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Volumn 31, Issue 2, 1997, Pages 171-186

Effects of acidosis on the distribution and processing of the β-amyloid precursor protein in cultured hippocampal neurons

Author keywords

Acidosis; Alzheimer disease; Hippocampus; Neuron culture; amyloid

Indexed keywords

AMYLOID PRECURSOR PROTEIN; LACTIC ACID;

EID: 0030823312     PISSN: 10447393     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02815241     Document Type: Article
Times cited : (27)

References (49)
  • 1
    • 0028060470 scopus 로고
    • A further analysis of physiological changes in rats in the forced swim test
    • Abel E. L. (1994) A further analysis of physiological changes in rats in the forced swim test. Physiol. Behav. 56, 795-800.
    • (1994) Physiol. Behav. , vol.56 , pp. 795-800
    • Abel, E.L.1
  • 2
    • 0026445465 scopus 로고
    • Human serum induces Alzheimer markers in cultured hippocampal neurons
    • Brewer G. J. and Ashford J. W. A. (1992) Human serum induces Alzheimer markers in cultured hippocampal neurons. J. Neurosci. Res. 33, 355-369.
    • (1992) J. Neurosci. Res. , vol.33 , pp. 355-369
    • Brewer, G.J.1    Ashford, J.W.A.2
  • 3
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free combination
    • Brewer G. J., Torricelli J. R., Evege E. K., and Price P. J. (1993) Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free combination. J. Neurosci. Res. 35, 567-576.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 4
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D. H., Matsudaira P., and Yankner B. A. (1993) Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA 90, 2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 6
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid protein precursor
    • Cai X., Golde T. E., and Younkin S. G. (1993) Release of excess amyloid beta protein from a mutant amyloid protein precursor. Science 259, 514-516.
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.1    Golde, T.E.2    Younkin, S.G.3
  • 7
    • 0026589836 scopus 로고
    • Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein
    • Caporaso G. L., Gandy S. E., Buxbaum J. D., and Greengard P. (1992) Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein. Proc. Nat. Acad. Sci. USA 89, 2252-2256.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 2252-2256
    • Caporaso, G.L.1    Gandy, S.E.2    Buxbaum, J.D.3    Greengard, P.4
  • 9
    • 0025368999 scopus 로고
    • Relationship between plasma glucose, brain lactate, and intracellular pH during cerebral ischemia in gerbels
    • Combs D., Dempsey R., Maley M., Donaldson D., and Smith C. (1990) Relationship between plasma glucose, brain lactate, and intracellular pH during cerebral ischemia in gerbels. Stroke 21, 936-942.
    • (1990) Stroke , vol.21 , pp. 936-942
    • Combs, D.1    Dempsey, R.2    Maley, M.3    Donaldson, D.4    Smith, C.5
  • 10
    • 0002850020 scopus 로고
    • Lysosomes, a new group of cytoplasmic particles
    • Hayashi T., ed., The Ronald Press, New York
    • DeDuve C. (1959) Lysosomes, a new group of cytoplasmic particles, in Subcellular Particles (Hayashi T., ed.), pp. 128-159, The Ronald Press, New York.
    • (1959) Subcellular Particles , pp. 128-159
    • DeDuve, C.1
  • 11
    • 0003868932 scopus 로고
    • Federation of American Societies for Experimental Biology, Washington, DC
    • Dittmer D. S. (1961) Blood and Other Body Fluids, p. 174. Federation of American Societies for Experimental Biology, Washington, DC.
    • (1961) Blood and Other Body Fluids , pp. 174
    • Dittmer, D.S.1
  • 12
    • 0027215550 scopus 로고
    • Intraneuronal compartments of the amyloid precursor protein
    • Ferreira A., Caceres A., and Kosik K. S. (1993) Intraneuronal compartments of the amyloid precursor protein. J. Neurosci. 13, 3112-3123.
    • (1993) J. Neurosci. , vol.13 , pp. 3112-3123
    • Ferreira, A.1    Caceres, A.2    Kosik, K.S.3
  • 13
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • Gibson G., Sheu K., Blass J., Baker A., Carlson K., Harding B., and Perrino P. (1988) Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease. Arch. Neurol. 45, 836-841.
    • (1988) Arch. Neurol. , vol.45 , pp. 836-841
    • Gibson, G.1    Sheu, K.2    Blass, J.3    Baker, A.4    Carlson, K.5    Harding, B.6    Perrino, P.7
  • 14
    • 0025129130 scopus 로고
    • Acidosis reduces NMDA receptor activation, glutamate neurotoxicity, and oxygen-glucose deprivation neuronal injury in cortical cultures
    • Gifford R. G., Monyer H., Christine C. W., and Choi D. W. (1990) Acidosis reduces NMDA receptor activation, glutamate neurotoxicity, and oxygen-glucose deprivation neuronal injury in cortical cultures. Brain Res. 506, 339-342.
    • (1990) Brain Res. , vol.506 , pp. 339-342
    • Gifford, R.G.1    Monyer, H.2    Christine, C.W.3    Choi, D.W.4
  • 16
    • 5344253299 scopus 로고
    • Differential effect of agents altering vesicular pH on the generation of amyloid beta-peptide derived from mutant or wild type beta-APP
    • Haass C., Citron M., Capell A., Teplow D., and Selkoe D. (1994) Differential effect of agents altering vesicular pH on the generation of amyloid beta-peptide derived from mutant or wild type beta-APP. Soc. Neurosci. Abs. 20, 191.7.
    • (1994) Soc. Neurosci. Abs. , vol.20
    • Haass, C.1    Citron, M.2    Capell, A.3    Teplow, D.4    Selkoe, D.5
  • 17
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
    • Haass C., Hung A. Y., Selkoe D. J., and Teplow D. B. (1994) Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor. J. Biol. Chem. 269, 17,741-17,748.
    • (1994) J. Biol. Chem. , vol.269
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 18
    • 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. (1992) Targeting of cell surface beta-amyloid precursor protein to lysosomes-alternative processing into amyloid-bearing fragments. Nature 357, 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
  • 20
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser J. (1989) Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell. Biol. 108, 855-864.
    • (1989) J. Cell. Biol. , vol.108 , pp. 855-864
    • Heuser, J.1
  • 21
    • 0027439062 scopus 로고
    • Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody-22C11
    • Hilbich C., Monning U., Grund C., Masters C. L., Beyreuther K. (1993) Amyloid-like properties of peptides flanking the epitope of amyloid precursor protein-specific monoclonal antibody-22C11. J. Biol. Chem. 268, 26,571-26,577.
    • (1993) J. Biol. Chem. , vol.268
    • Hilbich, C.1    Monning, U.2    Grund, C.3    Masters, C.L.4    Beyreuther, K.5
  • 22
    • 0023737618 scopus 로고
    • Glucose metabolism as the site of the primary abnormality
    • Hoyer S., Oesterreich K., and Wagner O. (1988) Glucose metabolism as the site of the primary abnormality. Neurology 235, 143-148.
    • (1988) Neurology , vol.235 , pp. 143-148
    • Hoyer, S.1    Oesterreich, K.2    Wagner, O.3
  • 23
    • 0027179773 scopus 로고
    • Neuroprotective effects of glutamate antagonists and extracellular acidity
    • Kaku D. A., Giffard R. G., and Choi D. W. (1993) Neuroprotective effects of glutamate antagonists and extracellular acidity. Science 260, 1516-1518.
    • (1993) Science , vol.260 , pp. 1516-1518
    • Kaku, D.A.1    Giffard, R.G.2    Choi, D.W.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • Mullan M., Crawford F., Axelman K., Houlden H., Lilius L., Winblad B., and Lannfelt L. (1992) A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nature Genet. 1, 345-347.
    • (1992) Nature Genet. , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3    Houlden, H.4    Lilius, L.5    Winblad, B.6    Lannfelt, L.7
  • 28
    • 0028985061 scopus 로고
    • Beta-amyloid peptide produced in vitro is degraded by proteinases released by cultured cells
    • Naidu A., Quon D., and Cordell B. (1995) Beta-amyloid peptide produced in vitro is degraded by proteinases released by cultured cells. J. Biol. Chem. 270, 1369-1374.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1369-1374
    • Naidu, A.1    Quon, D.2    Cordell, B.3
  • 29
    • 0028208241 scopus 로고
    • The influence of pH on glutamate- And depolarization-induced increases of intracellular calcium concentration in cortical neurons in primary culture
    • Ou-Yang Y. B., Kristian T., Mellergard P., and Siesjo B. K. (1994) The influence of pH on glutamate- and depolarization-induced increases of intracellular calcium concentration in cortical neurons in primary culture. Brain Res. 646, 65-72.
    • (1994) Brain Res. , vol.646 , pp. 65-72
    • Ou-Yang, Y.B.1    Kristian, T.2    Mellergard, P.3    Siesjo, B.K.4
  • 31
    • 0025024024 scopus 로고
    • Cytochrome oxidase deficiency in Alzheimer's disease
    • Parker W. D., Filley C. M., and Parks J. K. (1990) Cytochrome oxidase deficiency in Alzheimer's disease. Neurology 40, 1302, 1303.
    • (1990) Neurology , vol.40 , pp. 1302
    • Parker, W.D.1    Filley, C.M.2    Parks, J.K.3
  • 34
    • 0025829695 scopus 로고
    • pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton R., Dotti C., Bacallao R., Kurtz I., Simons K., and Prydz K. (1991) pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells. J. Cell Biol. 113, 261-274.
    • (1991) J. Cell Biol. , vol.113 , pp. 261-274
    • Parton, R.1    Dotti, C.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 35
    • 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. (1993) Neurodegeneration induced by beta-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
  • 37
    • 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. and Von Jagow G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Chem. 166, 368-379.
    • (1987) Anal. Chem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 39
    • 0028123071 scopus 로고
    • Alzheimer's disease: A central role for amyloid
    • Selkoe D. J. (1994) Alzheimer's disease: A central role for amyloid. J. Neuropathol. Exp. Neural. 53, 438-447.
    • (1994) J. Neuropathol. Exp. Neural. , vol.53 , pp. 438-447
    • Selkoe, D.J.1
  • 41
    • 0027420891 scopus 로고
    • Functional alterations in Alzheimer's disease - Diminution of cytochrome oxidase in the hippocampal formation
    • Simonian N. A. and Hyman B. T. (1993) Functional alterations in Alzheimer's disease - diminution of cytochrome oxidase in the hippocampal formation. J. Neuropath. Exp. Neural. 52, 580-585.
    • (1993) J. Neuropath. Exp. Neural. , vol.52 , pp. 580-585
    • Simonian, N.A.1    Hyman, B.T.2
  • 42
    • 0023025341 scopus 로고
    • Changes in extra- And intracellular pH in the brain during and following ischemia in hyperglycemic and in moderately hypoglycemic rats
    • Smith H. M., Hanwehr R., and Seisjo B. (1986) Changes in extra- and intracellular pH in the brain during and following ischemia in hyperglycemic and in moderately hypoglycemic rats. J. Cereb. Blood Flow Metab. 6, 574-583.
    • (1986) J. Cereb. Blood Flow Metab. , vol.6 , pp. 574-583
    • Smith, H.M.1    Hanwehr, R.2    Seisjo, B.3
  • 43
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease - Synapse loss is the major correlate of cognitive impairment
    • Terry R. D., Masliah E., Salmon D. P., Butters N., Deteresa R., Hill R., Hansen L. A., and Katzman R. (1991) Physical basis of cognitive alterations in Alzheimer's disease - synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30, 572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 44
    • 0028108931 scopus 로고
    • Mild acidosis delays hypoxic spreading depression and improves neuronal recovery in hippocampal slices
    • Tombaugh G. C. (1994) Mild acidosis delays hypoxic spreading depression and improves neuronal recovery in hippocampal slices. J. Neurosci. 14, 5635-5643.
    • (1994) J. Neurosci. , vol.14 , pp. 5635-5643
    • Tombaugh, G.C.1
  • 45
    • 0025057017 scopus 로고
    • Mild acidosis protects hippocampal neurons from injury induced by oxygen and glucose deprivation
    • Tombaugh G. C. and Sapolsky R. M. (1990) Mild acidosis protects hippocampal neurons from injury induced by oxygen and glucose deprivation. Brain Res. 506, 343-345.
    • (1990) Brain Res. , vol.506 , pp. 343-345
    • Tombaugh, G.C.1    Sapolsky, R.M.2
  • 46
    • 0028305902 scopus 로고
    • Paired helical filament tau in Alzheimers disease - The kinase connection
    • Trojanowski J. Q. and Lee V. M. Y. (1994) Paired helical filament tau in Alzheimers disease - the kinase connection. Amer. J. Pathol. 144, 449-453.
    • (1994) Amer. J. Pathol. , vol.144 , pp. 449-453
    • Trojanowski, J.Q.1    Lee, V.M.Y.2
  • 47
    • 0028058998 scopus 로고
    • Potentially amyloidogenic fragment of 50 kDa and intracellular processing of amyloid precursor protein in cells cultured under leupeptin
    • Tsuzuki K., Fukatsu R., Takamaru Y., Fujii N., and Takahata N. (1994) Potentially amyloidogenic fragment of 50 kDa and intracellular processing of amyloid precursor protein in cells cultured under leupeptin. Brain Res. 659, 213-220.
    • (1994) Brain Res. , vol.659 , pp. 213-220
    • Tsuzuki, K.1    Fukatsu, R.2    Takamaru, Y.3    Fujii, N.4    Takahata, N.5
  • 48
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A., Konig G., Bunke D., Fischer P., Salbaum J. M., Masters C. L., and Beyreuther K. (1989) Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57, 115-126.
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 49
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease
    • Yankner B., Dawes L., Fisher S., Villa-Komaroff L., Oster-Granite M., and Neve R. (1989) Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. Science 245, 417-420.
    • (1989) Science , vol.245 , pp. 417-420
    • Yankner, B.1    Dawes, L.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.5    Neve, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.