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Volumn 216, Issue 3, 1997, Pages 429-437

Effect of Alzheimer's Brain Extracts on Dynein Immunoreactivity in PC12 Cells

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN EXTRACT; DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 0030834468     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.3181/00379727-216-44193     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0028373064 scopus 로고
    • Transmissible cerebral amyloidoses as a model for Alzheimer's disease. An ultrastructural perspective
    • Liberski PP. Transmissible cerebral amyloidoses as a model for Alzheimer's disease. An ultrastructural perspective. Mol Neurobiol 8:67-77, 1994.
    • (1994) Mol Neurobiol , vol.8 , pp. 67-77
    • Liberski, P.P.1
  • 2
    • 0026446679 scopus 로고
    • The pathology of the neuronal cytoskeleton in Alzheimer's disease
    • Brion JP. The pathology of the neuronal cytoskeleton in Alzheimer's disease. Biochim Biophys Acta 1160:134-142, 1992.
    • (1992) Biochim Biophys Acta , vol.1160 , pp. 134-142
    • Brion, J.P.1
  • 3
    • 0026298636 scopus 로고
    • Ubiquination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease
    • Iqbal K, Grundke-Iqbal I. Ubiquination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease. Mol Neurobiol 5:399-410, 1991.
    • (1991) Mol Neurobiol , vol.5 , pp. 399-410
    • Iqbal, K.1    Grundke-Iqbal, I.2
  • 4
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ. The molecular pathology of Alzheimer's disease. Neuron 6:487-498, 1991.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 5
    • 0022558388 scopus 로고
    • New perspectives on Alzheimer's disease
    • Price DL. New perspectives on Alzheimer's disease. Annu Rev Neurosci 9:489-512, 1986.
    • (1986) Annu Rev Neurosci , vol.9 , pp. 489-512
    • Price, D.L.1
  • 6
    • 0028290204 scopus 로고
    • Axonal injury and membrane alterations in Alzheimer's disease suggested by in vivo proton magnetic resonance spectroscopic imaging
    • Meyerhoff DJ, MacKay S, Constans JM, Norman D, Van Dyke C, Fein G, Weiner MW. Axonal injury and membrane alterations in Alzheimer's disease suggested by in vivo proton magnetic resonance spectroscopic imaging. Ann Neurol 36:40-47, 1994.
    • (1994) Ann Neurol , vol.36 , pp. 40-47
    • Meyerhoff, D.J.1    MacKay, S.2    Constans, J.M.3    Norman, D.4    Van Dyke, C.5    Fein, G.6    Weiner, M.W.7
  • 9
    • 0027420369 scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Goedert M. Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci 16:460-465, 1993.
    • (1993) Trends Neurosci , vol.16 , pp. 460-465
    • Goedert, M.1
  • 10
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe DJ. Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol 10:373-403, 1994.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 11
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890, 1984.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 13
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal tau
    • Lee VMY, Baline BJ, Otvos JL, Trojanowski JQ. A68: A major subunit of paired helical filaments and derivatized forms of normal tau. Science 251:675-678, 1991.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.Y.1    Baline, B.J.2    Otvos, J.L.3    Trojanowski, J.Q.4
  • 16
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (τ) is a major antigenic component of paired helical filaments in Alzheimer's disease
    • Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (τ) is a major antigenic component of paired helical filaments in Alzheimer's disease. Proc Natl Acad Sci U S A 83:4044-4048, 1986.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 18
    • 0028361538 scopus 로고
    • Alzheimer paired helical filaments. Restoration of the biological activity dephosphorylation
    • Iqbal K, Zaidi T, Bancher C, Iqbal-Grundke I. Alzheimer paired helical filaments. Restoration of the biological activity dephosphorylation. FEBS Lett 349:104-108, 1994.
    • (1994) FEBS Lett , vol.349 , pp. 104-108
    • Iqbal, K.1    Zaidi, T.2    Bancher, C.3    Iqbal-Grundke, I.4
  • 19
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function
    • Holzbaur ELF, Vallee RB. Dyneins: Molecular structure and cellular function. Annu Rev Cell Biol 10:339-372, 1994.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 339-372
    • Holzbaur, E.L.F.1    Vallee, R.B.2
  • 20
    • 0023608935 scopus 로고
    • MAP1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal BM, Shpeter HS, Vallee RB. MAP1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol 105:1273-1282, 1987.
    • (1987) J Cell Biol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpeter, H.S.2    Vallee, R.B.3
  • 21
    • 0022385727 scopus 로고
    • Identification of a novel force generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Scheetz MP. Identification of a novel force generating protein, kinesin, involved in microtubule-based motility. Cell 42:39-50, 1985.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Scheetz, M.P.3
  • 22
    • 0026601916 scopus 로고
    • Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells
    • Lin SXH, Collins CA. Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells. J Cell Sci 101:125-137, 1992.
    • (1992) J Cell Sci , vol.101 , pp. 125-137
    • Lin, S.X.H.1    Collins, C.A.2
  • 23
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the golgi complex
    • Corthesy-Theulaz I, Pauloin A, Pfeffer SR. Cytoplasmic dynein participates in the centrosomal localization of the golgi complex. J Cell Biol 118:1333-1345, 1992.
    • (1992) J Cell Biol , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 24
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F, Emans N, Griffiths G, Gruenburg J. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol 123:1373-1387, 1993.
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenburg, J.4
  • 25
    • 0028343929 scopus 로고
    • Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans
    • Xiang X, Beckwith SM, Morris NR. Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans. Proc Natl Acad Sci U S A 91:2100-2104, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2100-2104
    • Xiang, X.1    Beckwith, S.M.2    Morris, N.R.3
  • 26
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong C-X, Singh TJ, Grundle-Iqbal I, Iqbal K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J Neurochem 61:921-927, 1993.
    • (1993) J Neurochem , vol.61 , pp. 921-927
    • Gong, C.-X.1    Singh, T.J.2    Grundle-Iqbal, I.3    Iqbal, K.4
  • 27
    • 0028339544 scopus 로고
    • Attenuated protein kinase C activity and translocation in Alzheimer's disease brain
    • Wang H-Y, Pisano MR, Friedman E. Attenuated protein kinase C activity and translocation in Alzheimer's disease brain. Neurobiol Aging 15:293-298, 1994.
    • (1994) Neurobiol Aging , vol.15 , pp. 293-298
    • Wang, H.-Y.1    Pisano, M.R.2    Friedman, E.3
  • 28
    • 0345704610 scopus 로고
    • Establishment of noradrenergic clonal line of rat adrenal pheochromocytoma cells which responds to nerve growth factor
    • Greene LA, Tischler AS. Establishment of noradrenergic clonal line of rat adrenal pheochromocytoma cells which responds to nerve growth factor. Proc Natl Acad Sci U S A 73:2424-2428, 1976.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 29
    • 0026092049 scopus 로고
    • Transmitter, ion channel and receptor properties of pheochromocytoma (PC12) cells: A model for neurotoxicological studies
    • Shafer TJ, Atchison WD. Transmitter, ion channel and receptor properties of pheochromocytoma (PC12) cells: A model for neurotoxicological studies. Neurotoxicology 12:473-492, 1991.
    • (1991) Neurotoxicology , vol.12 , pp. 473-492
    • Shafer, T.J.1    Atchison, W.D.2
  • 30
    • 0028003725 scopus 로고
    • Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients
    • Ulloa L, Montejo de Garcini E, Gomez-Ramos P, Moran MA, Avila J. Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients. Brain Res Mol Brain Res 26:113-122, 1994.
    • (1994) Brain Res Mol Brain Res , vol.26 , pp. 113-122
    • Ulloa, L.1    Montejo de Garcini, E.2    Gomez-Ramos, P.3    Moran, M.A.4    Avila, J.5
  • 31
    • 0020600266 scopus 로고
    • Fluorometric quantification of DNA in cells and tissue
    • Downs TR, Wilfinger WW. Fluorometric quantification of DNA in cells and tissue. Anal Biochem 131:538-547, 1983.
    • (1983) Anal Biochem , vol.131 , pp. 538-547
    • Downs, T.R.1    Wilfinger, W.W.2
  • 32
    • 0022262165 scopus 로고
    • A simplified in situ solubilization procedure for the determination of DNA and cell number in tissue cultured mammalian cells
    • West DC, Sattar A, Kumar S. A simplified in situ solubilization procedure for the determination of DNA and cell number in tissue cultured mammalian cells. Anal Biochem 147:289-295, 1985.
    • (1985) Anal Biochem , vol.147 , pp. 289-295
    • West, D.C.1    Sattar, A.2    Kumar, S.3
  • 33
    • 0025320820 scopus 로고
    • Localization of cytoplasmic dynein to mitotic spindles and kinetochores
    • Steuer ER, Wordeman TA, Schroer TA, Sheetz MP. Localization of cytoplasmic dynein to mitotic spindles and kinetochores. Nature 345:266-268, 1990.
    • (1990) Nature , vol.345 , pp. 266-268
    • Steuer, E.R.1    Wordeman, T.A.2    Schroer, T.A.3    Sheetz, M.P.4
  • 34
    • 0024512777 scopus 로고
    • Neurotrophic action of Alzheimer's disease brain extract is due to the loss of inhibitory factors for survival and neurite formation of cerebral cortical neurons
    • Uchida Y, Tomonaga M. Neurotrophic action of Alzheimer's disease brain extract is due to the loss of inhibitory factors for survival and neurite formation of cerebral cortical neurons. Brain Res 481:190-193, 1989.
    • (1989) Brain Res , vol.481 , pp. 190-193
    • Uchida, Y.1    Tomonaga, M.2
  • 36
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications. Proc Natl Acad Sci USA 76:4350-4354, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 37
    • 0030066783 scopus 로고    scopus 로고
    • Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia
    • Pfister KK, Salata MW, Dillman JF, Vaughan KT, Vallee RB, Torre E, Lye RJ. Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia. J Biol Chem 271:1687-1694, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 1687-1694
    • Pfister, K.K.1    Salata, M.W.2    Dillman, J.F.3    Vaughan, K.T.4    Vallee, R.B.5    Torre, E.6    Lye, R.J.7
  • 38
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW. Neu- rodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J Neurosci 13:1676-1687, 1993.
    • (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
  • 40
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman MS, Ragan CI, Iversen LL. Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc Natl Acad Sci U S A 91:1470-1474, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 42
    • 0029022112 scopus 로고
    • Nerve growth factor in Alzheimer's disease: Increased levels throughout the brain coupled with declines in nucleus basalis
    • Scott AS, Mufson EJ, Weingartner JA, Skau KA, Crutcher KA. Nerve growth factor in Alzheimer's disease: Increased levels throughout the brain coupled with declines in nucleus basalis. J Neurosci 15:6213-6221, 1995.
    • (1995) J Neurosci , vol.15 , pp. 6213-6221
    • Scott, A.S.1    Mufson, E.J.2    Weingartner, J.A.3    Skau, K.A.4    Crutcher, K.A.5
  • 43
    • 0028129444 scopus 로고
    • NGF mRNA is not decreased in frontal cortex from Alzheimer disease patients
    • Jette N, Cole MS, Fahnestock M. NGF mRNA is not decreased in frontal cortex from Alzheimer disease patients. Brain Res Mol Brain Res 25:242-250, 1994.
    • (1994) Brain Res Mol Brain Res , vol.25 , pp. 242-250
    • Jette, N.1    Cole, M.S.2    Fahnestock, M.3
  • 44
    • 0027427608 scopus 로고
    • Quantitation of subnanomolar amounts of phosphate bound to seryl and threonyl residues in phosphoproteins using alkaline hydrolysis and malachite green
    • Ekman P, Jager O. Quantitation of subnanomolar amounts of phosphate bound to seryl and threonyl residues in phosphoproteins using alkaline hydrolysis and malachite green. Anal Biochem 214:138-141, 1993.
    • (1993) Anal Biochem , vol.214 , pp. 138-141
    • Ekman, P.1    Jager, O.2
  • 45
    • 77957004737 scopus 로고
    • Protein fractionation on the basis of solubility in aqueous solutions of salts and organic solvents
    • Green AA, Hughes WL. Protein fractionation on the basis of solubility in aqueous solutions of salts and organic solvents. Methods Enzymol 1:67-90, 1955.
    • (1955) Methods Enzymol , vol.1 , pp. 67-90
    • Green, A.A.1    Hughes, W.L.2


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