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Volumn 29, Issue 2, 1997, Pages 129-134

Congo red reverses amyloid β protein-induced cellular stress in astrocytes

Author keywords

3 (4,5 Dimethylthiazol 2 yl) 2,5 diphenyltetrazolium bromide; Alzheimer's disease; Amyloid protein; Astrocyte; Congo red

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; AMYLOID BETA PROTEIN; CONGO RED;

EID: 0030870673     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(97)00081-3     Document Type: Article
Times cited : (15)

References (34)
  • 1
  • 2
    • 0030475798 scopus 로고    scopus 로고
    • Menadione toxicity in cultured rat cortical astrocytes
    • Abe, K., Saito, H., 1996. Menadione toxicity in cultured rat cortical astrocytes. Jpn. J. Pharmacol. 72, 299-306.
    • (1996) Jpn. J. Pharmacol. , vol.72 , pp. 299-306
    • Abe, K.1    Saito, H.2
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., Davis, J.B., Lesley, R., Schubert, D., 1994. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77, 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 4
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence and involvement of mitochondrial electron transport in MTT reduction
    • Berridge, M.V., Tan, A.S., 1993. Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence and involvement of mitochondrial electron transport in MTT reduction. Arch. Biochem. Biophys. 303, 474-482.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 6
    • 0028588694 scopus 로고
    • Congo red protects against toxicity of β-amyloid peptides on rat hippocampal neurons
    • Burgevin, M.C., Passat, M., Deniel, N., Capet, M., Doble, A., 1994. Congo red protects against toxicity of β-amyloid peptides on rat hippocampal neurons. Neuroreport 5, 2429-2432.
    • (1994) Neuroreport , vol.5 , pp. 2429-2432
    • Burgevin, M.C.1    Passat, M.2    Deniel, N.3    Capet, M.4    Doble, A.5
  • 7
    • 0027526419 scopus 로고
    • Release of excess amyloid betaprotein from a mutant amyloid beta-protein precursor
    • Cai, X.D., Golde, T., Youkin, S., 1993. Release of excess amyloid betaprotein from a mutant amyloid beta-protein precursor. Science 259, 514-516.
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.D.1    Golde, T.2    Youkin, S.3
  • 10
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine method
    • Cooper, J.H., 1974. Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine method. Lab. Invest. 31, 232-238.
    • (1974) Lab. Invest. , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 11
    • 0014346532 scopus 로고
    • Histochemical observations on amyloid with reference to polarization microscopy
    • DeLellis, R.A., Glenner, C.G., Ram, J.S., 1968. Histochemical observations on amyloid with reference to polarization microscopy. J. Histochem. Cytochem. 16, 663-665.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 663-665
    • DeLellis, R.A.1    Glenner, C.G.2    Ram, J.S.3
  • 12
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher, S., Glowinski, J., Premont, J., 1996. Astrocytes protect neurons from hydrogen peroxide toxicity. J. Neurosci. 16, 2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 14
    • 0023818885 scopus 로고
    • Alzheimer's disease: Its proteins and genes
    • Glenner, G.G., 1988. Alzheimer's disease: its proteins and genes. Cell 52, 307-308.
    • (1988) Cell , vol.52 , pp. 307-308
    • Glenner, G.G.1
  • 15
    • 0015408029 scopus 로고
    • The relation of the peptides of Congo red-stained amyloid fibrils to the beta-conformation
    • Glenner, G.G., Eanes, E.D., Page, D.L., 1972. The relation of the peptides of Congo red-stained amyloid fibrils to the beta-conformation. J. Histochem. Cytochem. 20, 821-826.
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 16
    • 0029031348 scopus 로고
    • Apoptotic cell death induced by β-amyloid 1-42 peptide is cell type dependent
    • Gschwind, M., Huber, G., 1995. Apoptotic cell death induced by β-amyloid 1-42 peptide is cell type dependent. J. Neurochem. 65, 292-300.
    • (1995) J. Neurochem. , vol.65 , pp. 292-300
    • Gschwind, M.1    Huber, G.2
  • 18
    • 0030962492 scopus 로고    scopus 로고
    • Nanomolar amyloid β protein-induced inhibition of cellular redox activity in cultured astrocytes
    • Kato, M., Saito, H., Abe, K., 1997. Nanomolar amyloid β protein-induced inhibition of cellular redox activity in cultured astrocytes. J. Neurochem. 68, 1889-1895.
    • (1997) J. Neurochem. , vol.68 , pp. 1889-1895
    • Kato, M.1    Saito, H.2    Abe, K.3
  • 19
    • 0028076051 scopus 로고
    • Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease
    • Klunk, W.E., Debnath, M.L., Pettegrew, J.W., 1994. Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease. Neurobiol. Aging 15, 691-698.
    • (1994) Neurobiol. Aging , vol.15 , pp. 691-698
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 20
    • 0343391401 scopus 로고
    • Chrysamine G, a Congo red analogue which enters the brain, prevents Aβ-induced toxicity in cell culture
    • Klunk, W.E., Koros, A.M., Debnath, M.L., Pettegrew, J.W., 1995. Chrysamine G, a Congo red analogue which enters the brain, prevents Aβ-induced toxicity in cell culture. Abstr. Soc. Neurosci. 21, 1011.
    • (1995) Abstr. Soc. Neurosci. , vol.21 , pp. 1011
    • Klunk, W.E.1    Koros, A.M.2    Debnath, M.L.3    Pettegrew, J.W.4
  • 21
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk, W.E., Pettegrew, J.W., Abraham, D.J., 1989. Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37, 1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 22
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo, A., Yankner, B.A., 1994. β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91, 12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 23
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M.P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., Rydel, R.E., 1992. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 24
    • 0030598110 scopus 로고    scopus 로고
    • Amyloid ox-fox transducers
    • Mattson, M.P., Rydel, R.E., 1996. Amyloid ox-fox transducers. Nature 382, 674-675.
    • (1996) Nature , vol.382 , pp. 674-675
    • Mattson, M.P.1    Rydel, R.E.2
  • 25
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T., 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65, 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 26
    • 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., Rohand Silva, H.A., 1996. β-Amyloid-mediated inhibition of redox activity (MTT reduction) is not an indicator of astroglial degeneration. Neuroreport 7, 2026-2030.
    • (1996) Neuroreport , vol.7 , pp. 2026-2030
    • Patel, A.J.1    Gunasekera, S.2    Jen, A.3    Rohand Silva, H.A.4
  • 27
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C.J., Burdick, D., Walencewicz, A.J., Glabe, C.G., Cotman, C.W., 1993. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 28
    • 0028172346 scopus 로고
    • β-Amyloid-induced changes in cultured astrocytes parallel reactive astrocytosis associated widh senile plaques in Alzheimer's disease
    • Pike, C.J., Cummings, B.J., Monzavi, R., Cotman, C.W., 1994. β-Amyloid-induced changes in cultured astrocytes parallel reactive astrocytosis associated widh senile plaques in Alzheimer's disease. Neuroscience 63, 517-531.
    • (1994) Neuroscience , vol.63 , pp. 517-531
    • Pike, C.J.1    Cummings, B.J.2    Monzavi, R.3    Cotman, C.W.4
  • 29
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells
    • Pollack, S.J., Sadler, I.I.J., Hawtin, S.R., Tailor, V.J., Shearman, M.S., 1995. Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells. Neurosci. Lett. 184, 113-116.
    • (1995) Neurosci. Lett. , vol.184 , pp. 113-116
    • Pollack, S.J.1    Sadler, I.I.J.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 30
    • 0013812532 scopus 로고
    • Congo red as a stain for fluorescence microscopy of amyloid
    • Puchtler, H., Sweat, F., 1965. Congo red as a stain for fluorescence microscopy of amyloid. J. Histochem. Cytochem. 13, 693-694.
    • (1965) J. Histochem. Cytochem. , vol.13 , pp. 693-694
    • Puchtler, H.1    Sweat, F.2
  • 31
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of, β-amyloid-mediated cell death
    • Shearman, M.S., Ragan, C.I., Iversen, L.L., 1994. Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of, β-amyloid-mediated cell death. Proc. Natl. Acad. Sci. USA 91, 1470-1474.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 32
    • 0028181758 scopus 로고
    • Reversible random coil-β sheet transition of the Alzheimer β-amyloid fragment (25-35)
    • Terzi, E., Holzemann, G., Seeling, J., 1994. Reversible random coil-β sheet transition of the Alzheimer β-amyloid fragment (25-35). Biochemistry 33, 1345-1350.
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Holzemann, G.2    Seeling, J.3
  • 34
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B.A., Duffy, L.K., Kirschner, D.A., 1990. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 25, 279-282.
    • (1990) Science , vol.25 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.