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Volumn 250, Issue 2, 1998, Pages 75-78

β-amyloid increases cathepsin D levels in hippocampus

Author keywords

Alzheimer's disease; Amyloid; Cathepsin D; Hippocampus; Lysosomes

Indexed keywords

ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ARTICLE; HIPPOCAMPUS; NEWBORN; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN LOCALIZATION; RAT;

EID: 0344505216     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(98)00364-4     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 0028171520 scopus 로고
    • Induction of β-amyloid containing polypeptides in hippocampus: Evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin
    • Bahr B.A., Abai B., Gall C.M., Vanderklish P.W., Hoffman K.B., Lynch G. Induction of β-amyloid containing polypeptides in hippocampus: evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin. Exp. Neurol. 129:1994;1-14.
    • (1994) Exp. Neurol. , vol.129 , pp. 1-14
    • Bahr, B.A.1    Abai, B.2    Gall, C.M.3    Vanderklish, P.W.4    Hoffman, K.B.5    Lynch, G.6
  • 3
    • 0032551528 scopus 로고    scopus 로고
    • Amyloid β-protein is selectively internalized by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein
    • in press
    • Bahr, B.A., Hoffman, K.B., Yang, A.J., Hess, U.S., Glabe, C.G. and Lynch, G., Amyloid β-protein is selectively internalized by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein, J. Comp. Neurol. (1998) in press.
    • (1998) J. Comp. Neurol.
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3    Hess, U.S.4    Glabe, C.G.5    Lynch, G.6
  • 4
    • 0029845397 scopus 로고    scopus 로고
    • Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L
    • Bednarski E., Lynch G. Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L. J. Neurochem. 67:1996;1846-1855.
    • (1996) J. Neurochem. , vol.67 , pp. 1846-1855
    • Bednarski, E.1    Lynch, G.2
  • 5
    • 0030905260 scopus 로고    scopus 로고
    • Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus
    • Bednarski E., Ribak C.E., Lynch G. Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus. J. Neurosci. 17:1997;4006-4021.
    • (1997) J. Neurosci. , vol.17 , pp. 4006-4021
    • Bednarski, E.1    Ribak, C.E.2    Lynch, G.3
  • 6
    • 0022841816 scopus 로고
    • Ratio of pyramidal cells versus non-pyramidal cells in the human frontal isocortex and changes in ratio with aging and Alzheimer's disease
    • Elsevier Science, New York
    • Braak, H. and Braak, E., (Eds.), Ratio of pyramidal cells versus non-pyramidal cells in the human frontal isocortex and changes in ratio with aging and Alzheimer's disease. In Progress in Brain Research, Elsevier Science, New York, 1986.
    • (1986) Progress in Brain Research
    • Braak, H.1    Braak, E.2
  • 7
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A beta 1-42, 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, A beta 1-42, 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
  • 8
    • 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., Greengard P. Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein. Proc. Natl. Acad. Sci. USA. 89:1992;2252-2256.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2252-2256
    • Caporaso, G.L.1    Gandy, S.E.2    Buxbaum, J.D.3    Greengard, P.4
  • 9
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo A.M., Nixon R.A. Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. USA. 87:1990;3861-3865.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 10
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: Evidence for a neuronal origin
    • Cataldo A.M., Thayer C.Y., Bird E.D., Wheelock T.R., Nixon R.A. Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res. 513:1990;181-192.
    • (1990) Brain Res. , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5
  • 11
    • 0029888368 scopus 로고    scopus 로고
    • Colocalization of lysosomal hydrolase and beta-amyloid in diffuse plaques of the cerebellum and striatum in Alzheimer's disease and Down's syndrome
    • Cataldo A.M., Barnett J.L., Mann D.M., Nixon R.A. Colocalization of lysosomal hydrolase and beta-amyloid in diffuse plaques of the cerebellum and striatum in Alzheimer's disease and Down's syndrome. J. Neuropathol. Exp. Neurol. 55:1996;704-715.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 704-715
    • Cataldo, A.M.1    Barnett, J.L.2    Mann, D.M.3    Nixon, R.A.4
  • 12
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • Cataldo A.M., Hamilton D.J., Barnett J.L., Paskevich P.A., Nixon R.A. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J. Neurosci. 16:1996;186-199.
    • (1996) J. Neurosci. , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 13
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde T.E., Estus S., Younkin L.H., Selkoe D.J., 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
  • 14
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • Green G.D., Shaw E. Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J. Biol. Chem. 256:1981;1923-1928.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1923-1928
    • Green, G.D.1    Shaw, E.2
  • 16
    • 0026276092 scopus 로고
    • Estimation and comparison of lysosomal and cytoplasmic pH of human fibroblasts from healthy donors and patients with lysosomal storage diseases
    • Ivleva T.S., Ogloblina T.A., Litinskaya L.L., Ya Wiederschain G. Estimation and comparison of lysosomal and cytoplasmic pH of human fibroblasts from healthy donors and patients with lysosomal storage diseases. Biomed. Sci. 2:1991;398-402.
    • (1991) Biomed. Sci. , vol.2 , pp. 398-402
    • Ivleva, T.S.1    Ogloblina, T.A.2    Litinskaya, L.L.3    Ya Wiederschain, G.4
  • 17
    • 0021675999 scopus 로고
    • Inhibitors of lysosomal enzymes: Accumulation of lipofuscin-like dense bodies in the brain
    • Ivy G., Shottler F., Wenzel J., Baudry M., Lynch G. Inhibitors of lysosomal enzymes: accumulation of lipofuscin-like dense bodies in the brain. Science. 226:1984;985-987.
    • (1984) Science , vol.226 , pp. 985-987
    • Ivy, G.1    Shottler, F.2    Wenzel, J.3    Baudry, M.4    Lynch, G.5
  • 18
    • 0024467482 scopus 로고
    • Anomalous accumulation of tau and ubiquitin immunoreactivities in rat brain caused by protease inhibition and by normal aging: A clue to PHF pathogenesis?
    • Ivy G., Kitani K., Ihara Y. Anomalous accumulation of tau and ubiquitin immunoreactivities in rat brain caused by protease inhibition and by normal aging: a clue to PHF pathogenesis? Brain Res. 489:1989;360-365.
    • (1989) Brain Res. , vol.489 , pp. 360-365
    • Ivy, G.1    Kitani, K.2    Ihara, Y.3
  • 19
    • 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., 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
  • 22
    • 0028277270 scopus 로고
    • Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-beta by cathepsin D
    • Ladror U.S., Snyder S.W., Wang G.T., Holzman T.F., Krafft G.A. Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-beta by cathepsin D. J. Biol. Chem. 269:1994;18422-18428.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18422-18428
    • Ladror, U.S.1    Snyder, S.W.2    Wang, G.T.3    Holzman, T.F.4    Krafft, G.A.5
  • 24
    • 0028323067 scopus 로고
    • Age-related changes in activities and localizations of cathepsin D, E, B and L in the rat brain tissues
    • Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T., Yamamoto K. Age-related changes in activities and localizations of cathepsin D, E, B and L in the rat brain tissues. Exp. Neurol. 126:1994;119-128.
    • (1994) Exp. Neurol. , vol.126 , pp. 119-128
    • Nakanishi, H.1    Tominaga, K.2    Amano, T.3    Hirotsu, I.4    Inoue, T.5    Yamamoto, K.6
  • 25
    • 0002348584 scopus 로고
    • The lysosomal proton pump and its effect on protein breakdown
    • H. Glaumann and F.J. Ballard (Eds.), Academic Press, London
    • Ohkuma, S., The lysosomal proton pump and its effect on protein breakdown. In H. Glaumann and F.J. Ballard (Eds.), Lysosomes: Their role in Protein Breakdown, Academic Press, London, 1987, pp. 115-148.
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 115-148
    • Ohkuma, S.1
  • 26
    • 0027052740 scopus 로고
    • Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases
    • Pliura D.H., Bonaventura B.J., Smith R.A., Coles P.J., Krantz A. Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases. Biochem. J. 288:1992;759-762.
    • (1992) Biochem. J. , vol.288 , pp. 759-762
    • Pliura, D.H.1    Bonaventura, B.J.2    Smith, R.A.3    Coles, P.J.4    Krantz, A.5
  • 27
    • 0028812394 scopus 로고
    • Elevated levels of the endosomal-lysosomal proteinase cathepsin D in cerebrospinal fluid in Alzheimer disease
    • Schwagerl A.L., Mohan P.S., Cataldo A.M., Vonsattel J.P., Kowall N.W., Nixon R.A. Elevated levels of the endosomal-lysosomal proteinase cathepsin D in cerebrospinal fluid in Alzheimer disease. J. Neurochem. 64:1995;443-446.
    • (1995) J. Neurochem. , vol.64 , pp. 443-446
    • Schwagerl, A.L.1    Mohan, P.S.2    Cataldo, A.M.3    Vonsattel, J.P.4    Kowall, N.W.5    Nixon, R.A.6
  • 28
    • 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., 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
  • 29
    • 0025805120 scopus 로고
    • A simple method for organotypic cultures of nervous tissue
    • Stoppini L., Buchs P.A., Muller D. A simple method for organotypic cultures of nervous tissue. J. Neurosci. Methods. 37:1991;173-182.
    • (1991) J. Neurosci. Methods , vol.37 , pp. 173-182
    • Stoppini, L.1    Buchs, P.A.2    Muller, D.3


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