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Volumn 27, Issue 1, 2005, Pages 1-12

β-amyloid protein structure determines the nature of cytokine release from rat microglia

Author keywords

Alzheimer's disease; ELISA; Inflammatory; Interferon ; Interleukin 1; Receptor antagonist

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; CYTOKINE; GAMMA INTERFERON; INTERLEUKIN 1 RECEPTOR BLOCKING AGENT; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 6; MONOMER; OLIGOMER; PEPTIDE; TUMOR NECROSIS FACTOR ALPHA;

EID: 23444455475     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/JMN:27:01:01     Document Type: Article
Times cited : (70)

References (77)
  • 2
    • 0037638809 scopus 로고    scopus 로고
    • Alzheimer's disease cooperative study. Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: A randomized controlled trial
    • Aisen P. S., Schafer K. A., Grundman M., Pfeiffer E., Sano M., Davis K. L., et al. (2003) Alzheimer's disease cooperative study. Effects of rofecoxib or naproxen vs placebo on Alzheimer disease progression: a randomized controlled trial. JAMA 289, 2819-2826.
    • (2003) JAMA , vol.289 , pp. 2819-2826
    • Aisen, P.S.1    Schafer, K.A.2    Grundman, M.3    Pfeiffer, E.4    Sano, M.5    Davis, K.L.6
  • 3
    • 0029661902 scopus 로고    scopus 로고
    • α-1-Antichymotrypsin interaction with Aβ (1-40) inhibits fibril formation but does not affect the peptide toxicity
    • Aksenova M. V., Aksenov M. Y., Butterfield D. A., and Carney J. M. (1996) α-1-Antichymotrypsin interaction with Aβ (1-40) inhibits fibril formation but does not affect the peptide toxicity. Neurosci. Lett. 211, 45-48.
    • (1996) Neurosci. Lett. , vol.211 , pp. 45-48
    • Aksenova, M.V.1    Aksenov, M.Y.2    Butterfield, D.A.3    Carney, J.M.4
  • 4
    • 0026602079 scopus 로고
    • β-Amyloid stimulates glial cells in vitro to produce growth factors that accumulate in senile plaques in Alzheimer's disease
    • Araujo D. M. and Cotman C. W. (1992) β-Amyloid stimulates glial cells in vitro to produce growth factors that accumulate in senile plaques in Alzheimer's disease. Brain Res. 569, 141-145.
    • (1992) Brain Res. , vol.569 , pp. 141-145
    • Araujo, D.M.1    Cotman, C.W.2
  • 5
    • 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., and Fratkin J. D. (1996) Scavenging of Alzheimer's amyloid β-protein by microglia in culture. J. Neurosci. Res. 43, 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
  • 6
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F., Cannon C., Barbour R., et al. (2000) Peripherally administered antibodies against amyloid β-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    Cannon, C.2    Barbour, R.3
  • 7
    • 0025763298 scopus 로고
    • Interleukin-6 and α-2-macroglobulin indicate an acute-phase state in Alzheimer's disease cortices
    • Bauer J., Strauss S., Schreiter-Gasser U., Ganter U., Schlegel P., Witt I., et al. (1991) Interleukin-6 and α-2-macroglobulin indicate an acute-phase state in Alzheimer's disease cortices. FEBS Lett. 285, 111-114.
    • (1991) FEBS Lett. , vol.285 , pp. 111-114
    • Bauer, J.1    Strauss, S.2    Schreiter-Gasser, U.3    Ganter, U.4    Schlegel, P.5    Witt, I.6
  • 8
    • 0034802570 scopus 로고    scopus 로고
    • Immunological aspects of microglia: Relevance to Alzheimer's disease
    • Benveniste E. N., Nguyen V. T., and O'Keefe G. M. (2001) Immunological aspects of microglia: relevance to Alzheimer's disease. Neurochem. Int. 39, 381-391.
    • (2001) Neurochem. Int. , vol.39 , pp. 381-391
    • Benveniste, E.N.1    Nguyen, V.T.2    O'Keefe, G.M.3
  • 9
    • 2942672221 scopus 로고    scopus 로고
    • Rapid photochemical crosslinking - A new tool for studies of metastable, amyloidogenic protein assemblies
    • Bitan G. and Teplow D. B. (2004) Rapid photochemical crosslinking - a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 37, 357-364.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 11
    • 0029417080 scopus 로고
    • Interleukin-1 β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimer's and de novo Parkinson's disease patients
    • Blum-Degen D., Muller T., Kuhn W., Gerlach M., Przuntek H., and Riederer P. (1995) Interleukin-1 β and interleukin-6 are elevated in the cerebrospinal fluid of Alzheimer's and de novo Parkinson's disease patients. Neurosci. Lett. 202, 17-20.
    • (1995) Neurosci. Lett. , vol.202 , pp. 17-20
    • Blum-Degen, D.1    Muller, T.2    Kuhn, W.3    Gerlach, M.4    Przuntek, H.5    Riederer, P.6
  • 13
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
    • Cleary, J. P., Walsh D. M., Hofmeister J. J., et al. (2005) Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nature Neurosci. 8, 79-84.
    • (2005) Nature Neurosci. , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 14
    • 0035866060 scopus 로고    scopus 로고
    • β-Amyloid stimulation of microglia and monocytes results in TNFα-dependent expression of inducible nitric oxide synthase and neuronal apoptosis
    • Combs C. K., Karlo J. C., Kao S. C., and Landreth G. E. (2001) β-Amyloid stimulation of microglia and monocytes results in TNFα-dependent expression of inducible nitric oxide synthase and neuronal apoptosis. J. Neurosci. 21, 1179-1188.
    • (2001) J. Neurosci. , vol.21 , pp. 1179-1188
    • Combs, C.K.1    Karlo, J.C.2    Kao, S.C.3    Landreth, G.E.4
  • 15
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
    • Dahlgren K. N., Manelli A. M., Stine W. B. Jr., Baker L. K., Krafft G. A., and LaDu M. J. (2002) Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. J. Biol. Chem. 277, 32046-32053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine Jr., W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 16
    • 0028946146 scopus 로고
    • Reciprocal control of inflammatory cytokines, IL-1 and IL-6, and β-amyloid production in cultures
    • Del Bo R., Angeretti N., Lucca E., De Simoni M. G., and Forloni G. (1995) Reciprocal control of inflammatory cytokines, IL-1 and IL-6, and β-amyloid production in cultures. Neurosci. Lett. 188, 70-74.
    • (1995) Neurosci. Lett. , vol.188 , pp. 70-74
    • Del Bo, R.1    Angeretti, N.2    Lucca, E.3    De Simoni, M.G.4    Forloni, G.5
  • 17
    • 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. H., and Brosnan C. (1993) Microglia and cytokines in neurological disease, with special reference to AIDS and Alzheimer's disease. Glia 7, 75-83.
    • (1993) Glia , vol.7 , pp. 75-83
    • Dickson, D.W.1    Lee, S.C.2    Mattiace, L.A.3    Yen, S.H.4    Brosnan, C.5
  • 19
    • 0032981238 scopus 로고    scopus 로고
    • Unchanged levels of interleukins, neopterin, interferon-γ and tumor necrosis factor-α in cerebrospinal fluid of patients with dementia of the Alzheimer type
    • Engelborghs S., De Brabander M., De Cree J., D'Hooge R., Geerts H., Verhaegen H., and De Deyn P. P. (1999) Unchanged levels of interleukins, neopterin, interferon-γ and tumor necrosis factor-α in cerebrospinal fluid of patients with dementia of the Alzheimer type. Neurochem. Int. 34, 523-530.
    • (1999) Neurochem. Int. , vol.34 , pp. 523-530
    • Engelborghs, S.1    De Brabander, M.2    De Cree, J.3    D'Hooge, R.4    Geerts, H.5    Verhaegen, H.6    De Deyn, P.P.7
  • 20
    • 0032805573 scopus 로고    scopus 로고
    • Immunohistochemical localization of interleukin-1β, interleukin-1 receptor antagonist and interleukin-1β converting enzyme/caspase-1 in the rat brain after peripheral administration of kainic acid
    • Eriksson C., Van Dam A.-M., Lucassen P. J., Bol J. G. J., Winblad B., and Schultzberg M. (1999) Immunohistochemical localization of interleukin-1β, interleukin-1 receptor antagonist and interleukin-1β converting enzyme/caspase-1 in the rat brain after peripheral administration of kainic acid. Neuroscience 93, 915-930.
    • (1999) Neuroscience , vol.93 , pp. 915-930
    • Eriksson, C.1    Van Dam, A.-M.2    Lucassen, P.J.3    Bol, J.G.J.4    Winblad, B.5    Schultzberg, M.6
  • 21
    • 0033119725 scopus 로고    scopus 로고
    • Propentofylline protects neurons in culture from death triggered by macrophage or microglial secretory products
    • Flavin M. P. and Ho L. T. (1999) Propentofylline protects neurons in culture from death triggered by macrophage or microglial secretory products. J. Neurosci. Res. 56, 54-59.
    • (1999) J. Neurosci. Res. , vol.56 , pp. 54-59
    • Flavin, M.P.1    Ho, L.T.2
  • 22
    • 0026452028 scopus 로고
    • Expression of amyloid precursor protein mRNAs in endothelial, neuronal and glial cells: Modulation by interleukin-1
    • Forloni G., Demicheli F., Giorgi S., Bendotti C. and Angeretti N. (1992) Expression of amyloid precursor protein mRNAs in endothelial, neuronal and glial cells: modulation by interleukin-1. Mol. Brain Res. 16, 128-134.
    • (1992) Mol. Brain Res. , vol.16 , pp. 128-134
    • Forloni, G.1    Demicheli, F.2    Giorgi, S.3    Bendotti, C.4    Angeretti, N.5
  • 23
    • 0029923520 scopus 로고    scopus 로고
    • Association of Aβ 40-positive senile plaques with microglial cells in the brains of patients with Alzheimer's disease and in non-demented aged individuals
    • Fukumoto H., Asami-Odaka A., Suzuki N., and Iwatsubo T. (1996) Association of Aβ 40-positive senile plaques with microglial cells in the brains of patients with Alzheimer's disease and in non-demented aged individuals. Neurodegeneration 5, 13-17.
    • (1996) Neurodegeneration , vol.5 , pp. 13-17
    • Fukumoto, H.1    Asami-Odaka, A.2    Suzuki, N.3    Iwatsubo, T.4
  • 24
    • 0028832354 scopus 로고
    • Amyloid β peptide potentiates cytokine secretion by interleukin-1 β-activated human astrocytoma cells
    • Gitter B. D., Cox L. M., Rydel R. E., and May P. C. (1995) Amyloid β peptide potentiates cytokine secretion by interleukin-1 β-activated human astrocytoma cells. Proc. Natl. Acad. Sci. U. S. A. 92, 10738-10741.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10738-10741
    • Gitter, B.D.1    Cox, L.M.2    Rydel, R.E.3    May, P.C.4
  • 25
    • 0029811105 scopus 로고    scopus 로고
    • Specific domains of β-amyloid from Alzheimer plaque elicit neuron killing in human microglia
    • Giulian D., Haverkamp L. J., Yu J. H., Karshin W., Tom D., Li J., et al. (1996) Specific domains of β-amyloid from Alzheimer plaque elicit neuron killing in human microglia. J. Neurosci. 16, 6021-6037.
    • (1996) J. Neurosci. , vol.16 , pp. 6021-6037
    • Giulian, D.1    Haverkamp, L.J.2    Yu, J.H.3    Karshin, W.4    Tom, D.5    Li, J.6
  • 26
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y., Chang L., Viola K. L., Lacor P. N., Lambert M. P., Finch C. E., et al. (2003) Alzheimer's disease-affected brain: presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U. S. A. 100, 10417-10422.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 27
    • 0028926976 scopus 로고
    • Interleukin-1 expression in different plaque types in Alzheimer's disease: Significance in plaque evolution
    • Griffin W. S., Sheng J. G., Roberts G. W., and Mrak R. E. (1995) Interleukin-1 expression in different plaque types in Alzheimer's disease: significance in plaque evolution. J. Neuropathol. Exp. Neurol. 54, 276-281.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 276-281
    • Griffin, W.S.1    Sheng, J.G.2    Roberts, G.W.3    Mrak, R.E.4
  • 29
    • 17644439518 scopus 로고    scopus 로고
    • Interleukin-6 is not altered in cerebrospinal fluid of first-degree relatives and patients with Alzheimer's disease
    • Hampel H., Schoen D., Schwarz M. J., et al. (1997) Interleukin-6 is not altered in cerebrospinal fluid of first-degree relatives and patients with Alzheimer's disease. Neurosci. Lett. 228, 143-146.
    • (1997) Neurosci. Lett. , vol.228 , pp. 143-146
    • Hampel, H.1    Schoen, D.2    Schwarz, M.J.3
  • 30
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper J. D., Wong S. S., Lieber C. M., and Lansbury P. T. (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 31
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D. M., Walsh D. M., Ye C. P., Diehl T., Vasquez S., Vassilev P. M., et al. (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884.
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6
  • 32
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M., Sato M., Matsumoto S., Noguchi A., Yasutake K., Yoshida N., and Sato K. (2003) Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. Proc. Natl. Acad. Sci. U. S. A. 100, 6370-6375.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 33
    • 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. A., Chromy B. A., and Van Eldik L. J. (1998) Amyloid-β peptide activates cultured astrocytes: morphological alterations, cytokine induction and nitric oxide release. Brain Res. 785, 195-206.
    • (1998) Brain Res. , vol.785 , pp. 195-206
    • Hu, J.1    Akama, K.T.2    Krafft, G.A.3    Chromy, B.A.4    Van Eldik, L.J.5
  • 34
    • 1842510004 scopus 로고    scopus 로고
    • Early Aβ accumulation and progressive synaptic loss, gliosis, and tangle formation in AD brain
    • Ingelsson M., Fukumoto H., Newell K. L., Growdon J. H., Hedley-Whyte E. T., Frosch M. P., et al. (2004) Early Aβ accumulation and progressive synaptic loss, gliosis, and tangle formation in AD brain. Neurology 62, 925-931.
    • (2004) Neurology , vol.62 , pp. 925-931
    • Ingelsson, M.1    Fukumoto, H.2    Newell, K.L.3    Growdon, J.H.4    Hedley-Whyte, E.T.5    Frosch, M.P.6
  • 35
    • 0034024589 scopus 로고    scopus 로고
    • A possible model of senile plaques using synthetic amyloid β-protein and rat glial culture
    • Isobe I., Yanagisawa K., and Michikawa M. (2000) A possible model of senile plaques using synthetic amyloid β-protein and rat glial culture. Exp. Neurol. 162, 51-60.
    • (2000) Exp. Neurol. , vol.162 , pp. 51-60
    • Isobe, I.1    Yanagisawa, K.2    Michikawa, M.3
  • 36
    • 0028169925 scopus 로고
    • Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., and Ihara Y. (1994) Visualization of Aβ 42(43) and Aβ 40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ 42(43). Neuron 13, 45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 37
    • 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
    • Jarrett J. T., Berger E. P., and Lansbury P. T. Jr. (1993) The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 38
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R., Head E., Thompson J. L., McIntire T. M., Milton S. C., Cotman C. W., and Glabe C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 41
    • 0032406078 scopus 로고    scopus 로고
    • Longitudinal study of inflammatory factors in serum, cerebrospinal fluid, and brain tissue in Alzheimer disease: Interleukin-1β, interleukin-6, interleukin-1 receptor antagonist, tumor necrosis factor-α, the soluble tumor necrosis factor receptors I and II, and α1-antichymotrypsin
    • Lanzrein A. S., Johnston C. M., Perry V. H., Jobst K. A., King E. M., and Smith A. D. (1998) Longitudinal study of inflammatory factors in serum, cerebrospinal fluid, and brain tissue in Alzheimer disease: interleukin-1β, interleukin-6, interleukin-1 receptor antagonist, tumor necrosis factor-α, the soluble tumor necrosis factor receptors I and II, and α1-antichymotrypsin. Alzheimer Dis. Assoc. Disord. 12, 215-227.
    • (1998) Alzheimer Dis. Assoc. Disord. , vol.12 , pp. 215-227
    • Lanzrein, A.S.1    Johnston, C.M.2    Perry, V.H.3    Jobst, K.A.4    King, E.M.5    Smith, A.D.6
  • 42
    • 0036644961 scopus 로고    scopus 로고
    • Cytokines, chemokines, and cytokine receptors in human microglia
    • Lee Y. B., Nagai A., and Kim S. U. (2002) Cytokines, chemokines, and cytokine receptors in human microglia. J. Neurosci. Res. 69, 94-103.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 94-103
    • Lee, Y.B.1    Nagai, A.2    Kim, S.U.3
  • 43
    • 0028832472 scopus 로고
    • Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution
    • Levine H. III. (1995) Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution. Neurobiol. Aging 16, 755-764.
    • (1995) Neurobiol. Aging , vol.16 , pp. 755-764
    • Levine III, H.1
  • 45
    • 33644582250 scopus 로고    scopus 로고
    • β-Amyloid-stimulated release of pro- and anti-inflammatory cytokines from rat microglia: Differential response to soluble and aggregated forms
    • New Orleans, LA
    • Lindberg C., Westlind-Danielsson A., and Schultzberg M. (2003) β-Amyloid-stimulated release of pro- and anti-inflammatory cytokines from rat microglia: differential response to soluble and aggregated forms, in The Society for Neuroscience 33rd Annual Meeting, New Orleans, LA.
    • (2003) The Society for Neuroscience 33rd Annual Meeting
    • Lindberg, C.1    Westlind-Danielsson, A.2    Schultzberg, M.3
  • 46
    • 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., and Brunden K. R. (1996) β-Amyloid induces increased release of interleukin-1β from lipopolysaccharide-activated human monocytes. J. Neuroimmunol. 67, 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
  • 47
    • 0028863201 scopus 로고
    • Microglial cells and amyloid β protein (Aβ) deposition; association with A β 40-containing plaques
    • Mann D. M., Iwatsubo T., Fukumoto H., Ihara Y., Odaka A., and Suzuki N. (1995) Microglial cells and amyloid β protein (Aβ) deposition; association with A β 40-containing plaques. Acta Neuropathol. 90, 472-477.
    • (1995) Acta Neuropathol. , vol.90 , pp. 472-477
    • Mann, D.M.1    Iwatsubo, T.2    Fukumoto, H.3    Ihara, Y.4    Odaka, A.5    Suzuki, N.6
  • 48
    • 0343569927 scopus 로고    scopus 로고
    • Increased cerebrospinal fluid fas (Apo-1) levels in Alzheimer's disease. Relationship with IL-6 concentrations
    • Martinez M., Fernandez-Vivancos E., Frank A., De la Fuente M., and Hernanz A. (2000) Increased cerebrospinal fluid fas (Apo-1) levels in Alzheimer's disease. Relationship with IL-6 concentrations. Brain Res. 869, 216-219.
    • (2000) Brain Res. , vol.869 , pp. 216-219
    • Martinez, M.1    Fernandez-Vivancos, E.2    Frank, A.3    De La Fuente, M.4    Hernanz, A.5
  • 49
    • 0027478347 scopus 로고
    • Evidence for excito-protective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
    • Mattson M. P., Cheng B., Culwell A. R., Esch F. S., Lieberburg I., and Rydel R. E. (1993) Evidence for excito-protective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein. Neuron 10, 243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 51
    • 0025332027 scopus 로고
    • Anti-inflammatory drugs and Alzheimer disease
    • McGeer P. L., McGeer E., Rogers J., and Sibley J. (1990) Anti-inflammatory drugs and Alzheimer disease. Lancet 335, 1037.
    • (1990) Lancet , vol.335 , pp. 1037
    • McGeer, P.L.1    McGeer, E.2    Rogers, J.3    Sibley, J.4
  • 53
    • 3542996239 scopus 로고    scopus 로고
    • Macrophage colony-stimulating factor augments γ-amyloid-induced interleukin-1, interleukin-6, and nitric oxide production by microglial cells
    • Murphy G. M. Jr., Yang L., and Cordell B. (1998) Macrophage colony-stimulating factor augments γ-amyloid-induced interleukin-1, interleukin-6, and nitric oxide production by microglial cells. J. Biol. Chem. 273, 20967-20971.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20967-20971
    • Murphy Jr., G.M.1    Yang, L.2    Cordell, B.3
  • 54
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Näslund J., Haroutunian V., Mohs R., Davis K. L., Davies P., Greengard P., and Buxbaum J. D. (2000) Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283, 1571-1577.
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Näslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 55
    • 0034612175 scopus 로고    scopus 로고
    • Inflammation and Alzheimer's disease
    • Neuroinflammation Working Group, Akiyama H., Barger S., et al. (2000) Inflammation and Alzheimer's disease. Neurobiol. Aging 21, 383-421.
    • (2000) Neurobiol. Aging , vol.21 , pp. 383-421
    • Akiyama, H.1    Barger, S.2
  • 56
    • 0037205434 scopus 로고    scopus 로고
    • Oxidation of methionine 35 attenuates formation of amyloid β-peptide 1-40 oligomers
    • Palmblad M., Westlind-Danielsson A., and Bergquist J. (2002) Oxidation of methionine 35 attenuates formation of amyloid β-peptide 1-40 oligomers. J. Biol. Chem. 277, 19506-19510.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19506-19510
    • Palmblad, M.1    Westlind-Danielsson, A.2    Bergquist, J.3
  • 57
    • 2342652177 scopus 로고    scopus 로고
    • Unique physicochemical profile of β-amyloid peptide variant Aβ1-40E22G protofibrils: Conceivable neuropathogen in arctic mutant carriers
    • Päiviö A., Jarvet J., Gräslund A., Lannfelt L., and Westlind-Danielsson A. (2004) Unique physicochemical profile of β-amyloid peptide variant Aβ1-40E22G protofibrils: conceivable neuropathogen in arctic mutant carriers. J. Mol. Biol. 339, 145-159.
    • (2004) J. Mol. Biol. , vol.339 , pp. 145-159
    • Päiviö, A.1    Jarvet, J.2    Gräslund, A.3    Lannfelt, L.4    Westlind-Danielsson, A.5
  • 58
    • 0027332081 scopus 로고
    • β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher A. E., Lowenson J. D., Clarke S., Woods A. S., Cotter R. J., Gowing E., and Ball M. J. (1993) β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 90, 10836-10840.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 59
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D., Eckman C., Jensen M., et al. (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870.
    • (1996) Nat. Med. , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 61
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe D. J. (1994) Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10, 373-403.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 62
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease
    • Selkoe D. J. (2002) Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease. J. Clin. Invest. 110, 1375-1381.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1375-1381
    • Selkoe, D.J.1
  • 63
    • 0030775197 scopus 로고    scopus 로고
    • Circulating cytokines in Alzheimer's disease
    • Singh V. K. and Guthikonda P. (1997) Circulating cytokines in Alzheimer's disease. J. Psychiatr. Res. 31, 657-660.
    • (1997) J. Psychiatr. Res. , vol.31 , pp. 657-660
    • Singh, V.K.1    Guthikonda, P.2
  • 65
    • 0033664955 scopus 로고    scopus 로고
    • Overproduction of IFN-γ and TNF-α from natural killer (NK) cells is associated with abnormal NK reactivity and cognitive derangement in Alzheimer's disease
    • Solerte S. B., Cravello L., Ferrari E., and Fioravanti M. (2000) Overproduction of IFN-γ and TNF-α from natural killer (NK) cells is associated with abnormal NK reactivity and cognitive derangement in Alzheimer's disease. Ann. N. Y. Acad. Sci. 917, 331-340.
    • (2000) Ann. N. Y. Acad. Sci. , vol.917 , pp. 331-340
    • Solerte, S.B.1    Cravello, L.2    Ferrari, E.3    Fioravanti, M.4
  • 66
    • 0035085610 scopus 로고    scopus 로고
    • Amyloid-β peptide fragments p3 and p4 induce proinflammatory cytokine and chemokine production in vitro and in vivo
    • Szczepanik A. M., Rampe D., and Ringheim G. E. (2001) Amyloid-β peptide fragments p3 and p4 induce proinflammatory cytokine and chemokine production in vitro and in vivo. J. Neurochem. 77, 304-317.
    • (2001) J. Neurochem. , vol.77 , pp. 304-317
    • Szczepanik, A.M.1    Rampe, D.2    Ringheim, G.E.3
  • 69
    • 0032868874 scopus 로고    scopus 로고
    • Intracerebral production of tumor necrosis factor-α, a local neuroprotective agent, in Alzheimer disease and vascular dementia
    • Tarkowski E., Blennow K., Wallin A., and Tarkowski A. (1999) Intracerebral production of tumor necrosis factor-α, a local neuroprotective agent, in Alzheimer disease and vascular dementia. J. Clin. Immunol. 19, 223-230.
    • (1999) J. Clin. Immunol. , vol.19 , pp. 223-230
    • Tarkowski, E.1    Blennow, K.2    Wallin, A.3    Tarkowski, A.4
  • 71
    • 0025801468 scopus 로고
    • Is amyloidogenesis during Alzheimer's disease due to an IL-1-/IL-6-mediated 'acute phase response' in the brain?
    • Vandenabeele P. and Fiers W. (1991) Is amyloidogenesis during Alzheimer's disease due to an IL-1-/IL-6-mediated 'acute phase response' in the brain? Immunol. Today 12, 217-219.
    • (1991) Immunol. Today , vol.12 , pp. 217-219
    • Vandenabeele, P.1    Fiers, W.2
  • 72
    • 0037333633 scopus 로고    scopus 로고
    • Immune reactive cells in senile plaques and cognitive decline in Alzheimer's disease
    • Vehmas A. K., Kawas C. H., Stewart W. F., and Troncoso J. C. (2003) Immune reactive cells in senile plaques and cognitive decline in Alzheimer's disease. Neurobiol. Aging 24, 321-331.
    • (2003) Neurobiol. Aging , vol.24 , pp. 321-331
    • Vehmas, A.K.1    Kawas, C.H.2    Stewart, W.F.3    Troncoso, J.C.4
  • 73
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., and Schenk D. B. (1993) Characterization of β-amyloid peptide from human cerebrospinal fluid. J. Neurochem. 61, 1965-1968.
    • (1993) J. Neurochem. , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 74
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh D. M., Lomakin A., Benedek G. B., Condron M. M., and Teplow D. B. (1997) Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272, 22364-22372.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 75
    • 33644564514 scopus 로고    scopus 로고
    • Natural, cell-derived Aβ oligomers: Their production, biological activity and inhibition
    • Walsh D. M., Kylubin I., Cleary J. P., et al. (2004) Natural, cell-derived Aβ oligomers: their production, biological activity and inhibition. Neurobiol. Aging 25, 161.
    • (2004) Neurobiol. Aging , vol.25 , pp. 161
    • Walsh, D.M.1    Kylubin, I.2    Cleary, J.P.3
  • 76
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of β- amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang H.W., Pasternak J.F., Kuo H., Ristic H., Lambert M.P., Chromy B., et al. (2002) Soluble oligomers of β- amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res. 924, 133-140.
    • (2002) Brain Res. , vol.924 , pp. 133-140
    • Wang, H.W.1    Pasternak, J.F.2    Kuo, H.3    Ristic, H.4    Lambert, M.P.5    Chromy, B.6
  • 77
    • 0035846576 scopus 로고    scopus 로고
    • Spontaneous in vitro formation of supramolecular β-amyloid structures, "βamy ballsβ, by β-amyloid 1-40 peptide
    • Westlind-Danielsson A. and Arnerup G. (2001) Spontaneous in vitro formation of supramolecular β-amyloid structures, "βamy ballsβ, by β-amyloid 1-40 peptide. Biochemistry 40, 14736-14743.
    • (2001) Biochemistry , vol.40 , pp. 14736-14743
    • Westlind-Danielsson, A.1    Arnerup, G.2


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