메뉴 건너뛰기




Volumn 68, Issue 2, 1997, Pages 698-703

Proteasome contributes to the α-secretase pathway of amyloid precursor protein in human cells

Author keywords

Alzheimer's disease; Amyloid peptide; Human kidney 293 cells; Proteasome; Secretase; Amyloid precursor protein

Indexed keywords

ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; CHYMOTRYPSIN; LACTACYSTIN; PHORBOL DIBUTYRATE; PROTEASOME; PROTEINASE; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0031022252     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68020698.x     Document Type: Article
Times cited : (44)

References (33)
  • 1
    • 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
  • 2
    • 0028296661 scopus 로고
    • Study of the phorbol ester effect on Alzheimer amyloid precursor processing: Sequence requirements and involvement of a cholera toxin sensitive protein
    • Efthimiopoulos S., Felsenstein K. M., Sambamurti K., Robakis N. K., and Refolo L. M. (1994) Study of the phorbol ester effect on Alzheimer amyloid precursor processing: sequence requirements and involvement of a cholera toxin sensitive protein. J. Neurosci. Res. 38, 81-90.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 81-90
    • Efthimiopoulos, S.1    Felsenstein, K.M.2    Sambamurti, K.3    Robakis, N.K.4    Refolo, L.M.5
  • 4
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R., Lane W. S., Choi S., Corey E. J., and Schreiber S. L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 5
    • 0026662356 scopus 로고
    • Secretory processing of the Alzheimer amyloid β/A4 protein precursor is increased by protein phosphorylation
    • Gillespie S., Golde T. E., and Younkin S. G. (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
  • 6
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (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
  • 7
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D., Lerman M. I., McBride O. W., Saffiotti U., and Gajdusek D. C. (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235, 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 8
    • 0029912242 scopus 로고    scopus 로고
    • Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB
    • Griscavage J. M., Wilk S., and Ignarro L. J. (1996) Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB. Proc. Natl. Acad. Sci. USA 93, 3308-3312.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3308-3312
    • Griscavage, J.M.1    Wilk, S.2    Ignarro, L.J.3
  • 9
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough R., Pratt G., and Rechesteiner M. (1987) Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J. Biol. Chem. 262, 8303-8313.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechesteiner, M.3
  • 10
    • 0028057224 scopus 로고
    • Selective ectodomain phosphorylation and regulated cleavage of β-amyloid precursor protein
    • Hung A. Y. and Selkoe D. J. (1994) Selective ectodomain phosphorylation and regulated cleavage of β-amyloid precursor protein. EMBO J. 13, 534-542.
    • (1994) EMBO J. , vol.13 , pp. 534-542
    • Hung, A.Y.1    Selkoe, D.J.2
  • 13
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T. J., Loo M. A., Find S., Williams D. B., Goldberg A. L., and Riordan J. R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Find, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 14
    • 0030038824 scopus 로고    scopus 로고
    • Changes in proteasome activity following transient ischemia
    • Kamikubo T. and Hayashi T. (1996) Changes in proteasome activity following transient ischemia. Neurochem. Int. 28, 209-212.
    • (1996) Neurochem. Int. , vol.28 , pp. 209-212
    • Kamikubo, T.1    Hayashi, T.2
  • 16
    • 0026691966 scopus 로고
    • Two-way cleavage of β-amyloid protein precursor by multicatalytic proteinase
    • Kojima I. and Oniori M. (1992) Two-way cleavage of β-amyloid protein precursor by multicatalytic proteinase. FEBS Lett. 304, 57-60.
    • (1992) FEBS Lett. , vol.304 , pp. 57-60
    • Kojima, I.1    Oniori, M.2
  • 17
    • 0029805807 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the proteasome: A contribution to the α-secretase pathway in human cells
    • Marambaud P., Wilk S., and Checler F. (1996) Protein kinase A phosphorylation of the proteasome: a contribution to the α-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
  • 20
    • 0030064136 scopus 로고    scopus 로고
    • Differential effects of a rabo mutant on secretory versus amyloidogenic processing of Alzheimer's β-amyloid precursor protein
    • McConlongue L., Castellano F., deWit C., Schenk D., and Maltese W. A. (1996) Differential effects of a rabo mutant on secretory versus amyloidogenic processing of Alzheimer's β-amyloid precursor protein. J. Biol. Chem. 271, 1343-1348.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1343-1348
    • McConlongue, L.1    Castellano, F.2    DeWit, C.3    Schenk, D.4    Maltese, W.A.5
  • 21
    • 0029870306 scopus 로고    scopus 로고
    • Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidyl inositol-linked protein in a pre-Golgi compartment
    • Oda K., Ikehara Y., and Omura S. (1996) Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidyl inositol-linked protein in a pre-Golgi compartment. Biochem. Biophys. Res. Commun. 219, 800-805.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 800-805
    • Oda, K.1    Ikehara, Y.2    Omura, S.3
  • 23
    • 0024351497 scopus 로고
    • Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity
    • Orlowski M. and Michaud C. (1989) Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity. Biochemistry 28, 9270-9278.
    • (1989) Biochemistry , vol.28 , pp. 9270-9278
    • Orlowski, M.1    Michaud, C.2
  • 24
    • 0026538022 scopus 로고
    • Enzymatic changes of the bovine pituitary multicatalytic proteinase complex, induced by magnesium ions
    • Pereira M. E., Yu B., and Wilk S. (1992) Enzymatic changes of the bovine pituitary multicatalytic proteinase complex, induced by magnesium ions. Arch. Biochem. Biophys. 294, 1-8.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 1-8
    • Pereira, M.E.1    Yu, B.2    Wilk, S.3
  • 25
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters J. M. (1994) Proteasomes: protein degradation machines of the cell. Trends Biochem. Sci. 19, 377-382.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377-382
    • Peters, J.M.1
  • 26
    • 0029257190 scopus 로고
    • Cell-surface β-amyloid precursor protein stimulates neunte outgrowth of hippocampal neurons in an isoform-dependent manner
    • Qiu W. Q., Ferreira A., Miller C., Koo E. H., and Selkoe D. J. (1995) Cell-surface β-amyloid precursor protein stimulates neunte outgrowth of hippocampal neurons in an isoform-dependent manner. J. Neurosci. 15, 2157-2167.
    • (1995) J. Neurosci. , vol.15 , pp. 2157-2167
    • Qiu, W.Q.1    Ferreira, A.2    Miller, C.3    Koo, E.H.4    Selkoe, D.J.5
  • 27
    • 0024395366 scopus 로고
    • Secreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts
    • Saitoh T., Sundsmo M., Roch J. M., Kimura N., Cole G., Schubert D., Olsterdorf T., and Schenk D. B. (1989) Secreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts. Cell 58, 615-622.
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.M.3    Kimura, N.4    Cole, G.5    Schubert, D.6    Olsterdorf, T.7    Schenk, D.B.8
  • 28
    • 0027433787 scopus 로고
    • Characterization of proteases with he specificity to cleave at the secretase-site of β-APP
    • Schönlein C., Probst A., and Huber G. (1993) Characterization of proteases with (he specificity to cleave at the secretase-site of β-APP. Neurosci. Lett. 161, 33-36.
    • (1993) Neurosci. Lett. , vol.161 , pp. 33-36
    • Schönlein, C.1    Probst, A.2    Huber, G.3
  • 30
    • 0025373508 scopus 로고
    • Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia S. S., Koo E. H., Beyreuther K., Unterbeck A., and Price D. L. (1990) Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-496.
    • (1990) Science , vol.248 , pp. 492-496
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 31
    • 0025365401 scopus 로고
    • a-inhibitor, a form of Alzheimer amyloid precursor protein
    • a-inhibitor, a form of Alzheimer amyloid precursor protein. Science 248, 1126-1128.
    • (1990) Science , vol.248 , pp. 1126-1128
    • Smith, R.P.1    Higuchi, D.A.2    Broze, G.J.3
  • 33
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C. L., Omura S., and Kopito R. R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.