메뉴 건너뛰기




Volumn 121, Issue 3, 1997, Pages 585-590

Deletion of an endosomal/lysosomal targeting signal promotes the secretion of Alzheimer's disease amyloid precursor protein (APP)

Author keywords

Alzheimer's disease; Amyloid precursor protein; Endosomal lysosomal pathway; Targeting sequence

Indexed keywords

AMYLOID PRECURSOR PROTEIN;

EID: 0030900187     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021625     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D.J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0023872043 scopus 로고
    • Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
    • Kitaguchi, N., Tokushima, Y., Shiojiri, S., and Ito, H. (1988) Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature 331, 530-532
    • (1988) Nature , vol.331 , pp. 530-532
    • Kitaguchi, N.1    Tokushima, Y.2    Shiojiri, S.3    Ito, H.4
  • 4
    • 0023850791 scopus 로고
    • Protease inhibitory domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease
    • Tanzi, R.E., McClatchey, A.I., Lamperti, E.D., Villa-Komaroff, L., Gusella, J., and Neve, R.L. (1988) Protease inhibitory domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature 331, 528-530
    • (1988) Nature , vol.331 , pp. 528-530
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.4    Gusella, J.5    Neve, R.L.6
  • 6
    • 0027333557 scopus 로고
    • Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
    • Haass, C. and Selkoe, D.J. (1993) Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell 75, 1039-1042
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 7
    • 0025831751 scopus 로고
    • Processing of β-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion
    • Anderson, J.P., Esch, F.S., Keim, P.S., Sambamuri, K., Lieberburg, I., and Robakis, N.K. (1991) Processing of β-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion. Neurosci. Lett. 128, 126-128
    • (1991) Neurosci. Lett. , vol.128 , pp. 126-128
    • Erson, J.P.1    Esch, F.S.2    Keim, P.S.3    Sambamuri, K.4    Lieberburg, I.5    Robakis, N.K.6
  • 8
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T., Estus, S., Younkin, L., Selkoe, D.J., and Younkin, S. (1992) Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255, 728-730
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.1    Estus, S.2    Younkin, L.3    Selkoe, D.J.4    Younkin, S.5
  • 9
    • 0026522375 scopus 로고
    • Potentially amyloidogenic, carboxylterminal derivatives of the amyloid precursor protein
    • Estus, S., Golde, T., Kunishita, T., Blades, D., Greenberg, B., and Younkin, S. (1992) Potentially amyloidogenic, carboxylterminal derivatives of the amyloid precursor protein. Science 255, 726-728
    • (1992) Science , vol.255 , pp. 726-728
    • Estus, S.1    Golde, T.2    Kunishita, T.3    Blades, D.4    Greenberg, B.5    Younkin, S.6
  • 11
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch, R., Slack, B., Wurtman, R., and Growdon, J. (1992) Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258, 39304-39307
    • (1992) Science , vol.258 , pp. 39304-39307
    • Nitsch, R.1    Slack, B.2    Wurtman, R.3    Growdon, J.4
  • 13
    • 0027526419 scopus 로고
    • Release of excess amyloid from mutant amyloid β-protein precursor
    • Cai, X.-D., Golde, T.E., and Younkin, S. (1993) Release of excess amyloid from mutant amyloid β-protein precursor. Science 259, 514-516
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.3
  • 14
    • 0027529491 scopus 로고
    • Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): Cleavage of APP occurs in a late compartment of the default secretion pathway
    • De Strooper, B., Umans, L., Van Leuven, F., and Van den Berghe, H. (1993) Study of the synthesis and secretion of normal and artificial mutants of murine amyloid precursor protein (APP): cleavage of APP occurs in a late compartment of the default secretion pathway. J. Cell. Biol. 121, 295-304
    • (1993) J. Cell. Biol. , vol.121 , pp. 295-304
    • De Strooper, B.1    Umans, L.2    Van Leuven, F.3    Van den Berghe, H.4
  • 15
    • 0027484116 scopus 로고
    • The Alzheimer β-amyloid protein precursor/ protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells
    • Kuentzel, S.L., Ali, S.M., Altman, R.A., Greenberg, B.D., and Raub, T.J. (1993) The Alzheimer β-amyloid protein precursor/ protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells. Biochem. J. 295, 367-378
    • (1993) Biochem. J. , vol.295 , pp. 367-378
    • Kuentzel, S.L.1    Ali, S.M.2    Altman, R.A.3    Greenberg, B.D.4    Raub, T.J.5
  • 17
    • 0025941495 scopus 로고
    • The processing of Alzheimer A4/beta-amyloid precursor: Identification of a human brain metallopeptidase which cleaves -Lys-Leu- in a model peptide
    • McDermott, J.R. and Gibson, A.M. (1991) The processing of Alzheimer A4/beta-amyloid precursor: identification of a human brain metallopeptidase which cleaves -Lys-Leu- in a model peptide. Biochem. Biophys. Res. Commun. 179, 1148-1154
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1148-1154
    • McDermott, J.R.1    Gibson, A.M.2
  • 20
    • 0028236274 scopus 로고
    • Targeting of membrane proteins to endosomes and lysosomes
    • Sandoval, I.V. and Bakke, O. (1994) Targeting of membrane proteins to endosomes and lysosomes. Trends Cell Biol. 4, 292-297
    • (1994) Trends Cell Biol. , vol.4 , pp. 292-297
    • Sandoval, I.V.1    Bakke, O.2
  • 22
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo, E.H. and Szuazzo, S.L. (1994) Evidence that production and release of amyloid β-protein involves the endocytic pathway. J. Biol. Chem. 269, 17386-17389
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Szuazzo, S.L.2
  • 23
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen, W.J., Goldstein, J.L., and Brown, M.S. (1990) NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265, 3116-3123
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 24
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker, W. and Fumey, C. (1994) A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J. 13, 2963-2969
    • (1994) EMBO J. , vol.13 , pp. 2963-2969
    • Hunziker, W.1    Fumey, C.2
  • 25
    • 0025172954 scopus 로고
    • Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail
    • Williams, M.A. and Fukuda, M. (1990) Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell. Biol. 111, 955-966
    • (1990) J. Cell. Biol. , vol.111 , pp. 955-966
    • Williams, M.A.1    Fukuda, M.2
  • 26
    • 0027389118 scopus 로고
    • Identification of the Alzheimer β/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells
    • Nordstedt, C., Caporaso, G., Thyberg, J., Gandy, S., and Greengard, P. (1993) Identification of the Alzheimer β/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells. J. Biol. Chem. 268, 608-612
    • (1993) J. Biol. Chem. , vol.268 , pp. 608-612
    • Nordstedt, C.1    Caporaso, G.2    Thyberg, J.3    Gandy, S.4    Greengard, P.5
  • 27
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass, C., Koo, E., Mellon, A., Hung, A.Y., and Selkoe, D.J. (1992) 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.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 28
    • 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
  • 29
    • 0024565449 scopus 로고
    • Expression of high-affinity binding of human immunoglobulin E by transfected cells
    • Miller, L., Blank, U., Metzger, H., and Kinet, J.P. (1989) Expression of high-affinity binding of human immunoglobulin E by transfected cells. Science 244, 334-337
    • (1989) Science , vol.244 , pp. 334-337
    • Miller, L.1    Blank, U.2    Metzger, H.3    Kinet, J.P.4
  • 30
    • 0024276856 scopus 로고
    • A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family
    • Ohno, S., Akita, Y., Konno, Y., Imajoh, S., and Suzuki, K. (1988) A novel phorbol ester receptor/protein kinase, nPKC, distantly related to the protein kinase C family. Cell 53, 731-741
    • (1988) Cell , vol.53 , pp. 731-741
    • Ohno, S.1    Akita, Y.2    Konno, Y.3    Imajoh, S.4    Suzuki, K.5
  • 31
    • 0023850352 scopus 로고
    • SR alpha promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of the human T-cell leukemia virus type 1 long terminal repeat
    • Takebe, M., Seiki, M., Fujisawa, J., Hoy, P., Yokota, K., Arai, K., Yoshida, M., and Arai, N. (1988) SR alpha promoter: an efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of the human T-cell leukemia virus type 1 long terminal repeat. Mol. Cell. Biol. 8, 466-472
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 466-472
    • Takebe, M.1    Seiki, M.2    Fujisawa, J.3    Hoy, P.4    Yokota, K.5    Arai, K.6    Yoshida, M.7    Arai, N.8
  • 32
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.M. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.M.1
  • 33
    • 0024550204 scopus 로고
    • Identification, biogenesis and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann, A., Koning, G., Bunke, D., Fischer, P., Salbaum, J. M., Masters, C., and Beyreuther, K. (1989) Identification, biogenesis and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57, 115-126
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Koning, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.6    Beyreuther, K.7
  • 34
    • 0028857502 scopus 로고
    • Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten Disease)
    • Ezaki, J., Wolfe, L.S., Higuti, T., Ishidoh, K., and Kominami, E. (1995) Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten Disease). J. Neurochem. 64, 733-741
    • (1995) J. Neurochem. , vol.64 , pp. 733-741
    • Ezaki, J.1    Wolfe, L.S.2    Higuti, T.3    Ishidoh, K.4    Kominami, E.5
  • 35
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Lorand, L., ed. Academic Press, New York
    • Barrett, A.J. and Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L in Methods in Enzymology (Lorand, L., ed.) Vol. 80, pp. 535-561, Academic Press, New York
    • (1981) Methods in Enzymology , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 36
    • 77956998789 scopus 로고
    • Isolation of Golgi apparatus
    • Jakoby, W.B., ed. Academic Press, New York
    • Morre, D.J. (1971) Isolation of Golgi apparatus in Methods in Enzymology (Jakoby, W.B., ed.) Vol. 22, pp. 130-148, Academic Press, New York
    • (1971) Methods in Enzymology , vol.22 , pp. 130-148
    • Morre, D.J.1
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0028965767 scopus 로고
    • Conventional protein kinase C (PKC)-α and novel PKCε, but not -δ increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA-transfected 3Y1 fibroblasts
    • Kinouchi, T., Sorimachi, H., Maruyama, K., Mizuno, K., Ohno, S., Ishiura, S., and Suzuki, K. (1995) Conventional protein kinase C (PKC)-α and novel PKCε, but not -δ increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA-transfected 3Y1 fibroblasts. FEBS Lett. 364, 203-206
    • (1995) FEBS Lett. , vol.364 , pp. 203-206
    • Kinouchi, T.1    Sorimachi, H.2    Maruyama, K.3    Mizuno, K.4    Ohno, S.5    Ishiura, S.6    Suzuki, K.7
  • 39
    • 0026736593 scopus 로고
    • α2-Macroglobulin and other proteinase inhibitors do not interfere with the secretion of amyloid precursor protein in mouse neuroblastoma cells
    • De Strooper, B., Van Leuven, F., and Van Den Berghe, H. (1992) α2-Macroglobulin and other proteinase inhibitors do not interfere with the secretion of amyloid precursor protein in mouse neuroblastoma cells. FEBS Lett. 308, 50-53
    • (1992) FEBS Lett. , vol.308 , pp. 50-53
    • De Strooper, B.1    Van Leuven, F.2    Van Den Berghe, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.