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Volumn 18, Issue 4, 2007, Pages 1490-1496

Activation of microglia acidifies lysosomes and leads to degradation of Alzheimer amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; AMYLOID; AMYLOID BETA PROTEIN; ANION TRANSPORT PROTEIN; COLONY STIMULATING FACTOR 1; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; FORSKOLIN; INTERLEUKIN 6; LYSOSOME ENZYME; PROTEINASE;

EID: 34247264399     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-10-0975     Document Type: Article
Times cited : (203)

References (41)
  • 1
    • 11844252117 scopus 로고    scopus 로고
    • Cutting edge: Macrophage inhibition by cyclic AMP (cAMP): differential roles of protein kinase A and exchange protein directly activated by cAMP-1
    • Aronoff, D. M., Canetti, C., Serezani, C. H., Luo, M., and Peters-Golden, M. (2005). Cutting edge: macrophage inhibition by cyclic AMP (cAMP): differential roles of protein kinase A and exchange protein directly activated by cAMP-1. J. Immunol. 174, 595-599.
    • (2005) J. Immunol , vol.174 , pp. 595-599
    • Aronoff, D.M.1    Canetti, C.2    Serezani, C.H.3    Luo, M.4    Peters-Golden, M.5
  • 3
    • 0025604331 scopus 로고
    • Protein kinase A regulates chloride conductance in endocytic vesicles from proximal tubule
    • Bae, H. R., and Verkman, A. S. (1990). Protein kinase A regulates chloride conductance in endocytic vesicles from proximal tubule. Nature 348, 637-639.
    • (1990) Nature , vol.348 , pp. 637-639
    • Bae, H.R.1    Verkman, A.S.2
  • 4
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard, F. et al. (2000). Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6, 916-919.
    • (2000) Nat. Med , vol.6 , pp. 916-919
    • Bard, F.1
  • 5
    • 0034595821 scopus 로고    scopus 로고
    • Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia
    • Brazil, M. I., Chung, H., and Maxfield, F. R. (2000). Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia. J. Biol. Chem. 275, 16941-16947.
    • (2000) J. Biol. Chem , vol.275 , pp. 16941-16947
    • Brazil, M.I.1    Chung, H.2    Maxfield, F.R.3
  • 6
    • 0034577943 scopus 로고    scopus 로고
    • IL-6 switches the differentiation of monocytes from dendritic cells to macrophages
    • Chomarat, P., Banchereau, J., Davoust, J., and Palucka, A. K. (2000). IL-6 switches the differentiation of monocytes from dendritic cells to macrophages. Nat. Immunol. 1, 510-514.
    • (2000) Nat. Immunol , vol.1 , pp. 510-514
    • Chomarat, P.1    Banchereau, J.2    Davoust, J.3    Palucka, A.K.4
  • 7
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells
    • Chung, H., Brazil, M. I., Soe, T. T., and Maxfield, F. R. (1999). Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells. J. Biol. Chem. 274, 32301-32308.
    • (1999) J. Biol. Chem , vol.274 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 8
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice
    • Das, P., Howard, V., Loosbrock, N., Dickson, D., Murphy, M. P., and Golde, T. E. (2003). Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice. J. Neurosci. 23, 8532-8538.
    • (2003) J. Neurosci , vol.23 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 9
    • 33748623095 scopus 로고    scopus 로고
    • Interleukin-1 receptor 1 knockout has no effect on amyloid deposition in Tg2576 mice and does not alter efficacy following Abeta immunotherapy
    • Das, P., Smithson, L. A., Price, R. W., Holloway, V. M., Levites, Y., Chakrabarty, P., and Golde, T. E. (2006). Interleukin-1 receptor 1 knockout has no effect on amyloid deposition in Tg2576 mice and does not alter efficacy following Abeta immunotherapy. J. Neuroinflammation 3, 17.
    • (2006) J. Neuroinflammation , vol.3 , pp. 17
    • Das, P.1    Smithson, L.A.2    Price, R.W.3    Holloway, V.M.4    Levites, Y.5    Chakrabarty, P.6    Golde, T.E.7
  • 10
    • 1442355270 scopus 로고    scopus 로고
    • Ratio imaging instrumentation
    • Dunn, K., and Maxfield, F. R. (2003). Ratio imaging instrumentation. Methods Cell Biol. 72, 389-413.
    • (2003) Methods Cell Biol , vol.72 , pp. 389-413
    • Dunn, K.1    Maxfield, F.R.2
  • 11
    • 0028111942 scopus 로고
    • Regulation of endocytic trafficking and acidification are independent of the cystic fibrosis transmembrane regulator
    • Dunn, K. W., Park, J., Semrad, C. E., German, D. L., Shevell, T., and McGraw, T. E. (1994). Regulation of endocytic trafficking and acidification are independent of the cystic fibrosis transmembrane regulator. J. Biol. Chem. 269, 5336-5345.
    • (1994) J. Biol. Chem , vol.269 , pp. 5336-5345
    • Dunn, K.W.1    Park, J.2    Semrad, C.E.3    German, D.L.4    Shevell, T.5    McGraw, T.E.6
  • 12
    • 0029787599 scopus 로고    scopus 로고
    • Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils
    • El Khoury, J., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., and Loike, J. D. (1996). Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils. Nature 382, 716-719.
    • (1996) Nature , vol.382 , pp. 716-719
    • El Khoury, J.1    Hickman, S.E.2    Thomas, C.A.3    Cao, L.4    Silverstein, S.C.5    Loike, J.D.6
  • 13
    • 24644435506 scopus 로고    scopus 로고
    • Nasal vaccination with a proteosome-based adjuvant and glatiramer acetate clears beta-amyloid in a mouse model of Alzheimer disease
    • Frenkel, D., Maron, R., Burt, D. S., and Weiner, H. L. (2005). Nasal vaccination with a proteosome-based adjuvant and glatiramer acetate clears beta-amyloid in a mouse model of Alzheimer disease. J. Clin. Investig. 115, 2423-2433.
    • (2005) J. Clin. Investig , vol.115 , pp. 2423-2433
    • Frenkel, D.1    Maron, R.2    Burt, D.S.3    Weiner, H.L.4
  • 14
    • 21544468846 scopus 로고    scopus 로고
    • Treatment with an amyloid-beta antibody ameliorates plaque load, learning deficits, and hippocampal long-term potentiation in a mouse model of Alzheimer's disease
    • Hartman, R. E., Izumi, Y., Bales, K. R., Paul, S. M., Wozniak, D. F., and Holtzman, D. M. (2005). Treatment with an amyloid-beta antibody ameliorates plaque load, learning deficits, and hippocampal long-term potentiation in a mouse model of Alzheimer's disease. J. Neurosci. 25, 6213-6220.
    • (2005) J. Neurosci , vol.25 , pp. 6213-6220
    • Hartman, R.E.1    Izumi, Y.2    Bales, K.R.3    Paul, S.M.4    Wozniak, D.F.5    Holtzman, D.M.6
  • 15
    • 33644508018 scopus 로고    scopus 로고
    • Diverse microglial responses after intrahippocampal administration of lipopolysaccharide
    • Herber, D. L., Maloney, J. L., Roth, L. M., Freeman, M. J., Morgan, D., and Gordon, M. N. (2006). Diverse microglial responses after intrahippocampal administration of lipopolysaccharide. Glia 53, 382-391.
    • (2006) Glia , vol.53 , pp. 382-391
    • Herber, D.L.1    Maloney, J.L.2    Roth, L.M.3    Freeman, M.J.4    Morgan, D.5    Gordon, M.N.6
  • 16
    • 5044222305 scopus 로고    scopus 로고
    • Time-dependent reduction in Abeta levels after intracranial LPS administration in APP transgenic mice
    • Herber, D. L., Roth, L. M., Wilson, D., Wilson, N., Mason, J. E., Morgan, D., and Gordon, M. N. (2004). Time-dependent reduction in Abeta levels after intracranial LPS administration in APP transgenic mice. Exp. Neurol. 190, 245-253.
    • (2004) Exp. Neurol , vol.190 , pp. 245-253
    • Herber, D.L.1    Roth, L.M.2    Wilson, D.3    Wilson, N.4    Mason, J.E.5    Morgan, D.6    Gordon, M.N.7
  • 17
    • 7944234506 scopus 로고    scopus 로고
    • Ion channels: Function unravelled by dysfunction
    • Jentsch, T. J., Hubner, C. A., and Fuhrmann, J. C. (2004). Ion channels: function unravelled by dysfunction. Nat. Cell Biol. 6, 1039-1047.
    • (2004) Nat. Cell Biol , vol.6 , pp. 1039-1047
    • Jentsch, T.J.1    Hubner, C.A.2    Fuhrmann, J.C.3
  • 18
    • 40849105303 scopus 로고    scopus 로고
    • Majumdar, A., Chung, H., Dolios, G., Wang, R., Asamoah, N., Lobel, P., and Maxfield, F. R. (2007). Degradation of fibrillar forms of Alzheimer's amyloid beta-peptide by macrophages. Neurobiol. Aging (in press). doi: 10.1016/j.neurobiolaging.2006.12.001.
    • Majumdar, A., Chung, H., Dolios, G., Wang, R., Asamoah, N., Lobel, P., and Maxfield, F. R. (2007). Degradation of fibrillar forms of Alzheimer's amyloid beta-peptide by macrophages. Neurobiol. Aging (in press). doi: 10.1016/j.neurobiolaging.2006.12.001.
  • 19
    • 0242268945 scopus 로고    scopus 로고
    • Immunotherapeutic approaches to Alzheimer's disease
    • Monsonego, A., and Weiner, H. L. (2003). Immunotherapeutic approaches to Alzheimer's disease. Science 302, 834-838.
    • (2003) Science , vol.302 , pp. 834-838
    • Monsonego, A.1    Weiner, H.L.2
  • 20
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan, D. et al. (2000). A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408, 982-985.
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1
  • 21
    • 24644438615 scopus 로고    scopus 로고
    • Dynamic complexity of the microglial activation response in transgenic models of amyloid deposition: Implications for Alzheimer therapeutics
    • Morgan, D., Gordon, M. N., Tan, J., Wilcock, D., and Rojiani, A. M. (2005). Dynamic complexity of the microglial activation response in transgenic models of amyloid deposition: implications for Alzheimer therapeutics. J. Neuropathol. Exp. Neurol. 64, 743-753.
    • (2005) J. Neuropathol. Exp. Neurol , vol.64 , pp. 743-753
    • Morgan, D.1    Gordon, M.N.2    Tan, J.3    Wilcock, D.4    Rojiani, A.M.5
  • 22
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: A case report
    • Nicoll, J. A., Wilkinson, D., Holmes, C., Steart, P., Markham, H., and Weller, R. O. (2003). Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report. Nat. Med. 9, 448-452.
    • (2003) Nat. Med , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 23
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases - nature's most versatile proton pumps
    • Nishi, T., and Forgac, M. (2002). The vacuolar (H+)-ATPases - nature's most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94-103.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 24
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma, S., and Poole, B. (1978). Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. USA 75, 3327-3331.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 25
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells
    • Paresce, D. M., Chung, H., and Maxfield, F. R. (1997). Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells. J. Biol. Chem. 272, 29390-29397.
    • (1997) J. Biol. Chem , vol.272 , pp. 29390-29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 26
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's Disease amyloid β-protein via a scavenger receptor
    • Paresce, D. M., Ghosh, R., and Maxfield, F. R. (1996). Microglial cells internalize aggregates of the Alzheimer's Disease amyloid β-protein via a scavenger receptor. Neuron 17, 553-565.
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.2    Maxfield, F.R.3
  • 27
    • 0036566039 scopus 로고    scopus 로고
    • Endolysosomal proteolysis and its regulation
    • Pillay, C. S., Elliott, E., and Dennison, C. (2002). Endolysosomal proteolysis and its regulation. Biochem. J. 363, 417-429.
    • (2002) Biochem. J , vol.363 , pp. 417-429
    • Pillay, C.S.1    Elliott, E.2    Dennison, C.3
  • 28
    • 7444254061 scopus 로고    scopus 로고
    • CSF-1 regulation of the wandering macrophage: Complexity in action
    • Pixley, F. J., and Stanley, E. R. (2004). CSF-1 regulation of the wandering macrophage: complexity in action. Trends Cell Biol. 14, 628-638.
    • (2004) Trends Cell Biol , vol.14 , pp. 628-638
    • Pixley, F.J.1    Stanley, E.R.2
  • 29
    • 0027203163 scopus 로고
    • The End2 mutation in CHO cells slows the exit of transferrin receptors from the recycling compartment but bulk membrane recycling is unaffected
    • Presley, J. F., Mayor, S., Dunn, K. W., Johnson, L. S., McGraw, T. E., and Maxfield, F. R. (1993). The End2 mutation in CHO cells slows the exit of transferrin receptors from the recycling compartment but bulk membrane recycling is unaffected. J. Cell Biol. 122, 1231-1241.
    • (1993) J. Cell Biol , vol.122 , pp. 1231-1241
    • Presley, J.F.1    Mayor, S.2    Dunn, K.W.3    Johnson, L.S.4    McGraw, T.E.5    Maxfield, F.R.6
  • 30
    • 0030610528 scopus 로고    scopus 로고
    • Bafilomycin A1 treatment retards transferrin receptor recycling more than bulk membrane recycling
    • Presley, J. F., Mayor, S., McGraw, T. E., Dunn, K. W., and Maxfield, F. R. (1997). Bafilomycin A1 treatment retards transferrin receptor recycling more than bulk membrane recycling. J. Biol. Chem. 272, 13929-13936.
    • (1997) J. Biol. Chem , vol.272 , pp. 13929-13936
    • Presley, J.F.1    Mayor, S.2    McGraw, T.E.3    Dunn, K.W.4    Maxfield, F.R.5
  • 32
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer disease-like pathology in the PDAPP mouse
    • Schenk, D. et al. (1999). Immunization with amyloid-β attenuates Alzheimer disease-like pathology in the PDAPP mouse. Nature 400, 173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 33
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. (2001). Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 34
    • 32344440522 scopus 로고    scopus 로고
    • Bone marrow-derived microglia play a critical role in restricting senile plaque formation in Alzheimer's disease
    • Simard, A. R., Soulet, D., Gowing, G., Julien, J. P., and Rivest, S. (2006). Bone marrow-derived microglia play a critical role in restricting senile plaque formation in Alzheimer's disease. Neuron 49, 489-502.
    • (2006) Neuron , vol.49 , pp. 489-502
    • Simard, A.R.1    Soulet, D.2    Gowing, G.3    Julien, J.P.4    Rivest, S.5
  • 35
    • 27744464859 scopus 로고    scopus 로고
    • The microglial "activation" continuum: From innate to adaptive responses
    • Town, T., Nikolic, V., and Tan, J. (2005). The microglial "activation" continuum: from innate to adaptive responses. J. Neuroinflammation 2, 24.
    • (2005) J. Neuroinflammation , vol.2 , pp. 24
    • Town, T.1    Nikolic, V.2    Tan, J.3
  • 37
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta, E. S., Ebersold, M., Garrett, W., Pypaert, M., and Mellman, I. (2003). Activation of lysosomal function during dendritic cell maturation. Science 299, 1400-1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 38
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynela, J., Sohar, I., Sleat, D. E., Gin, R. M., Donnelly, R. J., Baumann, M., Haltia, M., and Lobel, P. (2000). A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J. 19, 2786-2792.
    • (2000) EMBO J , vol.19 , pp. 2786-2792
    • Tyynela, J.1    Sohar, I.2    Sleat, D.E.3    Gin, R.M.4    Donnelly, R.J.5    Baumann, M.6    Haltia, M.7    Lobel, P.8
  • 39
    • 0038790267 scopus 로고    scopus 로고
    • Origin and turnover of microglial cells in fibrillar plaques of APPsw transgenic mice
    • Wegiel, J., Imaki, H., Wang, K. C., Wronska, A., Osuchowski, M., and Rubenstein, R. (2003). Origin and turnover of microglial cells in fibrillar plaques of APPsw transgenic mice. Acta Neuropathol. 105, 393-402.
    • (2003) Acta Neuropathol , vol.105 , pp. 393-402
    • Wegiel, J.1    Imaki, H.2    Wang, K.C.3    Wronska, A.4    Osuchowski, M.5    Rubenstein, R.6
  • 41
    • 23844451737 scopus 로고    scopus 로고
    • cAMP inhibits CSF-1-stimulated tyrosine phosphorylation but augments CSF-1R-mediated macrophage differentiation and ERK activation
    • Wilson, N. J., Cross, M., Nguyen, T., and Hamilton, J. A. (2005). cAMP inhibits CSF-1-stimulated tyrosine phosphorylation but augments CSF-1R-mediated macrophage differentiation and ERK activation. FEBS J. 272, 4141-4152.
    • (2005) FEBS J , vol.272 , pp. 4141-4152
    • Wilson, N.J.1    Cross, M.2    Nguyen, T.3    Hamilton, J.A.4


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