메뉴 건너뛰기




Volumn 66, Issue 5, 1996, Pages 2034-2040

Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein

Author keywords

Alzheimer's disease; C terminal fragment (CT105); Ca2+ influx; Internal injection; Ion channel formation; Toxicity; Two electrode voltage clamp; Xenopus oocytes; Amyloid precursor protein

Indexed keywords

AMYLOID BETA PROTEIN; PROTEIN PRECURSOR;

EID: 0029923244     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66052034.x     Document Type: Article
Times cited : (50)

References (48)
  • 1
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes
    • Arispe N., Pollard H. B., and Rojas E. (1993a) Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [(AβP-(1-40)] in bilayer membranes. Proc. Natl. Acad. Sci. USA 90, 10573-10577.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 2
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by trimethamine and aluminium
    • Arispe N., Rojas E., and Pollard H. B. (1993b) Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: blockade by trimethamine and aluminium. Proc. Natl. Acad. Sci. USA 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 3
    • 0023086182 scopus 로고
    • Damage to mammalian cells by proteins that form transmembrane pores
    • Bhakdi S. and Tranum-Jensen J. (1987) Damage to mammalian cells by proteins that form transmembrane pores. Rev. Physiol. Biochem. Pharmacol. 107, 147-210.
    • (1987) Rev. Physiol. Biochem. Pharmacol. , vol.107 , pp. 147-210
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 4
    • 0028351412 scopus 로고
    • Bacterial expression, purification of full length and carboxyl terminal fragments of Alzheimer precursor protein and their proteolytic processing by thrombin
    • Chong Y. H., Jung J. M., Choi W., Park C. H., Choi K. S., and Suh Y.-H. (1994) Bacterial expression, purification of full length and carboxyl terminal fragments of Alzheimer precursor protein and their proteolytic processing by thrombin. Life Sci. 54, 1259-1268.
    • (1994) Life Sci. , vol.54 , pp. 1259-1268
    • Chong, Y.H.1    Jung, J.M.2    Choi, W.3    Park, C.H.4    Choi, K.S.5    Suh, Y.-H.6
  • 5
    • 0021287107 scopus 로고
    • Xenopus oocyte resting potential, muscarinic responses and the role of calcium and guanosine 3′,5′-cyclic monophosphate
    • Dascal N., Landau E. M., and Lass Y. (1984) Xenopus oocyte resting potential, muscarinic responses and the role of calcium and guanosine 3′,5′-cyclic monophosphate. J. Physiol. (Lond.) 352, 551-574.
    • (1984) J. Physiol. (Lond.) , vol.352 , pp. 551-574
    • Dascal, N.1    Landau, E.M.2    Lass, Y.3
  • 8
    • 0026730350 scopus 로고
    • Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks T., Dyrks E., Hartmann T., Masters C., and Beyreuther K. (1992) Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J. Biol. Chem. 267, 18210-18217.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, T.3    Masters, C.4    Beyreuther, K.5
  • 9
    • 0028067212 scopus 로고
    • Dendritic pathology of granule cells in Alzheimer's disease is unrelated to neuritic plaques
    • Einstein G., Buranosky R., and Crain B. J. (1994) Dendritic pathology of granule cells in Alzheimer's disease is unrelated to neuritic plaques. J. Neurosci. 14, 5077-5088.
    • (1994) J. Neurosci. , vol.14 , pp. 5077-5088
    • Einstein, G.1    Buranosky, R.2    Crain, B.J.3
  • 13
    • 0000456112 scopus 로고
    • Xenopus oocytes: Endogenous electrophysiological characteristics
    • (Osborne N., ed), Macmillan Press, London
    • Fraser S. P. and Djamgoz M. B. A. (1992) Xenopus oocytes: endogenous electrophysiological characteristics, in Current Aspects of the Neurosciences, Vol. 4 (Osborne N., ed), pp. 267-315. Macmillan Press, London.
    • (1992) Current Aspects of the Neurosciences , vol.4 , pp. 267-315
    • Fraser, S.P.1    Djamgoz, M.B.A.2
  • 14
    • 0001962260 scopus 로고
    • Electrophysiology of Xenopus oocytes: An expression system in molecular neurobiology
    • (Wallis D. I., ed), Oxford University Press, Oxford
    • Fraser S. P., Moon C., and Djamgoz M. B. A. (1993) Electrophysiology of Xenopus oocytes: an expression system in molecular neurobiology, in Electrophysiology, a Practical Approach (Wallis D. I., ed), pp. 65-86. Oxford University Press, Oxford.
    • (1993) Electrophysiology, a Practical Approach , pp. 65-86
    • Fraser, S.P.1    Moon, C.2    Djamgoz, M.B.A.3
  • 15
    • 15844389207 scopus 로고
    • The C-terminal fragment of the Alzheimer's disease β-amyloid precursor protein is a potent inducer of membrane currents in Xenopus oocytes
    • Fraser S. P., Suh Y.-H., Chong Y. H., and Djamgoz M. B. A. (1995) The C-terminal fragment of the Alzheimer's disease β-amyloid precursor protein is a potent inducer of membrane currents in Xenopus oocytes. (Abstr.) J. Physiol. (Lond.) 489, 66P.
    • (1995) J. Physiol. (Lond.) , vol.489
    • Fraser, S.P.1    Suh, Y.-H.2    Chong, Y.H.3    Djamgoz, M.B.A.4
  • 16
    • 0026468207 scopus 로고
    • Expression of a carboxy-terminal region of the β-amyloid precursor protein in a heterogeneous culture of neuroblastoma cells: Evidence for altered processing and selective neurotoxicity
    • Fukuchi K.-I., Kamino K., Deeb S. S., Furlong C. E., Sundstrom J. A., Smith A. C., and Martin G. M. (1992) Expression of a carboxy-terminal region of the β-amyloid precursor protein in a heterogeneous culture of neuroblastoma cells: evidence for altered processing and selective neurotoxicity Mol. Brain Res. 16, 37-46.
    • (1992) Mol. Brain Res. , vol.16 , pp. 37-46
    • Fukuchi, K.-I.1    Kamino, K.2    Deeb, S.S.3    Furlong, C.E.4    Sundstrom, J.A.5    Smith, A.C.6    Martin, G.M.7
  • 18
    • 0028037404 scopus 로고
    • Amyloid β protein-induced irreversible currents in rat cortical neurones
    • Furukawa K., Abe Y., and Akaike N. (1994) Amyloid β protein-induced irreversible currents in rat cortical neurones. Neuroreport 5, 2016-2018.
    • (1994) Neuroreport , vol.5 , pp. 2016-2018
    • Furukawa, K.1    Abe, Y.2    Akaike, N.3
  • 20
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic carboxyl-terminal derivatives
    • Golde T. E., Estus S., Younkin L. H., Selkoe D. J., and Younkin S. G. (1992) Processing of the amyloid protein precursor to potentially amyloidogenic carboxyl-terminal derivatives. Science 255, 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
  • 22
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C., Koo E. H., Mellon A., Hung A. Y., and Selkoe D. (1992a) Targeting of cell-surface β-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.5
  • 24
    • 0028298389 scopus 로고
    • Apolipoprotein E and cholesterol affect neuronal calcium signalling: The possible relationship to beta-amyloid neurotoxicity
    • Hartmann H., Eckert A., and Muller W. E. (1994) Apolipoprotein E and cholesterol affect neuronal calcium signalling: the possible relationship to beta-amyloid neurotoxicity. Biochem. Biophys. Res. Commun. 200, 1185-1192.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1185-1192
    • Hartmann, H.1    Eckert, A.2    Muller, W.E.3
  • 25
    • 0026699985 scopus 로고
    • Protease inhibitors generate cytotoxic fragments from Alzheimer amyloid protein precursor in cDNA transfected glioma cells
    • Hayashi Y., Kashiwagi K., and Yoshikawa K. (1992) Protease inhibitors generate cytotoxic fragments from Alzheimer amyloid protein precursor in cDNA transfected glioma cells. Biochem. Biophys. Res. Commun. 187, 1249-1255.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1249-1255
    • Hayashi, Y.1    Kashiwagi, K.2    Yoshikawa, K.3
  • 27
    • 0024447098 scopus 로고
    • Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease
    • Joachim C. L., Morris J. H., and Selkoe D. J. (1989) Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease. Am. J. Pathol. 135, 309-319.
    • (1989) Am. J. Pathol. , vol.135 , pp. 309-319
    • Joachim, C.L.1    Morris, J.H.2    Selkoe, D.J.3
  • 28
    • 0027934516 scopus 로고
    • Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain
    • Kametani F., Tanaka K., Tokuda T., and Ikeda S.-I. (1994) Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain. FEBS Lett. 351, 165-167.
    • (1994) FEBS Lett. , vol.351 , pp. 165-167
    • Kametani, F.1    Tanaka, K.2    Tokuda, T.3    Ikeda, S.-I.4
  • 29
    • 0025133329 scopus 로고
    • Formation of amyloid-like fibrils in COS cells overexpressing part of the Alzheimer amyloid protein precursor
    • Maruyama K., Terakado K., Usami M., and Yoshikawa K. (1990) Formation of amyloid-like fibrils in COS cells overexpressing part of the Alzheimer amyloid protein precursor. Nature 347, 566-569.
    • (1990) Nature , vol.347 , pp. 566-569
    • Maruyama, K.1    Terakado, K.2    Usami, M.3    Yoshikawa, K.4
  • 30
    • 0028014381 scopus 로고
    • Altered processing characteristics of β amyloid-containing peptides in cytosol and media of familial Alzheimer's disease cells
    • Matsumoto A. (1994) Altered processing characteristics of β amyloid-containing peptides in cytosol and media of familial Alzheimer's disease cells. Biochim. Biophys. Acta 1225, 304-310.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 304-310
    • Matsumoto, A.1
  • 32
    • 0021646375 scopus 로고
    • Chloride currents induced by injection of calcium into Xenopus oocytes
    • Miledi R. and Parker I. (1984) Chloride currents induced by injection of calcium into Xenopus oocytes. J. Physiol. (Lond.) 357, 173-183.
    • (1984) J. Physiol. (Lond.) , vol.357 , pp. 173-183
    • Miledi, R.1    Parker, I.2
  • 33
    • 0026568638 scopus 로고
    • Brain transplants of cells expressing the carboxyl-terminal fragment of the Alzheimer amyloid protein precursor cause specific neurotoxicity in vivo
    • Neve R. L., Kammesheidt A., and Hohmann C. F. (1992) Brain transplants of cells expressing the carboxyl-terminal fragment of the Alzheimer amyloid protein precursor cause specific neurotoxicity in vivo. Proc. Natl. Acad. Sci. USA 89, 3448-3452.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3448-3452
    • Neve, R.L.1    Kammesheidt, A.2    Hohmann, C.F.3
  • 35
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the β-amyloid precursor protein
    • Selkoe D. J. (1994) Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17, 489-517.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 37
    • 0027166738 scopus 로고
    • Amyloid β-peptides act directly on single neurons
    • Simmons M. A. and Schneider C. R. (1993) Amyloid β-peptides act directly on single neurons. Neurosci. Lett. 150, 133-136.
    • (1993) Neurosci. Lett. , vol.150 , pp. 133-136
    • Simmons, M.A.1    Schneider, C.R.2
  • 38
    • 0026558595 scopus 로고
    • Identification of a stable fragment of the Alzheimer amyloid precursor containing the β-protein in brain microvessels
    • Tamaoka A., Kalaria R. N., Lieberburg I., and Selkoe D. J. (1992) Identification of a stable fragment of the Alzheimer amyloid precursor containing the β-protein in brain microvessels. Proc. Natl. Acad. Sci. USA 89, 1345-1349.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1345-1349
    • Tamaoka, A.1    Kalaria, R.N.2    Lieberburg, I.3    Selkoe, D.J.4
  • 39
    • 0028180304 scopus 로고
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurones in culture
    • 2+ channel blockers attenuate β-amyloid peptide toxicity to cortical neurones in culture. J. Neurochem. 62, 372-375.
    • (1994) J. Neurochem. , vol.62 , pp. 372-375
    • Weiss, J.H.1    Pike, C.J.2    Cotman, C.W.3
  • 40
    • 0024543836 scopus 로고
    • Amyloid β protein enhances survival of hippocampal neurons in vitro
    • Whitson J. S., Selkoe D. J., and Cotman C. W. (1989) Amyloid β protein enhances survival of hippocampal neurons in vitro. Science 243, 1488-1490.
    • (1989) Science , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 41
    • 0025095256 scopus 로고
    • β-Amyloid protein promotes neuritic branching in hippocampal cultures
    • Whitson J. S., Glabe C. G., Shintani E., Abcar A., and Cotman C. W. (1990) β-Amyloid protein promotes neuritic branching in hippocampal cultures Neurosci. Lett. 110, 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
  • 42
    • 0025316164 scopus 로고
    • Identification and characterization of C-terminal fragments of the amyloid β-amyloid precursor produced in cell culture
    • Wolf D., Quon D., Wang Y., and Cordell B. (1990) Identification and characterization of C-terminal fragments of the amyloid β-amyloid precursor produced in cell culture. EMBO J. 9, 2079-2084.
    • (1990) EMBO J. , vol.9 , pp. 2079-2084
    • Wolf, D.1    Quon, D.2    Wang, Y.3    Cordell, B.4
  • 43
    • 0025676531 scopus 로고
    • Characterization of stretch-activated ion channels in Xenopus oocytes
    • Yang X.-C. and Sachs F. (1990) Characterization of stretch-activated ion channels in Xenopus oocytes. J. Physiol. (Lond.) 431, 103-122.
    • (1990) J. Physiol. (Lond.) , vol.431 , pp. 103-122
    • Yang, X.-C.1    Sachs, F.2
  • 44
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor protein associated with Alzheimer's disease
    • Yankner B. A., Dawes L. R., Fisher S., Villa-Komaroff L., Oster-Granite M. L., and Neve R. L. (1989) Neurotoxicity of a fragment of the amyloid precursor protein associated with Alzheimer's disease. Science 245, 417-420.
    • (1989) Science , vol.245 , pp. 417-420
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villa-Komaroff, L.4    Oster-Granite, M.L.5    Neve, R.L.6
  • 45
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner B. A., Duffy L. K., and Kirscher D. A. (1990) Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250, 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirscher, D.A.3
  • 46
    • 0026779680 scopus 로고
    • Degeneration in vitro of post-mitotic neurons overexpressing the Alzheimer amyloid protein precursor
    • Yoshikawa K., Aizawa T., and Hayashi Y. (1992) Degeneration in vitro of post-mitotic neurons overexpressing the Alzheimer amyloid protein precursor. Nature 359, 64-67.
    • (1992) Nature , vol.359 , pp. 64-67
    • Yoshikawa, K.1    Aizawa, T.2    Hayashi, Y.3
  • 47
    • 0022558797 scopus 로고
    • Mechanism of membrane damage mediated by human eosinophil cationic protein
    • Young J. D., Peterson C. G. B., Venge P., and Conn Z. A. (1986) Mechanism of membrane damage mediated by human eosinophil cationic protein. Nature 321, 613-616.
    • (1986) Nature , vol.321 , pp. 613-616
    • Young, J.D.1    Peterson, C.G.B.2    Venge, P.3    Conn, Z.A.4
  • 48
    • 0023635124 scopus 로고
    • Family study of platelet membrane fluidity in Alzheimer's disease
    • Zubenko G. S., Wusylko M., Cohen B. M., Baller F., and Teply I. (1987) Family study of platelet membrane fluidity in Alzheimer's disease. Science 238, 539-542.
    • (1987) Science , vol.238 , pp. 539-542
    • Zubenko, G.S.1    Wusylko, M.2    Cohen, B.M.3    Baller, F.4    Teply, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.