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Volumn 96, Issue 1, 1999, Pages 121-130

The amino-terminus of the amyloid-β protein is critical for the cellular binding and consequent activation of the respiratory burst of human macrophages

Author keywords

Alzheimer's disease; Amyloid peptide; Chemiluminescence; Flow cytometry; Human macrophages; Respiratory burst activity

Indexed keywords

AMYLOID BETA PROTEIN; SYNTHETIC PEPTIDE;

EID: 0033118464     PISSN: 01655728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-5728(99)00019-3     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 0030038809 scopus 로고    scopus 로고
    • Scavenging of Alzheimer's amyloid-β protein by microglia in culture
    • Ard M.D., Cole G.M., Wei J., Mehrle A.P., Fratkin J.D. Scavenging of Alzheimer's amyloid-β protein by microglia in culture. J. Neurosci. Res. 43:1996;190-202.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 190-202
    • Ard, M.D.1    Cole, G.M.2    Wei, J.3    Mehrle, A.P.4    Fratkin, J.D.5
  • 2
    • 0029087348 scopus 로고
    • Modulation of human microglial cell superoxide production by cytokines
    • Chao C.C., Hu S., Peterson P.K. Modulation of human microglial cell superoxide production by cytokines. J. Leukocyte Biol. 58:1995;65-70.
    • (1995) J. Leukocyte Biol. , vol.58 , pp. 65-70
    • Chao, C.C.1    Hu, S.2    Peterson, P.K.3
  • 3
    • 0027355909 scopus 로고
    • Microglia, an in vivo source of reactive oxygen species in the brain
    • In: Seil, F.J. (Ed.), Advances in Neurology, Raven Press, New York
    • Colton, C., Gilbert, D.L., 1993. Microglia, an in vivo source of reactive oxygen species in the brain. In: Seil, F.J. (Ed.), Advances in Neurology, Vol. 59, Neuronal Injury and Regeneration. Raven Press, New York, pp. 321-326.
    • (1993) Neuronal Injury and Regeneration , vol.59 , pp. 321-326
    • Colton, C.1    Gilbert, D.L.2
  • 5
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • Dickson D.W. The pathogenesis of senile plaques. J. Neuropath. Exp. Neurol. 56:1997;321-339.
    • (1997) J. Neuropath. Exp. Neurol. , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 6
    • 0027354484 scopus 로고
    • Microglia and cytokines in neurological disease, with special reference to AIDS and Alzheimer's disease
    • Dickson D.W., Lee S.C., Mattiace L.A., Yen S.C., Brosnan C. Microglia and cytokines in neurological disease, with special reference to AIDS and Alzheimer's disease. Glia. 7:1993;75-83.
    • (1993) Glia , vol.7 , pp. 75-83
    • Dickson, D.W.1    Lee, S.C.2    Mattiace, L.A.3    Yen, S.C.4    Brosnan, C.5
  • 7
    • 0030250852 scopus 로고    scopus 로고
    • The role of complement and activated microglia in the pathogenesis of Alzheimer's disease
    • Eikelenboom P., Veerhuis R. The role of complement and activated microglia in the pathogenesis of Alzheimer's disease. Neurobiol. Aging. 17:1996;673-680.
    • (1996) Neurobiol. Aging , vol.17 , pp. 673-680
    • Eikelenboom, P.1    Veerhuis, R.2
  • 11
    • 0031578728 scopus 로고    scopus 로고
    • Immune responses and dementia
    • In: Reis, D.J., Posner, J.B. (Eds.), Annals of the New York Academy of Sciences, The NY Acad. Sci., New York, NY
    • Giulian, D., 1997. Immune responses and dementia. In: Reis, D.J., Posner, J.B. (Eds.), Annals of the New York Academy of Sciences, Vol. 835, Frontiers of Neurology: A Symposium In Honor Of Fred Plum. The NY Acad. Sci., New York, NY, pp. 91-110.
    • (1997) Frontiers of Neurology: A Symposium in Honor of Fred Plum. , vol.835 , pp. 91-110
    • Giulian, D.1
  • 14
    • 0023110005 scopus 로고
    • Lucigenin chemiluminescence in the assessment of neutrophil superoxide production
    • Gyllenhammar H. Lucigenin chemiluminescence in the assessment of neutrophil superoxide production. J. Immunol. Meth. 97:1987;209-213.
    • (1987) J. Immunol. Meth. , vol.97 , pp. 209-213
    • Gyllenhammar, H.1
  • 15
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59:1992;1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 16
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20:1997;154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 17
    • 0027468515 scopus 로고
    • Synthetic alzheimer amyloid-β/A4 peptides enhance production of complement C3 component by cultured microglial cells
    • Haga S., Ikeda K., Sato M., Ishii T. Synthetic alzheimer amyloid-β/A4 peptides enhance production of complement C3 component by cultured microglial cells. Brain Res. 601:1993;88-94.
    • (1993) Brain Res. , vol.601 , pp. 88-94
    • Haga, S.1    Ikeda, K.2    Sato, M.3    Ishii, T.4
  • 18
    • 0032473596 scopus 로고    scopus 로고
    • Amyloid-β peptide activates cultured astrocytes: Morphological alterations, cytokine induction and nitric oxide release
    • Hu J., Akama K.T., Krafft G., Chromy B.A., Van Eldik L.J. Amyloid-β peptide activates cultured astrocytes: morphological alterations, cytokine induction and nitric oxide release. Brain Res. 785:1998;195-206.
    • (1998) Brain Res. , vol.785 , pp. 195-206
    • Hu, J.1    Akama, K.T.2    Krafft, G.3    Chromy, B.A.4    Van Eldik, L.J.5
  • 19
    • 0030983079 scopus 로고    scopus 로고
    • Transcription factor NF-κB is activated in primary neurons by amyloid-β peptides and in neurons surrounding early plaques from patients with Alzheimer disease
    • Kaltschmidt B., Uherek M., Volk B., Baeurle P.A., Kaltschmidt C. Transcription factor NF-κB is activated in primary neurons by amyloid-β peptides and in neurons surrounding early plaques from patients with Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 94:1997;2642-2647.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2642-2647
    • Kaltschmidt, B.1    Uherek, M.2    Volk, B.3    Baeurle, P.A.4    Kaltschmidt, C.5
  • 20
    • 0030795049 scopus 로고    scopus 로고
    • β-amyloid protein enhances macrophage production of oxygen free radicals and glutamate
    • Klegeris A., McGeer P.L. β-amyloid protein enhances macrophage production of oxygen free radicals and glutamate. J. Neurosci. Res. 49:1997;229-235.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 229-235
    • Klegeris, A.1    McGeer, P.L.2
  • 23
    • 0029976439 scopus 로고    scopus 로고
    • Neurocytopathic effects of β-amyloid-stimulated monocytes: A potential mechanism for central nervous system damage in Alzheimer disease
    • London J.A., Biegel D., Pachter J.S. Neurocytopathic effects of β-amyloid-stimulated monocytes: a potential mechanism for central nervous system damage in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 93:1996;4147-4152.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4147-4152
    • London, J.A.1    Biegel, D.2    Pachter, J.S.3
  • 24
    • 0030981128 scopus 로고    scopus 로고
    • Beta-amyloid-induced IL-1β release from an activated human monocyte cell line is calcium- And G-protein-dependent
    • Lorton D. Beta-amyloid-induced IL-1β release from an activated human monocyte cell line is calcium- and G-protein-dependent. Mech. Ageing Dev. 94:1997;199-211.
    • (1997) Mech. Ageing Dev. , vol.94 , pp. 199-211
    • Lorton, D.1
  • 25
    • 0030153520 scopus 로고    scopus 로고
    • β-amyloid induces increased release of interleukin-1β from lipopolysaccharide-activated human monocytes
    • Lorton D., Kocsis J.-M., King L., Madden K., Brunden K.R. β-amyloid induces increased release of interleukin-1β from lipopolysaccharide-activated human monocytes. J. Neuroimmunol. 67:1996;21-29.
    • (1996) J. Neuroimmunol. , vol.67 , pp. 21-29
    • Lorton, D.1    Kocsis, J.-M.2    King, L.3    Madden, K.4    Brunden, K.R.5
  • 26
    • 0030961544 scopus 로고    scopus 로고
    • Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia
    • McDonald D.R., Brunden K.R., Landreth G.E. Amyloid fibrils activate tyrosine kinase-dependent signaling and superoxide production in microglia. J. Neurosci. 17:1997;2284-2294.
    • (1997) J. Neurosci. , vol.17 , pp. 2284-2294
    • McDonald, D.R.1    Brunden, K.R.2    Landreth, G.E.3
  • 29
    • 0030210955 scopus 로고    scopus 로고
    • β-amyloid (25-35) peptide and IFN-γ synergistically induce the production of the chemotactic cytokine MCP-1/JE in monocytes and microglial cells
    • Meda L., Bernasconi S., Bonaiuto C., Sozzani S., Zhou D., Otvos L. Jr., Mantovani A., Rossi F., Cassatella M.A. β-amyloid (25-35) peptide and IFN-γ synergistically induce the production of the chemotactic cytokine MCP-1/JE in monocytes and microglial cells. J. Immunol. 157:1996;1213-1218.
    • (1996) J. Immunol. , vol.157 , pp. 1213-1218
    • Meda, L.1    Bernasconi, S.2    Bonaiuto, C.3    Sozzani, S.4    Zhou, D.5    Otvos L., Jr.6    Mantovani, A.7    Rossi, F.8    Cassatella, M.A.9
  • 31
    • 0029086519 scopus 로고
    • Unraveling the neuroimmune mechanisms for the HIV-1 associated cognitive/motor complex
    • Nottet H.S.L.M., Gendelman H.E. Unraveling the neuroimmune mechanisms for the HIV-1 associated cognitive/motor complex. Immunol. Today. 16:1995;441-448.
    • (1995) Immunol. Today , vol.16 , pp. 441-448
    • Nottet, H.S.L.M.1    Gendelman, H.E.2
  • 33
    • 0028930457 scopus 로고
    • A regulatory role for astrocytes in HIV-1 encephalitis: An overexpression of eicosanoids, platelet-activating factor, and tumor necrosis factor-α By activated HIV-1-infected monocytes is attenuated by primary human astrocytes
    • Nottet H.S.L.M., Jett M., Flanagan C.R., Zhai Q.H., Persidsky Y., Rizzino A., Bernton E.W., Genis P., Baldwin T., Schwartz J., LaBenz C., Gendelman H.E. A regulatory role for astrocytes in HIV-1 encephalitis: an overexpression of eicosanoids, platelet-activating factor, and tumor necrosis factor-α by activated HIV-1-infected monocytes is attenuated by primary human astrocytes. J. Immunol. 154:1995;3567-3581.
    • (1995) J. Immunol. , vol.154 , pp. 3567-3581
    • Nottet, H.S.L.M.1    Jett, M.2    Flanagan, C.R.3    Zhai, Q.H.4    Persidsky, Y.5    Rizzino, A.6    Bernton, E.W.7    Genis, P.8    Baldwin, T.9    Schwartz, J.10    Labenz, C.11    Gendelman, H.E.12
  • 34
    • 0031172065 scopus 로고    scopus 로고
    • NF-κB: A crucial transcription factor for glial and neuronal cell function
    • O'Neill L.A.J., Kaltschmidt C. NF-κB: a crucial transcription factor for glial and neuronal cell function. Trends Neurosci. 20:1997;252-258.
    • (1997) Trends Neurosci. , vol.20 , pp. 252-258
    • O'Neill, L.A.J.1    Kaltschmidt, C.2
  • 35
    • 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.N., Maxfield F.R. Microglial cells internalize aggregates of the Alzheimer's disease amyloid-β protein via a scavenger receptor. Neuron. 17:1996;553-565.
    • (1996) Neuron , vol.17 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 37
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid-β protein and the genetics of Alzheimer's disease
    • Selkoe D.J. Amyloid-β protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271:1996;18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 39
    • 0028558519 scopus 로고
    • Human microglia cells have phenotypic and functional characteristics in common with both macrophages and dendritic antigen-presenting cells
    • Ulvestad E., Williams K., Bjerkvig R., Tiekotter K., Antel J., Matre R. Human microglia cells have phenotypic and functional characteristics in common with both macrophages and dendritic antigen-presenting cells. J. Leukocyte Biol. 56:1994;732-740.
    • (1994) J. Leukocyte Biol. , vol.56 , pp. 732-740
    • Ulvestad, E.1    Williams, K.2    Bjerkvig, R.3    Tiekotter, K.4    Antel, J.5    Matre, R.6
  • 40
    • 0030018662 scopus 로고    scopus 로고
    • Do non-steroidal anti-inflammatory drugs (NSAIDs) have a protective effect against dementia?
    • Van Muiswinkel F.L., Eikelenboom P. Do non-steroidal anti-inflammatory drugs (NSAIDs) have a protective effect against dementia? Drugs and Aging. 9:1996;1-7.
    • (1996) Drugs and Aging , vol.9 , pp. 1-7
    • Van Muiswinkel, F.L.1    Eikelenboom, P.2
  • 41
    • 0345165889 scopus 로고    scopus 로고
    • Inflammation and oxidative stress in Alzheimer's disease
    • In: Cacabelos, R., Winblad, B., Eikelenboom, P., (Eds.), Neurogerontology and Neurogeriatrics, Barcelona
    • Van Muiswinkel, F.L., Eikelenboom, P., 1998. Inflammation and oxidative stress in Alzheimer's disease. In: Cacabelos, R., Winblad, B., Eikelenboom, P., (Eds.), Neurogerontology and Neurogeriatrics, Vol. 2. Prous Science, Barcelona, pp. 43-55.
    • (1998) Prous Science , vol.2 , pp. 43-55
    • Van Muiswinkel, F.L.1    Eikelenboom, P.2
  • 42
    • 0029971210 scopus 로고    scopus 로고
    • Amyloid-β protein (Aβ) primes cultured rat microglial cells for an enhanced phorbol-myristate-acetate-induced respiratory burst activity
    • Van Muiswinkel F.L., Veerhuis R., Eikelenboom P. Amyloid-β protein (Aβ) primes cultured rat microglial cells for an enhanced phorbol-myristate-acetate-induced respiratory burst activity. J. Neurochem. 66:1996;2468-2476.
    • (1996) J. Neurochem. , vol.66 , pp. 2468-2476
    • Van Muiswinkel, F.L.1    Veerhuis, R.2    Eikelenboom, P.3
  • 43
    • 0344735682 scopus 로고    scopus 로고
    • Non-fibrillar β-amyloid is capable of priming the respiratory burst activity of rat microglial cells and human monocytes
    • Van Muiswinkel F.L., Azizeh B.Y., Tenner A.J., Cribbs D.H., Cotman C.W. Non-fibrillar β-amyloid is capable of priming the respiratory burst activity of rat microglial cells and human monocytes. Soc. Neurosci. Abstr. 23:1997;6358.
    • (1997) Soc. Neurosci. Abstr. , vol.23 , pp. 6358
    • Van Muiswinkel, F.L.1    Azizeh, B.Y.2    Tenner, A.J.3    Cribbs, D.H.4    Cotman, C.W.5
  • 44
    • 0031031747 scopus 로고    scopus 로고
    • Aspartate residue 7 in amyloid-β protein is critical for classical complement pathway activation: Implications for Alzheimer's disease pathogenesis
    • Velazques P., Cribbs D.H., Poulos T.L., Tenner A.J. Aspartate residue 7 in amyloid-β protein is critical for classical complement pathway activation: implications for Alzheimer's disease pathogenesis. Nat. Med. 3:1997;77-79.
    • (1997) Nat. Med. , vol.3 , pp. 77-79
    • Velazques, P.1    Cribbs, D.H.2    Poulos, T.L.3    Tenner, A.J.4
  • 45
    • 0031576547 scopus 로고    scopus 로고
    • Modulation of nitric oxide production in human macrophages by apolipoprotein-E and amyloid-beta peptide
    • Vitek M.P., Snell J., Dawson H., Colton C.A. Modulation of nitric oxide production in human macrophages by apolipoprotein-E and amyloid-beta peptide. Biochem. Biophys. Res. Commun. 240:1997;391-394.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 391-394
    • Vitek, M.P.1    Snell, J.2    Dawson, H.3    Colton, C.A.4
  • 46
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid-β peptide
    • Yan S.D., Yan S.F., Chen X., Fu J., Chen M., Kuppusamy P., Smith M.A., Perry G., Godman G.C., Nawroth P., Zweier J.L., Stern D. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid-β peptide. Nat. Med. 7:1995;693-699.
    • (1995) Nat. Med. , vol.7 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10    Zweier, J.L.11    Stern, D.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.