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Volumn 4, Issue 11, 1998, Pages 715-723

Post-transcriptional contribution of a cAMP-dependent pathway to the formation of α- and β/y-secretases-derived products of βAPP maturation in human cells expressing wildtype and swedish mutated βAPP

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BUCLADESINE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; DACTINOMYCIN; FORSKOLIN; PROTEIN KINASE C;

EID: 0032436113     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf03401766     Document Type: Article
Times cited : (32)

References (34)
  • 1
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, AIlsop D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12: 383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Ailsop, D.2
  • 2
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120: 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the beta-amyloid precursor protein
    • Selkoe DJ. (1994) Normal and abnormal biology of the beta-amyloid precursor protein. Annu. Rev. Neurosci. 17: 489-517.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 5
    • 0029379605 scopus 로고
    • Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler F. (1995) Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65: 1431-1444.
    • (1995) J. Neurochem. , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 6
    • 0028981466 scopus 로고
    • Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses
    • Maury CPJ. (1995) Molecular pathogenesis of β-amyloidosis in Alzheimer's disease and other cerebral amyloidoses. Lab. Invest. 72: 4-16.
    • (1995) Lab. Invest. , vol.72 , pp. 4-16
    • Cpj, M.1
  • 7
    • 0025295039 scopus 로고
    • Cleavage of amyloid β peptide during constitutive processing of its precursor
    • Esch FS, Keim PS, Beattie EC, et al. (1990) Cleavage of amyloid β peptide during constitutive processing of its precursor. Science 248: 1122-1128.
    • (1990) Science , vol.248 , pp. 1122-1128
    • Esch, F.S.1    Keim, P.S.2    Beattie, E.C.3
  • 8
    • 0026721943 scopus 로고
    • Proc
    • Sisodia S. (1992) β-amyloid precursor protein cleavage by a membrane-bound protease. Proc. Natl. Acad. Sci. U.S.A. 89: 6075-6079.
    • (1992) Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6075-6079
    • Sisodia, S.1
  • 10
    • 0026662356 scopus 로고
    • Secretory processing of the Alzheimer amyloid β/A4 protein precursor is increased by protein phosphorylation
    • Gillespie S, Golde TE, Younkin SG. (1992) Secretory processing of the Alzheimer amyloid β/A4 protein precursor is increased by protein phosphorylation. Biochem. Biophys. Res. Commun. 187: 1285-1290.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1285-1290
    • Gillespie, S.1    Golde, T.E.2    Younkin, S.G.3
  • 11
    • 0027435535 scopus 로고
    • Protein phosphorylation inhibits production of Alzheimer amyloid β/A4 peptide
    • Buxbaum JD, Koo EH, Greengard P. (1993) Protein phosphorylation inhibits production of Alzheimer amyloid β/A4 peptide. Proc. Natl. Acad. Sci. U.S.A. 90: 9195-9198.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9195-9198
    • Buxbaum, J.D.1    Koo, E.H.2    Greengard, P.3
  • 12
    • 0027453490 scopus 로고
    • Activation of protein kinase C inhibits cellular production of the amyloid β-protein
    • Hung AY, Haass C, Nitsch RM, et al. (1993) Activation of protein kinase C inhibits cellular production of the amyloid β-protein. J. Biol. Chem. 268: 22959-22962.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22959-22962
    • Hung, A.Y.1    Haass, C.2    Nitsch, R.M.3
  • 13
    • 0029805807 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the proteasome: A contribution to the a-secretase pathway in human cells
    • Marambaud P, Wilk S, Checler F. (1996) Protein kinase A phosphorylation of the proteasome: a contribution to the a-secretase pathway in human cells. J. Neurochem. 67: 2616-2619.
    • (1996) J. Neurochem. , vol.67 , pp. 2616-2619
    • Marambaud, P.1    Wilk, S.2    Checler, F.3
  • 14
    • 0029863203 scopus 로고    scopus 로고
    • Metabolism of Alzheimer β-amyloid precursor protein: Regulation by protein kinase A in intact cells and in cell-free system
    • Xu H, Sweeney D, Greengard P, Gandy S. (1996) Metabolism of Alzheimer β-amyloid precursor protein: regulation by protein kinase A in intact cells and in cell-free system. Proc. Natl. Acad. Sci. U.S.A. 93: 4081-4084.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4081-4084
    • Xu, H.1    Sweeney, D.2    Greengard, P.3    Gandy, S.4
  • 15
    • 0029993598 scopus 로고    scopus 로고
    • Two types of amyloid precursor protein (APP) mRNA in rat glioma cell lines: Upregulation via a cyclic AMP-dependent pathway
    • 1. Gegelashvili G, Bock E, Schousboe A, Linnemann D. (1996) Two types of amyloid precursor protein (APP) mRNA in rat glioma cell lines: upregulation via a cyclic AMP-dependent pathway. Mol. Brain. Res. 37: 151-156.
    • (1996) Mol. Brain. Res. , vol.37 , pp. 151-156
    • Gegelashvili, G.1    Bock, E.2    Schousboe, A.3    Linnemann, D.4
  • 16
    • 0031032434 scopus 로고    scopus 로고
    • Enhanced expression of amyloid precursor protein in response to dibutyryl cyclic AMP is not mediated by the transcription factor AP-2
    • Bourbonnière M, Shekarabi M, Nalbantoglu J. (1997) Enhanced expression of amyloid precursor protein in response to dibutyryl cyclic AMP is not mediated by the transcription factor AP-2. J. Neurochem. 68: 909-916.
    • (1997) J. Neurochem. , vol.68 , pp. 909-916
    • Bourbonnière, M.1    Shekarabi, M.2    Nalbantoglu, J.3
  • 17
    • 0031024889 scopus 로고    scopus 로고
    • Transcriptional regulation of amyloid precursor protein during dibutyryl cyclic AMP-induced differentiation of NG108-15 cells
    • Shekarahi M, Bourbonnière M, Dagenais A, Nalbantoglu J. (1997) Transcriptional regulation of amyloid precursor protein during dibutyryl cyclic AMP-induced differentiation of NG108-15 cells. J. Neurochem. 68: 970-978.
    • (1997) J. Neurochem. , vol.68 , pp. 970-978
    • Shekarahi, M.1    Bourbonnière, M.2    Dagenais, A.3    Nalbantoglu, J.4
  • 18
    • 0030924310 scopus 로고    scopus 로고
    • Stimulation of amyloid precursor protein synthesis by adrenergic receptors coupled to cAMP formation
    • Lee RKK, Araki W, Wurtman RJ. (1997) Stimulation of amyloid precursor protein synthesis by adrenergic receptors coupled to cAMP formation. Proc. N all. Acad. Sci. U.S.A. 94: 5422-5426.
    • (1997) Proc. N All. Acad. Sci. U.S.A. , vol.94 , pp. 5422-5426
    • Rkk, L.1    Araki, W.2    Wurtman, R.J.3
  • 19
    • 0031022252 scopus 로고    scopus 로고
    • Proteasome contributes to the a-secretase pathway of amyloid precursor protein in human cells
    • Marambaud P, Chevallier N, Barelli H, Wilk S, Glieder F. (1997) Proteasome contributes to the a-secretase pathway of amyloid precursor protein in human cells. J. Neurochem, 68: 698-703.
    • (1997) J. Neurochem , vol.68 , pp. 698-703
    • Marambaud, P.1    Chevallier, N.2    Barelli, H.3    Wilk, S.4    Glieder, F.5
  • 20
    • 0031001110 scopus 로고    scopus 로고
    • Examination of the role of endopeptidase 3.4.24.15 in Aβ secretion by human transfected cells
    • Chevallier N, Jiracek J, Vincent B, et al. (1997) Examination of the role of endopeptidase 3.4.24.15 in Aβ secretion by human transfected cells. Er. J. Pharmacol. 121: 556-562.
    • (1997) Er. J. Pharmacol. , vol.121 , pp. 556-562
    • Chevallier, N.1    Jiracek, J.2    Vincent, B.3
  • 21
    • 0029893183 scopus 로고    scopus 로고
    • Clonal cell lines produced by infection of neocortical neuroblasts using multiple oncogenes transduced by retroviruses
    • Chun J, Jaenisch R. (1996) Clonal cell lines produced by infection of neocortical neuroblasts using multiple oncogenes transduced by retroviruses. Mol. Cell. Neurosd. 7: 304-321.
    • (1996) Mol. Cell. Neurosd. , vol.7 , pp. 304-321
    • Chun, J.1    Jaenisch, R.2
  • 22
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N, Johannes H, Pantel J, et al. (1996) Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271: 22908-22914.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22908-22914
    • Ida, N.1    Johannes, H.2    Pantel, J.3
  • 23
    • 0030667097 scopus 로고    scopus 로고
    • Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's β amyloid precursor protein: Different control of early and late events by the proteasome
    • Marambaud P, Lopez-Perez E, Wilk S, Checler F. (1997) Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's β amyloid precursor protein: different control of early and late events by the proteasome. J. Neurochem. 69: 2500-2505.
    • (1997) J. Neurochem. , vol.69 , pp. 2500-2505
    • Marambaud, P.1    Lopez-Perez, E.2    Wilk, S.3    Checler, F.4
  • 24
    • 14444267540 scopus 로고    scopus 로고
    • Characterization of new polyclonal antibodies specific for 40 and 42 aminoacid-long amyloid β peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases
    • Barelli H, Lebeau A, Vizzavona J, et al. (1997) Characterization of new polyclonal antibodies specific for 40 and 42 aminoacid-long amyloid β peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases. Mol. Med. 3: 695-707.
    • (1997) Mol. Med. , vol.3 , pp. 695-707
    • Barelli, H.1    Lebeau, A.2    Vizzavona, J.3
  • 25
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid β protein by normal proteolytic processing
    • Shoji M, Golde TE, Ghiso J, et al. (1992) Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 258: 126-129.
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1    Golde, T.E.2    Ghiso, J.3
  • 26
    • 0028892096 scopus 로고
    • Production of intracellular amyloid-containing fragments in hippocampal neurons expressing human amyloid precursor protein and protection against amyloidogenesis by subtle amino acid substitutions in the rodent sequence
    • De Strooper B, Simons M, Multhaup G, Van Leuven F, Beyreuther K, Dotti CG. (1995) Production of intracellular amyloid-containing fragments in hippocampal neurons expressing human amyloid precursor protein and protection against amyloidogenesis by subtle amino acid substitutions in the rodent sequence. EMBO J. 14: 4932-4938.
    • (1995) EMBO J. , vol.14 , pp. 4932-4938
    • De Strooper, B.1    Simons, M.2    Multhaup, G.3    Van Leuven, F.4    Beyreuther, K.5    Dotti, C.G.6
  • 27
    • 0031946864 scopus 로고    scopus 로고
    • Estrogen reduces neuronal generation of Alzheimer β-amyloid peptides
    • Xu H, Gouras GK, Greenfield JP, et al. (1998) Estrogen reduces neuronal generation of Alzheimer β-amyloid peptides. Nat. Med. 4: 447-451.
    • (1998) Nat. Med. , vol.4 , pp. 447-451
    • Xu, H.1    Gouras, G.K.2    Greenfield, J.P.3
  • 28
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway
    • Haass C, Lemere CA, Capell A, et al. (1995) The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway. Nat. Med. 1: 1291-1296.
    • (1995) Nat. Med. , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3
  • 29
    • 0030273117 scopus 로고    scopus 로고
    • Direct modulation of the secretory machinery underlies PKA-dependent synaptic facilitation in hippocampal neurons
    • Trudeau L-E, Emery DG, Haydon PG. (1996) Direct modulation of the secretory machinery underlies PKA-dependent synaptic facilitation in hippocampal neurons. Neuron 17: 789-797.
    • (1996) Neuron , vol.17 , pp. 789-797
    • Trudeau, L.-E.1    Emery, D.G.2    Haydon, P.G.3
  • 30
    • 33748274442 scopus 로고    scopus 로고
    • Protein kinase A inhibitors drastically reduce constitutive production of Aβ40 and Aβ42 by human cells expressing normal and familial Alzheimer's disease-linked mutated βAPP and presenilin 1
    • in Press
    • Marambaud P, Ancolio K, Alves da Costa, C, and Checler F. ( 1998) Protein kinase A inhibitors drastically reduce constitutive production of Aβ40 and Aβ42 by human cells expressing normal and familial Alzheimer's disease-linked mutated βAPP and presenilin 1. Brit. J. Pharmacol. (in press).
    • (1998) Brit. J. Pharmacol
    • Marambaud, P.1    Ancolio, K.2    Costa, A.D.3    Checler, F.4
  • 31
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compatment of NT2N cells
    • Cook DG, Forman MS, Sung JC, et al. (1997) Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compatment of NT2N cells. Nat. Med. 3: 1021-1023.
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3
  • 32
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides
    • Hartmann T, Bieger SC, Brühl B, et al. (1997) Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides. Nat. Med. 3: 1016-1020.
    • (1997) Nat. Med. , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Brühl, B.3
  • 33
    • 0031950118 scopus 로고    scopus 로고
    • Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and trigger increased Aβ42 secretion by human cells
    • Marambaud P, Ancolio K, Lopez-Perez E, Checler F. (1998) Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and trigger increased Aβ42 secretion by human cells. Mol. Med. 4: 146-156.
    • (1998) Mol. Med. , vol.4 , pp. 146-156
    • Marambaud, P.1    Ancolio, K.2    Lopez-Perez, E.3    Checler, F.4
  • 34
    • 0032032493 scopus 로고    scopus 로고
    • Turnover of amyloid β-protein in mouse brain and acute reduction of its level by phorbol ester
    • Savage M, Trusko SP, Howland DS, et al. (1998) Turnover of amyloid β-protein in mouse brain and acute reduction of its level by phorbol ester. J. Neurosci. 18: 1743-1752.
    • (1998) J. Neurosci. , vol.18 , pp. 1743-1752
    • Savage, M.1    Trusko, S.P.2    Howland, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.