded by Anti-LRP/LR-Specific Antibody IgG1-iS18. PLoS One 8: e66297.
    • (2013) PLoS One , vol.8
    • Khumalo, T.1    Reusch, U.2    Knackmuss, S.3    Little, M.4    Veale, R.B.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 SF (2013) Downregulation of the non-integrin laminin receptor reduces cellular viability by inducing apoptosis in lung and cervical cancer cells. PLoS One 8: e57409.
    • (2013) PLoS One , vol.8
    • Moodley, K.1    Weiss, S.F.2
  • 21
    • 84874855399 scopus 로고    scopus 로고
    • In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor
    • Khusal R, Da Costa Dias B, Moodley K, Penny C, Reusch U, et al. (2013) In vitro inhibition of angiogenesis by antibodies directed against the 37 kDa/67 kDa laminin receptor. PLoS One 8: e58888.
    • (2013) PLoS One , vol.8
    • Khusal, R.1    Da Costa Dias, B.2    Moodley, K.3    Penny, C.4    Reusch, U.5
  • 22
    • 84884656967 scopus 로고    scopus 로고
    • Anti-LRP/LR specific antibodies and shRNAs impede amyloid beta shedding in Alzheimer's disease
    • Jovanovic K, Gonsalves D, Da Costa Dias B, Moodley K, Reusch U, et al. (2013) Anti-LRP/LR specific antibodies and shRNAs impede amyloid beta shedding in Alzheimer's disease. Sci Rep 3: 2699.
    • (2013) Sci Rep , vol.3 , pp. 2699
    • Jovanovic, K.1    Gonsalves, D.2    Da Costa Dias, B.3    Moodley, K.4    Reusch, U.5
  • 24
    • 42749095169 scopus 로고    scopus 로고
    • Subcellular localisation of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins
    • Nikles D, Vana K, Gauczynski S, Knetsch H, Ludewigs H, et al. (2008) Subcellular localisation of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins. Biochim Biophys Acta 1782: 335-340.
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 335-340
    • Nikles, D.1    Vana, K.2    Gauczynski, S.3    Knetsch, H.4    Ludewigs, H.5
  • 25
    • 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 (2006) A trans-dominant negative 37 kDa/67 kDa laminin receptor mutant impairs PrP(Sc) propagation in scrapie-infected neuronal cells. J Mol Biol 358: 57-66.
    • (2006) J Mol Biol , vol.358 , pp. 57-66
    • Vana, K.1    Weiss, S.2
  • 26
    • 9444282652 scopus 로고    scopus 로고
    • Demonstration of BACE (beta-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy
    • DOI 10.1242/jcs.01422
    • von Arnim CA, Tangredi MM, Peltan ID, Lee BM, Irizarry MC, et al. (2004) Demonstration of BACE (beta-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy. J Cell Sci 117: 5437-5445. (Pubitemid 39562504)
    • (2004) Journal of Cell Science , vol.117 , Issue.22 , pp. 5437-5445
    • Von, A.C.A.F.1    Tangredi, M.M.2    Peltan, I.D.3    Lee, B.M.4    Irizarry, M.C.5    Kinoshita, A.6    Hyman, B.T.7
  • 27
    • 70849116652 scopus 로고    scopus 로고
    • Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio
    • Uemura K, Lill CM, Li X, Peters JA, Ivanov A, et al. (2009) Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio. PLoS One 4: e7893.
    • (2009) PLoS One , vol.4
    • Uemura, K.1    Lill, C.M.2    Li, X.3    Peters, J.A.4    Ivanov, A.5
  • 28
    • 0032639282 scopus 로고    scopus 로고
    • Laterall modulated excitation microscopy: Improvement of resolution by using a diffraction grating
    • Bigio IJ, Schneckenburger H, Slavik J, Svanberg K, Viallet PM, editors.
    • Heintzmann R, Cremer CG (1999) Laterall modulated excitation microscopy: improvement of resolution by using a diffraction grating. In: Bigio IJ, Schneckenburger H, Slavik J, Svanberg K, Viallet PM, editors. SPIE digital Library. pp. 185-196.
    • (1999) SPIE Digital Library , pp. 185-196
    • Heintzmann, R.1    Cremer, C.G.2
  • 29
    • 0036618178 scopus 로고    scopus 로고
    • Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells
    • Shaw G, Morse S, Ararat M, Graham FL (2002) Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J 16: 869-871.
    • (2002) FASEB J , vol.16 , pp. 869-871
    • Shaw, G.1    Morse, S.2    Ararat, M.3    Graham, F.L.4
  • 31
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, et al. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 398: 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5
  • 32
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • DOI 10.1074/jbc.M409272200
    • Chyung JH, Raper DM, Selkoe DJ (2005) Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem 280: 4383-4392. (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
  • 34
    • 0033921739 scopus 로고    scopus 로고
    • Diverse patterns of expression of the 67-kD laminin receptor in human small intestinal mucosa: Potential binding sites for prion proteins?
    • DOI 10.1002/1096-9896(2000)9999:9999<::AID-PATH640
    • Shmakov AN, Bode J, Kilshaw PJ, Ghosh S (2000) Diverse patterns of expression of the 67-kD laminin receptor in human small intestinal mucosa: potential binding sites for prion proteins? J Pathol 191: 318-322. (Pubitemid 30441257)
    • (2000) Journal of Pathology , vol.191 , Issue.3 , pp. 318-322
    • Shmakov, A.N.1    Bode, J.2    Kilshaw, P.J.3    Ghosh, S.4
  • 37
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, et al. (1999) Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5
  • 39
    • 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 HH, Whitehouse IJ, Baybutt H, Brown D, Kellett KA, et al. (2011) 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) J Biol Chem , vol.286 , pp. 33489-33500
    • Griffiths, H.H.1    Whitehouse, I.J.2    Baybutt, H.3    Brown, D.4    Kellett, K.A.5
  • 41
    • 0242585507 scopus 로고    scopus 로고
    • Sc propagation in scrapie-infected neuronal cells
    • DOI 10.1038/sj.embor.embor768
    • Leucht C, Simoneau S, Rey C, Vana K, Rieger R, et al. (2003) The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep 4: 290-295. (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
  • 43
    • 0142059961 scopus 로고    scopus 로고
    • Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's beta-secretase
    • DOI 10.1083/jcb.200303059
    • Scholefield Z, Yates EA, Wayne G, Amour A, McDowell W, et al. (2003) Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's beta-secretase. J Cell Biol 163: 97-107. (Pubitemid 37271437)
    • (2003) Journal of Cell Biology , vol.163 , Issue.1 , pp. 97-107
    • Scholefield, Z.1    Yates, E.A.2    Wayne, G.3    Amour, A.4    McDowell, W.5    Turnbull, J.E.6
  • 44
    • 27844454447 scopus 로고    scopus 로고
    • Novel heparan sulphate analogues: Inhibition of beta-secretase cleavage of amyloid precursor protein
    • DOI 10.1042/BST20051116
    • Patey SJ, Yates EA, Turnbull JE (2005) Novel heparan sulphate analogues: inhibition of beta-secretase cleavage of amyloid precursor protein. Biochem Soc Trans 33: 1116-1118. (Pubitemid 41659127)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.5 , pp. 1116-1118
    • Patey, S.J.1    Yates, E.A.2    Turnbull, J.E.3
  • 45
    • 33744760876 scopus 로고    scopus 로고
    • Heparin activates beta-secretase (BACE1) of Alzheimer's disease and increases autocatalysis of the enzyme
    • DOI 10.1021/bi052498t
    • Beckman M, Holsinger RM, Small DH (2006) Heparin activates beta-secretase (BACE1) of Alzheimer's disease and increases autocatalysis of the enzyme. Biochemistry 45: 6703-6714. (Pubitemid 43825371)
    • (2006) Biochemistry , vol.45 , Issue.21 , pp. 6703-6714
    • Beckman, M.1    Holsinger, R.M.D.2    Small, D.H.3
  • 46
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • DOI 10.1523/JNEUROSCI.5345-07.2008
    • Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, et al. (2008) Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci 28: 2874-2882. (Pubitemid 351398889)
    • (2008) Journal of Neuroscience , vol.28 , Issue.11 , pp. 2874-2882
    • Schneider, A.1    Rajendran, L.2    Honsho, M.3    Gralle, M.4    Donnert, G.5    Wouters, F.6    Hell, S.W.7    Simons, M.8
  • 47
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • DOI 10.1083/jcb.200207113
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K (2003) Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160: 113-123. (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
  • 48
    • 64049093215 scopus 로고    scopus 로고
    • Molecular targets of (-)-epigallocatechin-3-gallate (EGCG): Specificity and interaction with membrane lipid rafts
    • Patra SK, Rizzi F, Silva A, Rugina DO, Bettuzzi S (2008) Molecular targets of (-)-epigallocatechin-3-gallate (EGCG): specificity and interaction with membrane lipid rafts. J Physiol Pharmacol 59 Suppl 9: 217-235.
    • (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


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