메뉴 건너뛰기




Volumn 746, Issue 1-2, 1997, Pages 275-284

Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A β1-42, in differentiated PC12 cells

Author keywords

Alzheimer's disease; Amyloid beta peptide; Amyloid precursor protein; Endosome; Lysosome; Neurodegeneration; PC12 cell

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN;

EID: 0031030053     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(96)01262-0     Document Type: Article
Times cited : (104)

References (54)
  • 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. and 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
    • 0015221791 scopus 로고
    • Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells
    • Avruch, J. and Wallach, D.F.H., Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells, Biochim. Biophys. Acta, 233, (1971) 334-347.
    • (1971) Biochim. Biophys. Acta , vol.233 , pp. 334-347
    • Avruch, J.1    Wallach, D.F.H.2
  • 3
    • 0024815331 scopus 로고
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects
    • Benowitz, L.I., Rodriguez, W., Paskevich, P., Mufson, E.J., Schenk, D. and Neve, R.L., The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. Exp. Neurol., 106 (1989) 237-250.
    • (1989) Exp. Neurol. , vol.106 , pp. 237-250
    • Benowitz, L.I.1    Rodriguez, W.2    Paskevich, P.3    Mufson, E.J.4    Schenk, D.5    Neve, R.L.6
  • 6
    • 0023692019 scopus 로고
    • A microsystem to assay lysosomal activities in cultured retinal pigment epithelial cells
    • Cabral, D., Unger, W., Boulton, M. and Marshall, J., A microsystem to assay lysosomal activities in cultured retinal pigment epithelial cells, Curr. Eye Res., 7 (1988) 1097-1104.
    • (1988) Curr. Eye Res. , vol.7 , pp. 1097-1104
    • Cabral, D.1    Unger, W.2    Boulton, M.3    Marshall, J.4
  • 7
    • 0024367837 scopus 로고
    • Evidence for lysosomal processing of amyloid beta-protein precursor in cultured cells
    • Cole, G.M., Huynh, T.V. and Saitoh, T., Evidence for lysosomal processing of amyloid beta-protein precursor in cultured cells, Neurochem. Res., 14 (1989) 933-939.
    • (1989) Neurochem. Res. , vol.14 , pp. 933-939
    • Cole, G.M.1    Huynh, T.V.2    Saitoh, T.3
  • 8
    • 0021352917 scopus 로고
    • Shift of equilibrium density induced by 3,3′-diaminobenzidine cytochemistry: A new procedure for the analysis and purification of peroxidase-containg organelles
    • Courtoy, P.J., Quintart, J. and Baudhuin, P., Shift of equilibrium density induced by 3,3′-diaminobenzidine cytochemistry: A new procedure for the analysis and purification of peroxidase-containg organelles, J. Cell Biol., 98 (1984) 870-876.
    • (1984) J. Cell Biol. , vol.98 , pp. 870-876
    • Courtoy, P.J.1    Quintart, J.2    Baudhuin, P.3
  • 10
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G.G. and Wong, C.W., Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochem. Biophys. Res. Comm., 120 (1984) 885-890.
    • (1984) Biochem. Biophys. Res. Comm. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 11
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T.E., Estus, S., Younkin, L.H., Selkoe, D.J. and Younkin, S.G., Processing of the amyloid protein precursor to potentially amyloidogenic derivatives, Science, 255 (1992) 728-730.
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 12
    • 0028915895 scopus 로고
    • Amyloid beta protein in Alzheimer's disease brain
    • Gravina, S.A., Ho, L., Eckman, C.B. et al., Amyloid beta protein in Alzheimer's disease brain, J. Biol. Chem., 270 (1995) 7013-7016.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3
  • 13
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass, C., Koo, E.H., Mellon, A., Hung, A.Y. and Selkoe, D.J., Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments, Nature, 357 (1992) 500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 15
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative procesing of amyloid β-protein precursor
    • Haass, C., Hung, A.Y., Selkoe, D.J. and Teplow, D.B., Mutations associated with a locus for familial Alzheimer's disease result in alternative procesing of amyloid β-protein precursor, J. Biol. Chem., 269 (1994) 17741-17748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 16
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • Haass, C. and Selkoe. D.J., Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide, Cell, 75 (1993) 1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 17
    • 0014559444 scopus 로고
    • The isolation of lysosomes from Ehrlich ascites tumor cells following pretreatment of mice with triton WR-1339
    • Horvat, A., Touster, O. and Baxandall, J., The isolation of lysosomes from Ehrlich ascites tumor cells following pretreatment of mice with triton WR-1339, J. Cell Biol., 42 (1969) 469-476.
    • (1969) J. Cell Biol. , vol.42 , pp. 469-476
    • Horvat, A.1    Touster, O.2    Baxandall, J.3
  • 18
    • 0028169925 scopus 로고
    • Visualization of A β42(43) and A β40 in senile plaques with end specific A β monoclonals: Evidence that an initially deposited species is A β42(43)
    • Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N. and Ihara, Y., Visualization of A β42(43) and A β40 in senile plaques with end specific A β monoclonals: Evidence that an initially deposited species is A β42(43), Nature, 13 (1994) 45-53.
    • (1994) Nature , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 20
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein
    • Knauer, M.F., Soreghan, B., Burdick, D., Kosmoski, J. and Glabe, C.G., Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein, Proc. Natl. Acad. Sci. USA, 89 (1992) 7437-7441.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 21
    • 0026674585 scopus 로고
    • Evidence for a nonsecretory, acidic degradation pathway for amyloid precursor protein in 293 cells. Identification of a novel, 22 kDa, beta-peptide-containing intermediate
    • Knops, J., Lieberburg, I. and Sinha, S., Evidence for a nonsecretory, acidic degradation pathway for amyloid precursor protein in 293 cells. Identification of a novel, 22 kDa, beta-peptide-containing intermediate, J. Biol. Chem., 267 (1992) 16022-16024.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16022-16024
    • Knops, J.1    Lieberburg, I.2    Sinha, S.3
  • 22
    • 0026526712 scopus 로고
    • Specific storage of subunit c of the mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease)
    • Kominami, E., Ezaki, J., Muno, D., Ishido, K., Uneo, T. and Wolfe, L.S., Specific storage of subunit c of the mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease), J. Biochem., 111 (1992) 278-282.
    • (1992) J. Biochem. , vol.111 , pp. 278-282
    • Kominami, E.1    Ezaki, J.2    Muno, D.3    Ishido, K.4    Uneo, T.5    Wolfe, L.S.6
  • 24
    • 0028972233 scopus 로고
    • Intracellular accumulation of beta-amyloid in cells expressing the Swedish mutation amyloid precursor protein
    • Martin, B.L., Schrader-Fischer, G., Busciglio, J., Duke, M., Paganetti, P. and Yankner, B.A., Intracellular accumulation of beta-amyloid in cells expressing the Swedish mutation amyloid precursor protein, J. Biol. Chem., 270 (1995) 26727-26730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26727-26730
    • Martin, B.L.1    Schrader-Fischer, G.2    Busciglio, J.3    Duke, M.4    Paganetti, P.5    Yankner, B.A.6
  • 27
    • 0027422751 scopus 로고
    • Genetic and molecular advances in Alzheimer's disease
    • Mullan, M. and Crawford, F., Genetic and molecular advances in Alzheimer's disease, Trends Neurosci., 16 (1993) 398-403.
    • (1993) Trends Neurosci. , vol.16 , pp. 398-403
    • Mullan, M.1    Crawford, F.2
  • 29
    • 0025829695 scopus 로고
    • pH-induced microtuble-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton, R.G., Dotti, C.G., Bacallao, R., Kurtz, I., Simons, K. and Prydz, K., pH-induced microtuble-dependent redistribution of late endosomes in neuronal and epithelial cells, J. Cell Biol., 113 (1991) 261-274.
    • (1991) J. Cell Biol. , vol.113 , pp. 261-274
    • Parton, R.G.1    Dotti, C.G.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 30
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C.J., Burdick, D., Walencewicz, A.J., Glabe, C.G. and Cotman, C.W., Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state, J. Neurosci., 13 (1993) 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
  • 31
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C.J., Walencewicz, A.J., Glabe, C.G. and Cotman, C.W., In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity, Brain. Res., 563 (1991) 311-314.
    • (1991) Brain. Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 32
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli, F., Castano, E., Glenner, G.G. and Frangione, B., Differences between vascular and plaque core amyloid in Alzheimer's disease, J. Neurochem., 51 (1988) 648-651.
    • (1988) J. Neurochem. , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3    Frangione, B.4
  • 33
  • 36
    • 0027332081 scopus 로고
    • Beta-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., beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease, Proc. Natl. Acad. Sci. USA, 90 (1993) 10836-10840.
    • (1993) Proc. Natl. Acad. Sci. USA , 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
  • 37
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe, D.J., 1994. Cell biology of the amyloid beta-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
  • 39
    • 0027250352 scopus 로고
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments
    • Siman, R., Mistretta, S., Durkin, J.T., Savage, M.J., Loh, T., Trusko, S. and Scott, R.W., Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments, J. Biol. Chem., 268 (1993) 16602-16609.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16602-16609
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3    Savage, M.J.4    Loh, T.5    Trusko, S.6    Scott, R.W.7
  • 40
    • 0029047722 scopus 로고
    • Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease
    • Snow, A.D., Kinsella, M.G., Parks, E., Sekiguchi, R.T., Miller, J.D., Kimata, K. and Wight., T.N., Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease, Arch. Biochem. Biophys., 320 (1995) 84-95.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 84-95
    • Snow, A.D.1    Kinsella, M.G.2    Parks, E.3    Sekiguchi, R.T.4    Miller, J.D.5    Kimata, K.6    Wight, T.N.7
  • 41
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • Suzuki, N., Cheung, T.T., Cai, X.D., Odaka, A., Otvos, L. Jr., Eckman, C., Golde, T.E. and Younkin, S.G., An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants, Science, 264 (1994) 1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos L., Jr.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 42
    • 0027057883 scopus 로고
    • Amyloid beta/A4 prepursor protein (APP) processing in lysosomes
    • Tagawa, K., Maruyama, K. and Ishiura, S., Amyloid beta/A4 prepursor protein (APP) processing in lysosomes, Ann. N.Y. Acad. Sci., 674 (1992) 129-137.
    • (1992) Ann. N.Y. Acad. Sci. , vol.674 , pp. 129-137
    • Tagawa, K.1    Maruyama, K.2    Ishiura, S.3
  • 43
    • 0028922520 scopus 로고
    • Amyloid beta protein 1-42/43 (A beta 1-42/43) in cerebellar diffuse plaques: Enzyme-linked immunosorbent assay and immunocytochemical study
    • Tamaoka, A., Sawamura, N., Odaka, A., Suzuki, N., Mizusawa, H., Shoji, S. and Mori., H., Amyloid beta protein 1-42/43 (A beta 1-42/43) in cerebellar diffuse plaques: enzyme-linked immunosorbent assay and immunocytochemical study, Brain. Res., 679 (1995) 151-156.
    • (1995) Brain. Res. , vol.679 , pp. 151-156
    • Tamaoka, A.1    Sawamura, N.2    Odaka, A.3    Suzuki, N.4    Mizusawa, H.5    Shoji, S.6    Mori, H.7
  • 44
    • 0027379395 scopus 로고
    • Characterization of beta-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey, C., Lee, D., Keim, P., Lieberburg, I. and Schenk, D.B., Characterization of beta-amyloid peptide from human cerebrospinal fluid, J. Neurochem., 61 (1993) 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
  • 46
    • 0025095256 scopus 로고
    • Beta-amyloid protein promotes neuritic branching in hippocampal cultures
    • Whitson, J.S., Glabe, C.G., Shintani, E., Abcar, A. and Cotman, C.W., Beta-amyloid protein promotes neuritic branching in hippocampal cultures, Neurosci. Lett., 110 (1990) 319-324.
    • (1990) Neurosci. Lett. , vol.110 , pp. 319-324
    • Whitson, J.S.1    Glabe, C.G.2    Shintani, E.3    Abcar, A.4    Cotman, C.W.5
  • 47
    • 0024543836 scopus 로고
    • Amyloid beta protein enhances the survival of hippocampal neurons in vitro
    • Whitson, J.S., Selkoe, D.J. and Cotman, C.W., Amyloid beta protein enhances the survival of hippocampal neurons in vitro, Science, 243 (1989) 1488-1490.
    • (1989) Science , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 49
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid beta-protein (a beta): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa, K., Odaka, A., Suzuki, N. and Ihara, Y., GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease Nat. Med., 1 (1995) 1062-1066.
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 50
    • 0029057814 scopus 로고
    • Intracellular a beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang, A.J., Knauer, M., Burdick, D.A. and Glabe. C., Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells, J. Biol. Chem., 270 (1995) 14786-14792.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 51
  • 52
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner, B.A., Duffy, L.K. and Kirschner, D.A., Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides, Science, 250 (1990) 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 53
    • 0028945660 scopus 로고
    • Evidence that a beta 42 is the real culprit in Alzheimer's disease
    • Younkin, S.G., Evidence that A beta 42 is the real culprit in Alzheimer's disease, Ann. Neurol., 37 (1995) 287-288.
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.G.1
  • 54
    • 0028537416 scopus 로고
    • The amyloid beta protein precursor mutations linked to familial Alzheimer's disease alter processing in a way that fosters amyloid deposition
    • Younkin, S.G., The amyloid beta protein precursor mutations linked to familial Alzheimer's disease alter processing in a way that fosters amyloid deposition, Tohoku. J. Exp. Med., 174 (1994) 217-223.
    • (1994) Tohoku. J. Exp. Med. , vol.174 , pp. 217-223
    • Younkin, S.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.