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Volumn , Issue , 2012, Pages

Microglial amyloid-β1-40 phagocytosis dysfunction is caused by high-mobility group box protein-1: Implications for the pathological progression of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; HIGH MOBILITY GROUP B1 PROTEIN;

EID: 84862288751     PISSN: None     EISSN: 20900252     Source Type: Journal    
DOI: 10.1155/2012/685739     Document Type: Article
Times cited : (57)

References (56)
  • 1
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • DOI 10.1126/science.1074069
    • Selkoe D. J., Alzheimer's disease is a synaptic failure Science 2002 298 5594 789 791 (Pubitemid 35231524)
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 2
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils
    • DOI 10.1126/science.1062097
    • Gtz J., Chen F., Van Dorpe J., Nitsch R. M., Formation of neurofibrillary tangles in P301L tau transgenic mice induced by A 42 fibrils Science 2001 293 5534 1491 1495 (Pubitemid 32807681)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 11
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J., Selkoe D. J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 2002 297 5580 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 12
    • 18444393054 scopus 로고    scopus 로고
    • Highly conserved and disease-specific patterns of carboxyterminally truncated Aβ peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation
    • DOI 10.1046/j.1471-4159.2002.00818.x
    • Wiltfang J., Esselmann H., Bibl M., Smirnov A., Otto M., Paul S., Schmidt B., Klafki H. W., Maler M., Dyrks T., Bienert M., Beyermann M., Rther E., Kornhuber J., Highly conserved and disease-specific patterns of carboxyterminally truncated A peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation Journal of Neurochemistry 2002 81 3 481 496 (Pubitemid 34809327)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.3 , pp. 481-496
    • Wiltfang, J.1    Esselmann, H.2    Bibl, M.3    Smirnov, A.4    Otto, M.5    Paul, S.6    Schmidt, B.7    Klafki, H.-W.8    Maler, M.9    Dyrks, T.10    Bienert, M.11    Beyermann, M.12    Ruther, E.13    Kornhuber, J.14
  • 13
    • 0028169925 scopus 로고
    • Visualization of A 42(43) and A 40 in senile plaques with end-specific A monoclonals: Evidence that an initially deposited species is A 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., Ihara Y., Visualization of A 42(43) and A 40 in senile plaques with end-specific A monoclonals: evidence that an initially deposited species is A 42(43) Neuron 1994 13 1 45 53
    • (1994) Neuron , vol.13 , Issue.1 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 14
    • 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 amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 1993 32 18 4693 4697 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 15
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • DOI 10.1074/jbc.M201750200
    • Dahlgren K. N., Manelli A. M., Blaine Stine W., Baker L. K., Krafft G. A., Ladu M. J., Oligomeric and fibrillar species of amyloid- peptides differentially affect neuronal viability Journal of Biological Chemistry 2002 277 35 32046 32053 (Pubitemid 34969015)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Blaine Stine Jr., W.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 17
    • 0025095717 scopus 로고
    • Morphologic association between microglia and senile plaque amyloid in Alzheimer's disease
    • DOI 10.1016/0304-3940(90)90748-X
    • Perlmutter L. S., Barron E., Chui H. C., Morphologic association between microGlia and senile plaque amyloid in Alzheimer's disease Neuroscience Letters 1990 119 1 32 36 (Pubitemid 20349720)
    • (1990) Neuroscience Letters , vol.119 , Issue.1 , pp. 32-36
    • Perlmutter, L.S.1    Barron, E.2    Chui, H.C.3
  • 18
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor
    • DOI 10.1016/S0896-6273(00)80187-7
    • Paresce D. M., Ghosh R. N., Maxfield F. R., MicroGlial cells internalize aggregates of the Alzheimer's disease amyloid -protein via a scavenger receptor Neuron 1996 17 3 553 565 (Pubitemid 26322226)
    • (1996) Neuron , vol.17 , Issue.3 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 19
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β- protein by microglial cells
    • DOI 10.1074/jbc.272.46.29390
    • Paresce D. M., Chung H., Maxfield F. R., Slow degradation of aggregates of the Alzheimer's disease amyloid -protein by microGlial cells Journal of Biological Chemistry 1997 272 46 29390 29397 (Pubitemid 27498234)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.46 , pp. 29390-29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 26
    • 1042291300 scopus 로고    scopus 로고
    • Dystrophic Microglia in the Aging Human Brain
    • DOI 10.1002/glia.10319
    • Streit W. J., Sammons N. W., Kuhns A. J., Sparks D. L., Dystrophic MicroGlia in the Aging Human Brain Glia 2004 45 2 208 212 (Pubitemid 38196997)
    • (2004) GLIA , vol.45 , Issue.2 , pp. 208-212
    • Streit, W.J.1    Sammons, N.W.2    Kuhns, A.J.3    Sparks, D.L.4
  • 27
    • 51149120624 scopus 로고    scopus 로고
    • MicroGlial dysfunction and defective -amyloid clearance pathways in aging alzheimer's disease mice
    • Hickman S. E., Allison E. K., El Khoury J., MicroGlial dysfunction and defective -amyloid clearance pathways in aging alzheimer's disease mice Journal of Neuroscience 2008 28 33 8354 8360
    • (2008) Journal of Neuroscience , vol.28 , Issue.33 , pp. 8354-8360
    • Hickman, S.E.1    Allison, E.K.2    El Khoury, J.3
  • 28
    • 0035882102 scopus 로고    scopus 로고
    • The double life of HMGB1 chromatin protein: Architectural factor and extracellular signal
    • DOI 10.1093/emboj/20.16.4337
    • Mller S., Scaffidi P., Degryse B., Bonaldi T., Ronfani L., Agresti A., Beltrame M., Bianchi M. E., The double life of HMGB1 chromatin protein: architectural factor and extracellular signal EMBO Journal 2001 20 16 4337 4340 (Pubitemid 32772027)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4337-4340
    • Muller, S.1    Scaffidi, P.2    Degryse, B.3    Bonaldi, T.4    Ronfani, L.5    Agresti, A.6    Beltrame, M.7    Bianchi, M.E.8
  • 29
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • DOI 10.1038/nature00858
    • Scaffidi P., Misteli T., Bianchi M. E., Release of chromatin protein HMGB1 by necrotic cells triggers inflammation Nature 2002 418 6894 191 195 (Pubitemid 34773774)
    • (2002) Nature , vol.418 , Issue.6894 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 30
    • 1542380035 scopus 로고    scopus 로고
    • Involvement of Toll-like Receptors 2 and 4 in Cellular Activation by High Mobility Group Box 1 Protein
    • DOI 10.1074/jbc.M306793200
    • Park J. S., Svetkauskaite D., He Q., Kim J. Y., Strassheim D., Ishizaka A., Abraham E., Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein Journal of Biological Chemistry 2004 279 9 7370 7377 (Pubitemid 38294612)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7370-7377
    • Park, J.S.1    Svetkauskaite, D.2    He, Q.3    Kim, J.-Y.4    Strassheim, D.5    Ishizaka, A.6    Abraham, E.7
  • 32
    • 10644273486 scopus 로고    scopus 로고
    • High mobility group box protein-1 inhibits microglial Aβ clearance and enhances Aβ neurotoxicity
    • DOI 10.1002/jnr.20340
    • Takata K., Kitamura Y., Tsuchiya D., Kawasaki T., Taniguchi T., Shimohama S., High mobility group box protein-1 inhibits microGlial A clearance and enhances A neurotoxicity Journal of Neuroscience Research 2004 78 6 880 891 (Pubitemid 39657575)
    • (2004) Journal of Neuroscience Research , vol.78 , Issue.6 , pp. 880-891
    • Takata, K.1    Kitamura, Y.2    Tsuchiya, D.3    Kawasaki, T.4    Taniguchi, T.5    Shimohama, S.6
  • 34
    • 0032509773 scopus 로고    scopus 로고
    • Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease
    • DOI 10.1016/S0006-8993(97)01202-X, PII S000689939701202X
    • Kitamura Y., Shimohama S., Kamoshima W., Ota T., Matsuoka Y., Nomura Y., Smith M. A., Perry G., Whitehouse P. J., Taniguchi T., Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease Brain Research 1998 780 2 260 269 (Pubitemid 28082914)
    • (1998) Brain Research , vol.780 , Issue.2 , pp. 260-269
    • Kitamura, Y.1    Shimohama, S.2    Kamoshima, W.3    Ota, T.4    Matsuoka, Y.5    Nomura, Y.6    Smith, M.A.7    Perry, G.8    Whitehouse, P.J.9    Taniguchi, T.10
  • 36
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice
    • DOI 10.1126/science.274.5284.99
    • Hsiao K., Chapman P., Nilsen S., Eckman C., Harigaya Y., Younkin S., Yang F., Cole G., Correlative memory deficits, A elevation, and amyloid plaques in transgenic mice Science 1996 274 5284 99 102 (Pubitemid 26332733)
    • (1996) Science , vol.274 , Issue.5284 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 40
    • 32344440522 scopus 로고    scopus 로고
    • Bone marrow-derived microglia play a critical role in restricting senile plaque formation in Alzheimer's disease
    • DOI 10.1016/j.neuron.2006.01.022, PII S0896627306000754
    • Simard A. R., Soulet D., Gowing G., Julien J. P., Rivest S., Bone marrow-derived microGlia play a critical role in restricting senile plaque formation in Alzheimer's disease Neuron 2006 49 4 489 502 (Pubitemid 43221886)
    • (2006) Neuron , vol.49 , Issue.4 , pp. 489-502
    • Simard, A.R.1    Soulet, D.2    Gowing, G.3    Julien, J.-P.4    Rivest, S.5
  • 41
    • 34147115541 scopus 로고    scopus 로고
    • Ccr2 deficiency impairs microglial accumulation and accelerates progression of Alzheimer-like disease
    • DOI 10.1038/nm1555, PII NM1555
    • El Khoury J., Toft M., Hickman S. E., Means T. K., Terada K., Geula C., Luster A. D., Ccr2 deficiency impairs microGlial accumulation and accelerates progression of Alzheimer-like disease Nature Medicine 2007 13 4 432 438 (Pubitemid 46559828)
    • (2007) Nature Medicine , vol.13 , Issue.4 , pp. 432-438
    • El Khoury, J.1    Toft, M.2    Hickman, S.E.3    Means, T.K.4    Terada, K.5    Geula, C.6    Luster, A.D.7
  • 42
    • 77956229704 scopus 로고    scopus 로고
    • Neuropathology after active A 42 immunotherapy: Implications for Alzheimer's disease pathogenesis
    • Boche D., Denham N., Holmes C., Nicoll J. A. R., Neuropathology after active A 42 immunotherapy: implications for Alzheimer's disease pathogenesis Acta Neuropathologica 2010 120 3 369 384
    • (2010) Acta Neuropathologica , vol.120 , Issue.3 , pp. 369-384
    • Boche, D.1    Denham, N.2    Holmes, C.3    Nicoll, J.A.R.4
  • 43
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report
    • DOI 10.1038/nm840
    • Nicolll J. A. R., Wilkinson D., Holmes C., Steart P., Markham H., Weller R. O., Neuropathology of human Alzheimer disease after immunization with amyloid- peptide: a case report Nature Medicine 2003 9 4 448 452 (Pubitemid 36460079)
    • (2003) Nature Medicine , vol.9 , Issue.4 , pp. 448-452
    • Nicolll, J.A.R.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 45
    • 0035964405 scopus 로고    scopus 로고
    • Amphoterin includes a sequence motif which is homologous to the Alzheimer's β-amyloid peptide (Aβ), forms amyloid fibrils in vitro, and binds avidly to Aβ
    • DOI 10.1021/bi002095n
    • Kallijrvi J., Haltia M., Baumann M. H., Amphoterin includes a sequence motif which is homologous to the Alzheimer's -amyloid peptide (A ), forms amyloid fibrils in vitro, and binds avidly to A Biochemistry 2001 40 34 10032 10037 (Pubitemid 32800110)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10032-10037
    • Kallijarvi, J.1    Haltia, M.2    Baumann, M.H.3
  • 46
    • 27344441173 scopus 로고    scopus 로고
    • Metabolism of amyloid-β peptide and Alzheimer's disease
    • DOI 10.1016/j.pharmthera.2005.03.010, PII S0163725805000999
    • Iwata N., Higuchi M., Saido T. C., Metabolism of amyloid- peptide and Alzheimer's disease Pharmacology and Therapeutics 2005 108 2 129 148 (Pubitemid 41527082)
    • (2005) Pharmacology and Therapeutics , vol.108 , Issue.2 , pp. 129-148
    • Iwata, N.1    Higuchi, M.2    Saido, T.C.3
  • 48
    • 58749093072 scopus 로고    scopus 로고
    • IL-4-induced selective clearance of oligomeric -amyloid peptide 1-42 by rat primary type 2 microGlia
    • Shimizu E., Kawahara K., Kajizono M., Sawada M., Nakayama H., IL-4-induced selective clearance of oligomeric -amyloid peptide 1-42 by rat primary type 2 microGlia Journal of Immunology 2008 181 9 6503 6513
    • (2008) Journal of Immunology , vol.181 , Issue.9 , pp. 6503-6513
    • Shimizu, E.1    Kawahara, K.2    Kajizono, M.3    Sawada, M.4    Nakayama, H.5
  • 49
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE)in Alzheimer's disease: Identification of a cellular activation mechanism
    • DOI 10.1006/exnr.2001.7732
    • Lue L. F., Walker D. G., Brachova L., Beach T. G., Rogers J., Schmidt A. M., Stern D. M., Yan S. D., Involvement of microGlial receptor for advanced glycation endproducts (RAGE)in Alzheimer's disease: identification of a cellular activation mechanism Experimental Neurology 2001 171 1 29 45 (Pubitemid 32848443)
    • (2001) Experimental Neurology , vol.171 , Issue.1 , pp. 29-45
    • Lue, L.-F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 50
    • 33750576993 scopus 로고    scopus 로고
    • Role of toll-like receptor signalling in Aβ uptake and clearance
    • DOI 10.1093/brain/awl249
    • Tahara K., Kim H. D., Jin J. J., Maxwell J. A., Li L., Fukuchi K. I., Role of toll-like receptor signalling in A uptake and clearance Brain 2006 129 11 3006 3019 (Pubitemid 44684521)
    • (2006) Brain , vol.129 , Issue.11 , pp. 3006-3019
    • Tahara, K.1    Kim, H.-D.2    Jin, J.-J.3    Maxwell, J.A.4    Li, L.5    Fukuchi, K.-I.6
  • 52
    • 0033557386 scopus 로고    scopus 로고
    • Occurrence of the diffuse amyloid β-protein (Aβ) deposits with numerous Aβ-containing glial cells in the cerebral cortex of patients with Alzheimer's disease
    • DOI 10.1002/(SICI)1098-1136(19990215)25:4<324::AID-GLIA2>3.0.CO;2-5
    • Akiyama H., Mori H., Saido T., Kondo H., Ikeda K., McGeer P. L., Occurrence of the diffuse amyloid -protein (A ) deposits with numerous A -containing Glial cells in the cerebral cortex of patients with Alzheimer's disease Glia 1999 25 4 324 331 (Pubitemid 29083832)
    • (1999) GLIA , vol.25 , Issue.4 , pp. 324-331
    • Akiyama, H.1    Mori, H.2    Saido, T.3    Kondo, H.4    Ikeda, K.5    McGeer, P.L.6
  • 53
    • 34848917621 scopus 로고    scopus 로고
    • High mobility group box 1 protein is released by neural cells upon different stresses and worsens ischemic neurodegeneration in vitro and in vivo
    • DOI 10.1111/j.1471-4159.2007.04788.x
    • Faraco G., Fossati S., Bianchi M. E., Patrone M., Pedrazzi M., Sparatore B., Moroni F., Chiarugi A., High mobility group box 1 protein is released by neural cells upon different stresses and worsens ischemic neurodegeneration in vitro and in vivo Journal of Neurochemistry 2007 103 2 590 603 (Pubitemid 47498027)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.2 , pp. 590-603
    • Faraco, G.1    Fossati, S.2    Bianchi, M.E.3    Patrone, M.4    Pedrazzi, M.5    Sparatore, B.6    Moroni, F.7    Chiarugi, A.8
  • 54
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal
    • DOI 10.1038/nri1594
    • Lotze M. T., Tracey K. J., High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal Nature Reviews Immunology 2005 5 4 331 342 (Pubitemid 40516158)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.4 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 55
    • 36849076615 scopus 로고    scopus 로고
    • Anti-high mobility group box 1 monoclonal antibody ameliorates brain infarction induced by transient ischemia in rats
    • DOI 10.1096/fj.07-8770com
    • Liu K., Mori S., Takahashi H. K., Tomono Y., Wake H., Kanke T., Sato Y., Hiraga N., Adachi N., Yoshino T., Nishibori M., Anti-high mobility group box 1 monoclonal antibody ameliorates brain infarction induced by transient ischemia in rats FASEB Journal 2007 21 14 3904 3916 (Pubitemid 350232348)
    • (2007) FASEB Journal , vol.21 , Issue.14 , pp. 3904-3916
    • Liu, K.1    Mori, S.2    Takahashi, H.K.3    Tomono, Y.4    Wake, H.5    Kanke, T.6    Sato, Y.7    Hiraga, N.8    Adachi, N.9    Yoshino, T.10    Nishibori, M.11


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