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Volumn 66, Issue 2 SUPPL. 1, 2006, Pages

Amyloidogenic processing of β-amyloid precursor protein in intracellular compartments

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; COMPLEMENTARY DNA; GAMMA SECRETASE; JAGGED1; JAGGED2; NOTCH1 RECEPTOR; PROTEIN PSEN1; PROTEIN PSEN2; UNCLASSIFIED DRUG; ASPARTIC PROTEINASE; BACE1 PROTEIN, HUMAN; MEMBRANE PROTEIN; PRESENILIN 1; PRESENILIN 2; PROTEINASE; PSEN1 PROTEIN, HUMAN; PSEN2 PROTEIN, HUMAN; SECRETASE;

EID: 33644849690     PISSN: 00283878     EISSN: None     Source Type: Journal    
DOI: 10.1212/01.wnl.0000192107.17175.39     Document Type: Conference Paper
Times cited : (176)

References (39)
  • 1
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 1991;12:383-388.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001;81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0036548070 scopus 로고    scopus 로고
    • Gamma-secretase, Notch, Abeta and Alzheimer's disease: Where do the presenilins fit in?
    • Sisodia SS, St George-Hyslop PH. Gamma-secretase, Notch, Abeta and Alzheimer's disease: where do the presenilins fit in? Nat Rev Neurosci 2002;3:281-290.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 4
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi RE, Bertram L. Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 2005;120:545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 6
    • 0029379605 scopus 로고
    • Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler F. Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease. J Neurochem 1995;65:1431-1444.
    • (1995) J Neurochem , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 7
    • 0033049442 scopus 로고    scopus 로고
    • Activity of alpha-secretase as the common final effector of protein kinase C-dependent and -independent modulation of amyloid precursor protein metabolism
    • Racchi M, Solano DC, Sironi M, Govoni S. Activity of alpha-secretase as the common final effector of protein kinase C-dependent and -independent modulation of amyloid precursor protein metabolism. J Neurochem 1999;72:2464-2470.
    • (1999) J Neurochem , vol.72 , pp. 2464-2470
    • Racchi, M.1    Solano, D.C.2    Sironi, M.3    Govoni, S.4
  • 8
  • 9
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: The beta-secretase enzyme in Alzheimer's disease
    • Vassar R. BACE1: the beta-secretase enzyme in Alzheimer's disease. J Mol Neurosci 2004;23:105-114.
    • (2004) J Mol Neurosci , vol.23 , pp. 105-114
    • Vassar, R.1
  • 10
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: Proteasome of the membrane?
    • Kopan R, Ilagan MX. Gamma-secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 2004;5:499-504.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 12
    • 4043052896 scopus 로고    scopus 로고
    • Identification of the role of presenilins beyond Alzheimer's disease
    • Thinakaran G, Parent AT. Identification of the role of presenilins beyond Alzheimer's disease. Pharmacol Res 2004;50:411-418.
    • (2004) Pharmacol Res , vol.50 , pp. 411-418
    • Thinakaran, G.1    Parent, A.T.2
  • 13
    • 0026721943 scopus 로고
    • Beta-amyloid precursor protein cleavage by a membrane-bound protease
    • U S A
    • Sisodia SS. Beta-amyloid precursor protein cleavage by a membrane-bound protease. Proc Natl Acad Sci U S A 1992;89:6075-6079.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 14
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo EH, Squazzo SL. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem 1994;269:17386-17389.
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 15
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's a beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC, et al. Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 1997;3:1021-1023.
    • (1997) Nat Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3
  • 16
    • 0033582159 scopus 로고    scopus 로고
    • Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer beta-amyloid peptides
    • U S A
    • Greenfield JP, Tsai J, Gouras GK, et al. Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer beta-amyloid peptides. Proc Natl Acad Sci U S A 1999;96:742-747.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 742-747
    • Greenfield, J.P.1    Tsai, J.2    Gouras, G.K.3
  • 17
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology
    • Takahashi RH, Milner TA, Li F, et al. Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am J Pathol 2002;161:1869-1879.
    • (2002) Am J Pathol , vol.161 , pp. 1869-1879
    • Takahashi, R.H.1    Milner, T.A.2    Li, F.3
  • 18
    • 0030963605 scopus 로고    scopus 로고
    • Generation of Alzheimer beta-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
    • U S A
    • Xu H, Sweeney D, Wang R, et al. Generation of Alzheimer beta-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation. Proc Natl Acad Sci U S A 1997;94:3748-3752.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 3748-3752
    • Xu, H.1    Sweeney, D.2    Wang, R.3
  • 19
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane
    • Kaether C, Lammich S, Edbauer D, et al. Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane. J Cell Biol 2002;158:551-561.
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3
  • 20
    • 14244268498 scopus 로고    scopus 로고
    • Gamma -secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung JH, Raper DM, Selkoe DJ . gamma -secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem 2005;280:4383-4392.
    • (2005) J Biol Chem , vol.280 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 21
    • 7244258941 scopus 로고    scopus 로고
    • Association of g-secretase with lipid rafts in post-golgi and endosome membranes
    • Vetrivel KS, Cheng H, Lin W, et al. Association of g-secretase with lipid rafts in post-golgi and endosome membranes. J Biol Chem 2004;279:44945-44954.
    • (2004) J Biol Chem , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1    Cheng, H.2    Lin, W.3
  • 22
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42
    • Perez RG, Soriano S, Hayes JD, et al. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J Biol Chem 1999;274:18851-18856.
    • (1999) J Biol Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3
  • 23
    • 0345743462 scopus 로고    scopus 로고
    • Adaptor protein interactions: Modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?
    • King GD, Turner SR. Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer's disease risk? Exp Neurol 2004;185:208-219.
    • (2004) Exp Neurol , vol.185 , pp. 208-219
    • King, G.D.1    Turner, S.R.2
  • 24
    • 2442498577 scopus 로고    scopus 로고
    • FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein
    • Pietrzik CU, Yoon IS, Jaeger S, Busse T, Weggen S, Koo EH. FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein. J Neurosci 2004;24:4259-4265.
    • (2004) J Neurosci , vol.24 , pp. 4259-4265
    • Pietrzik, C.U.1    Yoon, I.S.2    Jaeger, S.3    Busse, T.4    Weggen, S.5    Koo, E.H.6
  • 25
    • 0142123260 scopus 로고    scopus 로고
    • APP processing is regulated by cytoplasmic phosphorylation
    • Lee MS, Kao SC, Lemere CA, et al. APP processing is regulated by cytoplasmic phosphorylation. J Cell Biol 2003;163:83-95.
    • (2003) J Cell Biol , vol.163 , pp. 83-95
    • Lee, M.S.1    Kao, S.C.2    Lemere, C.A.3
  • 26
    • 8744225623 scopus 로고    scopus 로고
    • Proteolytic processing of amyloid-beta precursor protein by secretases does not require cell surface transport
    • Khvotchev M, Sudhof TC. Proteolytic processing of amyloid-beta precursor protein by secretases does not require cell surface transport. J Biol Chem 2004;279:47101-47108.
    • (2004) J Biol Chem , vol.279 , pp. 47101-47108
    • Khvotchev, M.1    Sudhof, T.C.2
  • 27
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10
    • U S A
    • Kojro E, Gimpl G, Lammich S, Marz W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10. Proc Natl Acad Sci U S A 2001;98:5815-5820.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 28
    • 10344263931 scopus 로고    scopus 로고
    • Neuronal membrane cholesterol loss enhances amyloid peptide generation
    • Abad-Rodriguez J, Ledesma MD, Craessaerts K, et al. Neuronal membrane cholesterol loss enhances amyloid peptide generation. J Cell Biol 2004;167:953-960.
    • (2004) J Cell Biol , vol.167 , pp. 953-960
    • Abad-Rodriguez, J.1    Ledesma, M.D.2    Craessaerts, K.3
  • 29
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 2000;1:31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 30
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 31
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell DR, Christie G, Hussain I, Dingwall C. Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr Biol 2001;11:1288-1293.
    • (2001) Curr Biol , vol.11 , pp. 1288-1293
    • Riddell, D.R.1    Christie, G.2    Hussain, I.3    Dingwall, C.4
  • 32
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • U S A
    • Cordy JM, Hussain I, Dingwall C, Hooper NM, Turner AJ. Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein. Proc Natl Acad Sci U S A 2003;100:11735-11740.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 11735-11740
    • Cordy, J.M.1    Hussain, I.2    Dingwall, C.3    Hooper, N.M.4    Turner, A.J.5
  • 33
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003;160:113-123.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 34
    • 21844448354 scopus 로고    scopus 로고
    • Spatial segregation of g-secretase and substrates in distinct membrane domains
    • Vetrivel KS, Cheng H, Kim SH, et al. Spatial segregation of g-secretase and substrates in distinct membrane domains. J Biol Chem 2005;280:25892-25900.
    • (2005) J Biol Chem , vol.280 , pp. 25892-25900
    • Vetrivel, K.S.1    Cheng, H.2    Kim, S.H.3
  • 35
    • 0036797633 scopus 로고    scopus 로고
    • Inclusion-body myositis and myopathies: Different etiologies, possibly similar pathogenic mechanisms
    • Askanas V, Engel WK. Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms. Curr Opin Neurol 2002;15:525-531.
    • (2002) Curr Opin Neurol , vol.15 , pp. 525-531
    • Askanas, V.1    Engel, W.K.2
  • 36
    • 0742321934 scopus 로고    scopus 로고
    • Proposed pathogenetic cascade of inclusion-body myositis: Importance of amyloid-beta, misfolded proteins, predisposing genes, and aging
    • Askanas V, Engel WK. Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging. Curr Opin Rheumatol 2003;15:737-744.
    • (2003) Curr Opin Rheumatol , vol.15 , pp. 737-744
    • Askanas, V.1    Engel, W.K.2
  • 37
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G, Engel WK, McFerrin J, Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 2004;164:1-7.
    • (2004) Am J Pathol , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 38
    • 17444418324 scopus 로고    scopus 로고
    • Involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis
    • Ferrer I, Carmona M, Blanco R, Moreno D, Torrejon-Escribano B, Olive M. Involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis. Brain Pathol 2005;15:101-108.
    • (2005) Brain Pathol , vol.15 , pp. 101-108
    • Ferrer, I.1    Carmona, M.2    Blanco, R.3    Moreno, D.4    Torrejon-Escribano, B.5    Olive, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.