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Volumn 43, Issue 3, 2003, Pages 251-261

Effect of β-amyloid on endothelial cells: Lack of direct toxicity, enhancement of MTT-induced cell death and intracellular accumulation

Author keywords

Alzheimer's disease; Endothelial cell lines; Toxicity; Vascular deposits; Amyloid

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; ADENOSINE TRIPHOSPHATASE; AMYLOID BETA PROTEIN; BAFILOMYCIN A1; FORMAZAN; LACTATE DEHYDROGENASE; NEUTRAL RED;

EID: 0037411846     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(03)00008-1     Document Type: Article
Times cited : (22)

References (56)
  • 1
    • 0033614679 scopus 로고    scopus 로고
    • Both oxidative stress-dependent and independent effects of amyloid β protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2,5diphenyltetrazolium bromide (MTT) reduction assay
    • Abe K., Saito H. Both oxidative stress-dependent and independent effects of amyloid β protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2,5diphenyltetrazolium bromide (MTT) reduction assay. Brain Res. 830:1999;146-154.
    • (1999) Brain Res. , vol.830 , pp. 146-154
    • Abe, K.1    Saito, H.2
  • 2
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 3
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2, diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence, and involvement of mithocondrial electron transport in MTT reduction
    • Berridge M.V., Tan A.S. Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2, diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mithocondrial electron transport in MTT reduction. Arch. Biochem. Biophys. 303:1993;474-482.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 4
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: Evidence for AβP channel-mediated cellular toxicity
    • Bhatia R., Lin H., Ratneshwar L. Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: evidence for AβP channel-mediated cellular toxicity. FASEB J. 14:2000;1233-1242.
    • (2000) FASEB J. , vol.14 , pp. 1233-1242
    • Bhatia, R.1    Lin, H.2    Ratneshwar, L.3
  • 5
    • 0031004788 scopus 로고    scopus 로고
    • Amyloid-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells
    • Blanc E.M., Toborek M., Mark R.J., Bernhard H., Mattson M.P. Amyloid-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells. J. Neurochem. 68:1997;1870-1881.
    • (1997) J. Neurochem. , vol.68 , pp. 1870-1881
    • Blanc, E.M.1    Toborek, M.2    Mark, R.J.3    Bernhard, H.4    Mattson, M.P.5
  • 6
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide Aβ1-42 in differentiated PC12 cells
    • Burdick D., Kosmoski J., Knauer M.F., Glabe C.G. Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide Aβ1-42 in differentiated PC12 cells. Brain Res. 746:1997;275-284.
    • (1997) Brain Res. , vol.746 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 7
    • 0026055091 scopus 로고
    • Murine endothelioma cell lines transformed by polyoma middle T oncogene as target for and producers of cytokines
    • Bussolino F., Rossi M., Sica A., Colotta F., Wang J.M., Bocchietto E.et al. Murine endothelioma cell lines transformed by polyoma middle T oncogene as target for and producers of cytokines. J. Immunol. 147:1991;2122-2129.
    • (1991) J. Immunol. , vol.147 , pp. 2122-2129
    • Bussolino, F.1    Rossi, M.2    Sica, A.3    Colotta, F.4    Wang, J.M.5    Bocchietto, E.6
  • 8
    • 0030071207 scopus 로고    scopus 로고
    • Oxidative stress after acute and chronic application of β amyloid fragment 25-35 in cortical cultures
    • Café C., Torri C., Bertorelli L., Angeretti N., Lucca E., Forloni G.et al. Oxidative stress after acute and chronic application of β amyloid fragment 25-35 in cortical cultures. Neurosci. Lett. 203:1996;1-5.
    • (1996) Neurosci. Lett. , vol.203 , pp. 1-5
    • Café, C.1    Torri, C.2    Bertorelli, L.3    Angeretti, N.4    Lucca, E.5    Forloni, G.6
  • 9
    • 0034683225 scopus 로고    scopus 로고
    • Potassium channel openers prevent β-amyloid toxicity in bovine vascular endothelial cells
    • Chi X., Sutton E.T., Hellermann G., Price J.M. Potassium channel openers prevent β-amyloid toxicity in bovine vascular endothelial cells. Neurosci. Lett. 290:2000;9-12.
    • (2000) Neurosci. Lett. , vol.290 , pp. 9-12
    • Chi, X.1    Sutton, E.T.2    Hellermann, G.3    Price, J.M.4
  • 10
    • 0036218738 scopus 로고    scopus 로고
    • Alzheimer disease as a vascular disorder
    • de la Torre J.C. Alzheimer disease as a vascular disorder. Stroke. 33:2002;1152-1162.
    • (2002) Stroke , vol.33 , pp. 1152-1162
    • De la Torre, J.C.1
  • 11
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid-β efflux: A measure of brain amyloid burden in a mouse model of Alzheimer's disease
    • DeMattos R.B., Bales K.R., Cummins D.J., Paul S.M., Holtzman D.M. Brain to plasma amyloid-β efflux: a measure of brain amyloid burden in a mouse model of Alzheimer's disease. Science. 295:2002;2264-2267.
    • (2002) Science , vol.295 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Paul, S.M.4    Holtzman, D.M.5
  • 12
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Drose S., Altendorf K. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J. Exp. Biol. 200:1997;1-8.
    • (1997) J. Exp. Biol. , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 13
    • 0035047718 scopus 로고    scopus 로고
    • Cerebral microvascular pathology in aging and Alzheimer's disease
    • Farkas E., Luiten P.G.M. Cerebral microvascular pathology in aging and Alzheimer's disease. Prog. Neurobiol. 64:2001;575-611.
    • (2001) Prog. Neurobiol. , vol.64 , pp. 575-611
    • Farkas, E.1    Luiten, P.G.M.2
  • 14
    • 0027191973 scopus 로고
    • Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35
    • Forloni G., Chiesa R., Smiroldo S., Salmona M., Tagliavini F., Angeretti N. Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35. NeuroReport. 4:1993;523-526.
    • (1993) NeuroReport , vol.4 , pp. 523-526
    • Forloni, G.1    Chiesa, R.2    Smiroldo, S.3    Salmona, M.4    Tagliavini, F.5    Angeretti, N.6
  • 15
    • 0030779130 scopus 로고    scopus 로고
    • Amidation of β-amyloid peptide strongly reduced the amyloidogenic activity without alteration of the neurotoxicity
    • Forloni G., Lucca E., Angeretti N., Della Torre P., Salmona M. Amidation of β-amyloid peptide strongly reduced the amyloidogenic activity without alteration of the neurotoxicity. J. Neurochem. 69:1997;2048-2054.
    • (1997) J. Neurochem. , vol.69 , pp. 2048-2054
    • Forloni, G.1    Lucca, E.2    Angeretti, N.3    Della Torre, P.4    Salmona, M.5
  • 16
    • 0028239057 scopus 로고
    • Progressive growth in immunodeficient mice and host cell recruitment by mouse endothelial cells transformed by polyoma middle-sized T antigen: Implications for the pathogenesis of opportunistic vascular tumors
    • Garlanda C., Parravicini C., Sironi M., De Rossi M., Wainstok de Calmanovici R., Carozzi F.et al. Progressive growth in immunodeficient mice and host cell recruitment by mouse endothelial cells transformed by polyoma middle-sized T antigen: implications for the pathogenesis of opportunistic vascular tumors. Proc. Natl. Acad. Sci. U.S.A. 91:1994;7291-7295.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7291-7295
    • Garlanda, C.1    Parravicini, C.2    Sironi, M.3    De Rossi, M.4    Wainstok de Calmanovici, R.5    Carozzi, F.6
  • 17
    • 0029902540 scopus 로고    scopus 로고
    • β-Amyloid-induced cell toxicity: Enhancement of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide-dependent cell death
    • Hertel C., Hauser N., Schubenel R., Seilhheimer B., Kemp J.A. β-Amyloid-induced cell toxicity: enhancement of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide-dependent cell death. J. Neurochem. 67:1996;272-276.
    • (1996) J. Neurochem. , vol.67 , pp. 272-276
    • Hertel, C.1    Hauser, N.2    Schubenel, R.3    Seilhheimer, B.4    Kemp, J.A.5
  • 18
    • 0033363939 scopus 로고    scopus 로고
    • SOD1 rescues cerebral endothelial dysfunction in mice overexpressing amyloid precursor protein
    • Iadacola C., Zhang F., Niwa K., Eckman C., Turner S.K., Fischer E.et al. SOD1 rescues cerebral endothelial dysfunction in mice overexpressing amyloid precursor protein. Nat. Neurosci. 2:1999;157-161.
    • (1999) Nat. Neurosci. , vol.2 , pp. 157-161
    • Iadacola, C.1    Zhang, F.2    Niwa, K.3    Eckman, C.4    Turner, S.K.5    Fischer, E.6
  • 20
    • 0033532236 scopus 로고    scopus 로고
    • Enhancement of MTT, a tetrazolium salt, exocytosis by amyloid β-protein and chloroquine in cultured rat astrocytes
    • Isobe I., Michikawa M., Yanigisawa K. Enhancement of MTT, a tetrazolium salt, exocytosis by amyloid β-protein and chloroquine in cultured rat astrocytes. Neurosci. Lett. 266:1999;129-132.
    • (1999) Neurosci. Lett. , vol.266 , pp. 129-132
    • Isobe, I.1    Michikawa, M.2    Yanigisawa, K.3
  • 21
    • 85030294214 scopus 로고    scopus 로고
    • Apolipoprotein E, arteriosclerosis and Alzheimer's disease
    • Kalaria R.N. Apolipoprotein E, arteriosclerosis and Alzheimer's disease. Lancet. 349:1997;1174-1175.
    • (1997) Lancet , vol.349 , pp. 1174-1175
    • Kalaria, R.N.1
  • 22
    • 0034603512 scopus 로고    scopus 로고
    • The role of cerebral ischemia in Alzheimer's disease
    • Kalaria R.N. The role of cerebral ischemia in Alzheimer's disease. Neurobiol. Aging. 21:2000;321-330.
    • (2000) Neurobiol. Aging , vol.21 , pp. 321-330
    • Kalaria, R.N.1
  • 23
    • 0036130159 scopus 로고    scopus 로고
    • Small vessel disease and Alzheimer's dementia: Pathological considerations
    • Kalaria R.N. Small vessel disease and Alzheimer's dementia: pathological considerations. Cerebrovasc. Dis. 13(Suppl. 2):2002;48-52.
    • (2002) Cerebrovasc. Dis. , vol.13 , pp. 48-52
    • Kalaria, R.N.1
  • 24
    • 0033005082 scopus 로고    scopus 로고
    • Inhibitors of V-Type ATPases, bafilomycin al and concanamycin a, protect against β-amyloid-mediated effects on 3-(4,5-dimethylthiazol-2-yl)-2, dipheny1tetrazolinm bromide (MTT) reduction
    • Kane M.D., Schwarz R.D., St. Pierre L., Watson M.D., Emmerling M.R., Boxer P.A.et al. Inhibitors of V-Type ATPases, bafilomycin al and concanamycin a, protect against β-amyloid-mediated effects on 3-(4,5-dimethylthiazol-2-yl)-2, dipheny1tetrazolinm bromide (MTT) reduction. J. Neurochem. 72:1999;1939-1947.
    • (1999) J. Neurochem. , vol.72 , pp. 1939-1947
    • Kane, M.D.1    Schwarz, R.D.2    St. Pierre, L.3    Watson, M.D.4    Emmerling, M.R.5    Boxer, P.A.6
  • 25
    • 0030962492 scopus 로고    scopus 로고
    • Nanomolar amyloid beta protein-induced inhibition of cellular redox activity
    • Kato M., Saito H., Abe K. Nanomolar amyloid beta protein-induced inhibition of cellular redox activity. J. Neurochem. 68:1997;1889-1895.
    • (1997) J. Neurochem. , vol.68 , pp. 1889-1895
    • Kato, M.1    Saito, H.2    Abe, K.3
  • 26
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein
    • Knauer M.F., Soreghan B., Burdick D., Kosmoski J., Glabe C.G. Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/β protein. Proc. Natl. Acad. Sci. U.S.A. 89:1992;7437-7441.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 27
    • 0023204372 scopus 로고
    • Acid-vesicle function, intracellular pathogens, and the action of chloroquine against Plasmodium falciparum
    • Krogstad D.J., Schlesinger P.H. Acid-vesicle function, intracellular pathogens, and the action of chloroquine against Plasmodium falciparum. New Engl. J. Med. 317:1987;542-549.
    • (1987) New Engl. J. Med. , vol.317 , pp. 542-549
    • Krogstad, D.J.1    Schlesinger, P.H.2
  • 28
    • 0030695856 scopus 로고    scopus 로고
    • Cytotoxic amyloid peptides inhibit cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis
    • Liu Y., Schubert D. Cytotoxic amyloid peptides inhibit cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction by enhancing MTT formazan exocytosis. J. Neurochem. 69:1997;2285-2293.
    • (1997) J. Neurochem. , vol.69 , pp. 2285-2293
    • Liu, Y.1    Schubert, D.2
  • 29
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y., Peterson D.A., Kimura H., Schubert D. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69:1997;581-593.
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 30
    • 0030794931 scopus 로고    scopus 로고
    • Influence of cell culture conditions on the protective effect of antioxidants against β-amyloid: Studies with lazaroids
    • Lucca E., Angeretti N., Forloni G. Influence of cell culture conditions on the protective effect of antioxidants against β-amyloid: studies with lazaroids. Brain Res. 764:1997;293-298.
    • (1997) Brain Res. , vol.764 , pp. 293-298
    • Lucca, E.1    Angeretti, N.2    Forloni, G.3
  • 32
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and citotoxicity assays
    • Mosmann M.P. Rapid colorimetric assay for cellular growth and survival: application to proliferation and citotoxicity assays. J. Immunol. Meth. 65:1983;55-63.
    • (1983) J. Immunol. Meth. , vol.65 , pp. 55-63
    • Mosmann, M.P.1
  • 33
    • 0037092164 scopus 로고    scopus 로고
    • Vitamin E but not estradiol protects against vascular toxicity induced by beta-amyloid type and the Dutch amyloid variant
    • Munoz F.J., Opazo C., Gil-Gomez G., Tapia G., Fernandez V., Valverde M.A.et al. Vitamin E but not estradiol protects against vascular toxicity induced by beta-amyloid type and the Dutch amyloid variant. J. Neurosci. 22:2002;3081-3089.
    • (2002) J. Neurosci. , vol.22 , pp. 3081-3089
    • Munoz, F.J.1    Opazo, C.2    Gil-Gomez, G.3    Tapia, G.4    Fernandez, V.5    Valverde, M.A.6
  • 34
    • 0036883586 scopus 로고    scopus 로고
    • Human amyloid-beta causes changes in the levels of endothelial protein kinase C and its alpha isoform in vitro
    • Pakaski M., Balaspiri L., Checler F., Kasa P. Human amyloid-beta causes changes in the levels of endothelial protein kinase C and its alpha isoform in vitro. Neurochem. Int. 41:2002;409-414.
    • (2002) Neurochem. Int. , vol.41 , pp. 409-414
    • Pakaski, M.1    Balaspiri, L.2    Checler, F.3    Kasa, P.4
  • 35
    • 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., Maxfield F.R. Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells. J. Biol. Chem. 272:1997;29390-29397.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29390-29397
    • Paresce, D.M.1    Chung, H.2    Maxfield, F.R.3
  • 36
    • 0034603601 scopus 로고    scopus 로고
    • Soluble β-amyloid peptides mediate vasoactivity via activation of a pro-inflammatory pathway
    • Paris D., Town T., Mori T., Parker T.A., Humphrey J., Mullan M. Soluble β-amyloid peptides mediate vasoactivity via activation of a pro-inflammatory pathway. Neurobiol. Aging. 21:2000;183-197.
    • (2000) Neurobiol. Aging , vol.21 , pp. 183-197
    • Paris, D.1    Town, T.2    Mori, T.3    Parker, T.A.4    Humphrey, J.5    Mullan, M.6
  • 37
    • 0029860696 scopus 로고    scopus 로고
    • β-Amyloid-mediated inhibition of redox activity (MTT reduction) is not an indicator of astroglial degeneration
    • Patel A.J., Gunasekera S., Jen A., Rohan de Silva H.A. β-Amyloid-mediated inhibition of redox activity (MTT reduction) is not an indicator of astroglial degeneration. NeuroReport. 7:1996;2026-2030.
    • (1996) NeuroReport , vol.7 , pp. 2026-2030
    • Patel, A.J.1    Gunasekera, S.2    Jen, A.3    Rohan de Silva, H.A.4
  • 38
    • 0028170719 scopus 로고
    • Soluble amyloid beta-protein in the cerebrospinal fluid from patients with Alzheimer s disease, vascular dementia and controls
    • Pittila T., Kim K.S., Mehta P.D., Frey H., Wisniewsky H.M. Soluble amyloid beta-protein in the cerebrospinal fluid from patients with Alzheimer s disease, vascular dementia and controls. J. Neurol. Sci. 127:1994;90-95.
    • (1994) J. Neurol. Sci. , vol.127 , pp. 90-95
    • Pittila, T.1    Kim, K.S.2    Mehta, P.D.3    Frey, H.4    Wisniewsky, H.M.5
  • 39
    • 0032512867 scopus 로고    scopus 로고
    • Toxic effects of β-amyloid (25-35) on immortalised rat brain endothelial cell: Protection by carnosine, homocarnosine and β-alanine
    • Preston J.E., Hipkiss A.R., Himsworth D.T.J., Romero I.A., Abbott J.N. Toxic effects of β-amyloid (25-35) on immortalised rat brain endothelial cell: protection by carnosine, homocarnosine and β-alanine. Neurosci. Lett. 242:1998;105-108.
    • (1998) Neurosci. Lett. , vol.242 , pp. 105-108
    • Preston, J.E.1    Hipkiss, A.R.2    Himsworth, D.T.J.3    Romero, I.A.4    Abbott, J.N.5
  • 40
    • 0034940552 scopus 로고    scopus 로고
    • Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production
    • Price J.M., Chi X., Hellermann G., Sutton P.T. Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production. Neurol. Res. 23:2001;506-512.
    • (2001) Neurol. Res. , vol.23 , pp. 506-512
    • Price, J.M.1    Chi, X.2    Hellermann, G.3    Sutton, P.T.4
  • 41
    • 0033844315 scopus 로고    scopus 로고
    • Apolipoprotein E and intronic polymorphism of presenilin 1 and alpha-1-antichymotypsin in Alzheimer's disease and vascular dementia
    • Rodriguez-Martin T., Calella A.M., Silva S., Munna E., Modena P., Chiesa R.et al. Apolipoprotein E and intronic polymorphism of presenilin 1 and alpha-1-antichymotypsin in Alzheimer's disease and vascular dementia. Dement. Geriatr. Cogn. Disord. 11:2000;239-244.
    • (2000) Dement. Geriatr. Cogn. Disord. , vol.11 , pp. 239-244
    • Rodriguez-Martin, T.1    Calella, A.M.2    Silva, S.3    Munna, E.4    Modena, P.5    Chiesa, R.6
  • 42
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 43
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature. 399:1999;A23-A31.
    • (1999) Nature , vol.399 , pp. 23-A31
    • Selkoe, D.J.1
  • 44
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4, dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides
    • Shearman M.S., Hawtin S.R., Tailor V.J. The intracellular component of cellular 3-(4, dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides. J. Neurochem. 65:1995;218-227.
    • (1995) J. Neurochem. , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 45
    • 0034521392 scopus 로고    scopus 로고
    • 1-40 peptide from brain by low-density lipoprotein receptor-related protein-1 at the blood brain barrier
    • 1-40 peptide from brain by low-density lipoprotein receptor-related protein-1 at the blood brain barrier. J. Clin. Invest. 106:2000;1489-1499.
    • (2000) J. Clin. Invest. , vol.106 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3
  • 46
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture
    • Skovronsky D.M., Doms R.W., Lee V.M.Y. Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture. J. Cell Biol. 141:1998;1031-1039.
    • (1998) J. Cell Biol. , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.Y.3
  • 47
    • 18244365872 scopus 로고    scopus 로고
    • Amyloid-beta tau alterations and mitochondrial dysfunction in Alzheimer disease the chickens or the eggs
    • Smith M.A., Drew K.L., Nunomura A., Takeda A., Hirai K., Zhu X. Amyloid-beta tau alterations and mitochondrial dysfunction in Alzheimer disease the chickens or the eggs. Neurochem. Int. 40:2002;527-531.
    • (2002) Neurochem. Int. , vol.40 , pp. 527-531
    • Smith, M.A.1    Drew, K.L.2    Nunomura, A.3    Takeda, A.4    Hirai, K.5    Zhu, X.6
  • 48
    • 0030851944 scopus 로고    scopus 로고
    • Superoxide free radical and intracellular calcium mediate Aβ1-42 induced endothelial toxicity
    • Suo Z., Fang C., Crawford F., Mullan M. Superoxide free radical and intracellular calcium mediate Aβ1-42 induced endothelial toxicity. Brain Res. 762:1997;144-152.
    • (1997) Brain Res. , vol.762 , pp. 144-152
    • Suo, Z.1    Fang, C.2    Crawford, F.3    Mullan, M.4
  • 49
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer Aβ42 accumulates in multivescicular bodies and is associated with synaptic pathology
    • Takahashi R.H., Milner T.A., Li F., Nam E.E., Edgar M.A., Yamaguchi H. Intraneuronal Alzheimer Aβ42 accumulates in multivescicular bodies and is associated with synaptic pathology. J. Am. Pathol. 161:2002;1869-1879.
    • (2002) J. Am. Pathol. , vol.161 , pp. 1869-1879
    • Takahashi, R.H.1    Milner, T.A.2    Li, F.3    Nam, E.E.4    Edgar, M.A.5    Yamaguchi, H.6
  • 50
    • 0029670094 scopus 로고    scopus 로고
    • β-Amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas T., Thomas G., McLendon C., Sutton T., Mullan M. β-Amyloid-mediated vasoactivity and vascular endothelial damage. Nature. 380:1996;168-171.
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 51
    • 0028261087 scopus 로고
    • Microvasculature in brain biopsy specimens from patients with Alzheimer's disease: An immunohistochemical and ultrastructural study
    • Vinters H.V., Secor D.L., Read S.L., Frazee J.G., Tomyiasu U., Stanley T.et al. Microvasculature in brain biopsy specimens from patients with Alzheimer's disease: an immunohistochemical and ultrastructural study. Ultrastruct. Pathol. 18:1994;333-348.
    • (1994) Ultrastruct. Pathol. , vol.18 , pp. 333-348
    • Vinters, H.V.1    Secor, D.L.2    Read, S.L.3    Frazee, J.G.4    Tomyiasu, U.5    Stanley, T.6
  • 53
    • 0032731216 scopus 로고    scopus 로고
    • Amyloid β-(1-40) stimulates cyclic GMP production via release of kinins in primary cultured endothelial cells
    • Wirth K.J., Fink E., Rudolphi K., Heitsch H., Deutschländer N., Wiemer G. Amyloid β-(1-40) stimulates cyclic GMP production via release of kinins in primary cultured endothelial cells. Eur. J. Pharmacol. 382:2000;27-33.
    • (2000) Eur. J. Pharmacol. , vol.382 , pp. 27-33
    • Wirth, K.J.1    Fink, E.2    Rudolphi, K.3    Heitsch, H.4    Deutschländer, N.5    Wiemer, G.6
  • 54
    • 0034981701 scopus 로고    scopus 로고
    • Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation
    • Xu J., Chen S., Ku G., Abmed S.H., Chen H., Hsu C.Y. Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation. J. Cereb. Blood Flow Metab. 21:2001;702-710.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 702-710
    • Xu, J.1    Chen, S.2    Ku, G.3    Abmed, S.H.4    Chen, H.5    Hsu, C.Y.6
  • 55
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of β-amyloid protein: Reversal by tachykinin neuropeptides
    • Yankner B.S., Duffy L.K., Kirshner D.A. Neurotrophic and neurotoxic effects of β-amyloid protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.S.1    Duffy, L.K.2    Kirshner, D.A.3
  • 56
    • 0037038820 scopus 로고    scopus 로고
    • Vascular disorder in Alzheimer's disease: Role in the pathogenesis of dementia and therapeutic targets
    • Ziokovic B.V. Vascular disorder in Alzheimer's disease: role in the pathogenesis of dementia and therapeutic targets. Adv. Drug. Deliv. Rev. 54:2002;1553-1559.
    • (2002) Adv. Drug. Deliv. Rev. , vol.54 , pp. 1553-1559
    • Ziokovic, B.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.