메뉴 건너뛰기




Volumn 74, Issue 5, 2000, Pages 1878-1884

Mutant presenilin 1 increases the levels of Alzheimer amyloid β-peptide aβ42 in late compartments of the constitutive secretory pathway

Author keywords

Amyloid peptide; Familial Alzheimer's disease; Neuroblastoma; Plasma membrane; Proteolytic processing; Rab; Trans Golgi network

Indexed keywords

AMYLOID BETA PROTEIN; NOTCH RECEPTOR; PRESENILIN 1;

EID: 0034100349     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0741878.x     Document Type: Article
Times cited : (40)

References (46)
  • 1
    • 0342679950 scopus 로고    scopus 로고
    • Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., and Struhl K., eds, John Wiley, New York
    • Ausubel F. M. (1996) Current Protocols in Molecular Biology, Vol. 2 (Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., and Struhl K., eds), 10.7.1-10.9.1. John Wiley, New York.
    • (1996) Current Protocols in Molecular Biology , vol.2 , pp. 1071-1091
    • Ausubel, F.M.1
  • 3
    • 0030877659 scopus 로고    scopus 로고
    • Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane
    • Blaumueller C. M., Qi H., Zagouras P., and Artavanis-Tsakonis S. (1997) Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane. Cell 90, 281-291.
    • (1997) Cell , vol.90 , pp. 281-291
    • Blaumueller, C.M.1    Qi, H.2    Zagouras, P.3    Artavanis-Tsakonis, S.4
  • 5
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D. H., Matsudaira P., and Yankner B. A. (1993) Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA 90, 2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 7
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell A., Grunberg J., Pesold B., Diehlmann A., Citron M., Nixon R., Beyreuther K., Selkoe D. J., and Haass C. (1998) The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J. Biol. Chem. 273, 3205-3211.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6    Beyreuther, K.7    Selkoe, D.J.8    Haass, C.9
  • 9
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's a beta (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook D. G., Forman M. S., Sung J. C., Leight S., Kolson D. L., Iwatsubo T., Lee V. M., and Doms R. W. (1997) Alzheimer's A beta (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3, 180-182.
    • (1997) Nat. Med. , vol.3 , pp. 180-182
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.7    Doms, R.W.8
  • 14
    • 0032796128 scopus 로고    scopus 로고
    • Neurohormonal signalling pathways and the regulation of Alzheimer amyloid metabolism
    • Gandy S. (1999) Neurohormonal signalling pathways and the regulation of Alzheimer amyloid metabolism. Trends Endocrinol. Metab. 10, 273-279.
    • (1999) Trends Endocrinol. Metab. , vol.10 , pp. 273-279
    • Gandy, S.1
  • 16
    • 0033535470 scopus 로고    scopus 로고
    • Alzheimer's disease: In search of γ-secretase
    • Hardy J. and Israel A. (1999) Alzheimer's disease: in search of γ-secretase. Nature 398, 466-467.
    • (1999) Nature , vol.398 , pp. 466-467
    • Hardy, J.1    Israel, A.2
  • 19
    • 0027517448 scopus 로고
    • Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane
    • Huber L. A., Pimplikar S., Parton R. G., Virta H., Zerial M., and Simons K. (1993) Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J. Cell Biol. 123, 35-45.
    • (1993) J. Cell Biol. , vol.123 , pp. 35-45
    • Huber, L.A.1    Pimplikar, S.2    Parton, R.G.3    Virta, H.4    Zerial, M.5    Simons, K.6
  • 20
    • 0342679948 scopus 로고    scopus 로고
    • Identification of the intracellular site of Aβ42 generation that is influenced by mutant presenilins
    • Iwata H., Tomita T., Iwai A., Maruyama K., and Iwatsubo T. (1999) Identification of the intracellular site of Aβ42 generation that is influenced by mutant presenilins. Soc. Neurosci. Abstr. 25, 595.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 595
    • Iwata, H.1    Tomita, T.2    Iwai, A.3    Maruyama, K.4    Iwatsubo, T.5
  • 21
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T., Odaka A., Suzuki N., Mizusawa H., Nukina N., and Ihara Y. (1994) Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 13, 45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 22
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta peptides and APO E in down syndrome: Implications for initial events in amyloid plaque formation
    • Lemere C. A., Blusztajn J. K., Yamaguchi H., Wisniewski T., Saido T. C., and Selkoe D. J. (1996) Sequence of deposition of heterogeneous amyloid beta peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation. Neurobiol. Dis. 3, 16-32.
    • (1996) Neurobiol. Dis. , vol.3 , pp. 16-32
    • Lemere, C.A.1    Blusztajn, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 23
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external KDEL protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vera cells
    • Majoul I. V., Bastiaens P., and Soling H. D. (1996) Transport of an external KDEL protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vera cells. J. Cell Biol. 133, 777-789.
    • (1996) J. Cell Biol. , vol.133 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.2    Soling, H.D.3
  • 24
    • 0031876002 scopus 로고    scopus 로고
    • Localization and possible functions of presenilins in brain
    • McGeer P. L., Kawamata T., and McGeer E. G. (1998) Localization and possible functions of presenilins in brain. Rev. Neurosci. 9, 1-15.
    • (1998) Rev. Neurosci. , vol.9 , pp. 1-15
    • McGeer, P.L.1    Kawamata, T.2    McGeer, E.G.3
  • 26
    • 0029989591 scopus 로고    scopus 로고
    • Enhanced release of amyloid beta-protein from codon 670/671 "Swedish" mutant beta-amyloid precursor protein occurs in both secretory and endocytic pathways
    • Perez R. G., Squazzo S. L., and Koo E. H. (1996) Enhanced release of amyloid beta-protein from codon 670/671 "Swedish" mutant beta-amyloid precursor protein occurs in both secretory and endocytic pathways. J. Biol. Chem. 271, 1090-1097.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1090-1097
    • Perez, R.G.1    Squazzo, S.L.2    Koo, E.H.3
  • 28
    • 4244106984 scopus 로고    scopus 로고
    • Subcellular localization of amyloid precursor protein derivatives in neuroblastoma cells expressing wild-type or mutant presenilin 1
    • Petanceska S., Seeger M., Checler F., Sisodia S., Greengard P., and Gandy S. (1998) Subcellular localization of amyloid precursor protein derivatives in neuroblastoma cells expressing wild-type or mutant presenilin 1. Neurobiol. Aging 19 (Suppl. 4), S191.
    • (1998) Neurobiol. Aging , vol.19 , Issue.SUPPL. 4
    • Petanceska, S.1    Seeger, M.2    Checler, F.3    Sisodia, S.4    Greengard, P.5    Gandy, S.6
  • 29
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price D. L. and Sisodia S. (1998) Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neurosci. 21, 479-505.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.2
  • 30
    • 0032032847 scopus 로고    scopus 로고
    • Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Abeta1-42/43 expression
    • Qian S., Jiang P., Guan X. M., Singh G., Trumbauer M. E., Yu H., Chen H. Y., Van de Ploeg L. H., and Zheng H. (1998) Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Abeta1-42/43 expression. Neuron 20, 611-617.
    • (1998) Neuron , vol.20 , pp. 611-617
    • Qian, S.1    Jiang, P.2    Guan, X.M.3    Singh, G.4    Trumbauer, M.E.5    Yu, H.6    Chen, H.Y.7    Van De Ploeg, L.H.8    Zheng, H.9
  • 32
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter E. H., Kisslinger J., and Kopan R. (1998) Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.2    Kopan, R.3
  • 34
    • 0032235452 scopus 로고    scopus 로고
    • Introduction: Notch signaling and choice of cell fates in development
    • Simpson P. (1998) Introduction: Notch signaling and choice of cell fates in development. Semin. Cell Dev. Biol. 9, 581-582.
    • (1998) Semin. Cell Dev. Biol. , vol.9 , pp. 581-582
    • Simpson, P.1
  • 35
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture
    • Skovronsky D. M., Doms R. W., and Lee V. M. (1998) Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J. Cell Biol. 141, 931-939.
    • (1998) J. Cell Biol. , vol.141 , pp. 931-939
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.3
  • 36
    • 0033583047 scopus 로고    scopus 로고
    • The biological and pathological function of the presenilin-1 delta exon 9 mutation is independent of its defect to undergo proteolytic processing
    • Steiner H. R. H., Grim M. G., Philipp U., Pesold B., Citron M., Baumeister R., and Haass C. (1999) The biological and pathological function of the presenilin-1 delta exon 9 mutation is independent of its defect to undergo proteolytic processing. J. Biol. Chem. 274, 7615-7618.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7615-7618
    • Steiner, H.R.H.1    Grim, M.G.2    Philipp, U.3    Pesold, B.4    Citron, M.5    Baumeister, R.6    Haass, C.7
  • 37
    • 0031686460 scopus 로고    scopus 로고
    • Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid β-protein 1-42 and its N-terminally truncated variant(s) which are generated at distinct sites
    • Sudoh S., Kawamura Y., Sato S., Wang R., Saido T. C., Oyama F., Sakaki Y., Komano H., and Yanagisawa K. (1998) Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid β-protein 1-42 and its N-terminally truncated variant(s) which are generated at distinct sites. J. Neurochem. 71, 1535-1543.
    • (1998) J. Neurochem. , vol.71 , pp. 1535-1543
    • Sudoh, S.1    Kawamura, Y.2    Sato, S.3    Wang, R.4    Saido, T.C.5    Oyama, F.6    Sakaki, Y.7    Komano, H.8    Yanagisawa, K.9
  • 39
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the "swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta secretase" site occurs in the Golgi apparatus
    • Thinakaran G., Teplow D. B., Siman R., Greenberg B., and Sisodia S. S. (1996b) Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta secretase" site occurs in the Golgi apparatus. J. Biol. Chem. 271, 9390-9397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 41
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42
    • Wild-Bode C., Yamazaki T., Capell A., Leimer U., Steiner H., Ihara Y., and Haass C. (1997) Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42. J. Biol. Chem. 272, 16085-16088.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3    Leimer, U.4    Steiner, H.5    Ihara, Y.6    Haass, C.7
  • 42
    • 0343550262 scopus 로고    scopus 로고
    • Presenilin-1 is involved in neuronal Aβ production in the trans-Golgi network but not in the endoplasmic reticulum
    • Wilson C. A., Zheng H., Doms R. W., and Lee V. M. Y. (1999) Presenilin-1 is involved in neuronal Aβ production in the trans-Golgi network but not in the endoplasmic reticulum. Soc. Neurosci. Abstr. 25, 57.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 57
    • Wilson, C.A.1    Zheng, H.2    Doms, R.W.3    Lee, V.M.Y.4
  • 43
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe M., Xia W., Ostaszewski B. L., Diehl T. S., Kimberly W. T., and Selkoe D. (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.6
  • 44
    • 0032564388 scopus 로고    scopus 로고
    • Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and golgi
    • Xia W., Zhang J., Ostazsewski B. L., Kimberly W. T., Seubert P., Koo E. H., Shen J., and Selkoe D. J. (1998) Presenilin 1 regulates the processing of beta-amyloid precursor protein C-terminal fragments and the generation of amyloid beta-protein in endoplasmic reticulum and Golgi. Biochemistry 37, 16465-16471.
    • (1998) Biochemistry , vol.37 , pp. 16465-16471
    • Xia, W.1    Zhang, J.2    Ostazsewski, B.L.3    Kimberly, W.T.4    Seubert, P.5    Koo, E.H.6    Shen, J.7    Selkoe, D.J.8
  • 45
  • 46
    • 0032524865 scopus 로고    scopus 로고
    • Subcellular distribution and turnover of presenilins in transfected cells
    • Zhang J., Kang D. E., Xia W., Okochi M., Mori H., Selkoe D. J., and Koo E. H. (1998) Subcellular distribution and turnover of presenilins in transfected cells. J. Biol. Chem. 273, 12436-12442.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12436-12442
    • Zhang, J.1    Kang, D.E.2    Xia, W.3    Okochi, M.4    Mori, H.5    Selkoe, D.J.6    Koo, E.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.