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Volumn 31, Issue 10, 2012, Pages 2261-2274

The mechanism of γ-Secretase dysfunction in familial Alzheimer disease

Author keywords

Alzheimer; amyloid; FAD mutations; g secretase; presenilin

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; CARBOXYPEPTIDASE; GAMMA SECRETASE; NOTCH RECEPTOR; PRESENILIN;

EID: 84861194622     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2012.79     Document Type: Article
Times cited : (425)

References (68)
  • 1
    • 0035923750 scopus 로고    scopus 로고
    • Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins
    • DOI 10.1016/S0896-6273(01)00512-8
    • Annaert WG, Esselens C, Baert V, Boeve C, Snellings G, Cupers P, Craessaerts K, De Strooper B (2001) Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron 32: 579-589 (Pubitemid 33145193)
    • (2001) Neuron , vol.32 , Issue.4 , pp. 579-589
    • Annaert, W.G.1    Esselens, C.2    Baert, V.3    Boeve, C.4    Snellings, G.5    Cupers, P.6    Craessaerts, K.7    De Strooper, B.8
  • 4
    • 15244341378 scopus 로고    scopus 로고
    • Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein
    • DOI 10.1523/JNEUROSCI.0364-05.2005
    • Berezovska O, Lleo A, Herl LD, Frosch MP, Stern EA, Bacskai BJ, Hyman BT (2005) Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein. J Neurosci 25: 3009-3017 (Pubitemid 40389259)
    • (2005) Journal of Neuroscience , vol.25 , Issue.11 , pp. 3009-3017
    • Berezovska, O.1    Lleo, A.2    Herl, L.D.3    Frosch, M.P.4    Stern, E.A.5    Bacskai, B.J.6    Hyman, B.T.7
  • 5
    • 76449085569 scopus 로고    scopus 로고
    • Gamma-secretases: From cell biology to therapeutic strategies
    • Bergmans BA, De Strooper B (2010) Gamma-secretases: from cell biology to therapeutic strategies. Lancet Neurol 9(2): 215-226
    • (2010) Lancet Neurol , vol.9 , Issue.2 , pp. 215-226
    • Bergmans, B.A.1    De Strooper, B.2
  • 6
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I, Mattson MP (2008) Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 31: 454-463
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 9
    • 50649119079 scopus 로고    scopus 로고
    • Glu(332) in the Nicastrin ectodomain is essential for gamma-secretase complex maturation but not for its activity
    • Chavez-Gutierrez L, Tolia A, Maes E, Li T, Wong PC, de Strooper B (2008) Glu(332) in the Nicastrin ectodomain is essential for gamma-secretase complex maturation but not for its activity. J Biol Chem 283: 20096-20105
    • (2008) J Biol Chem , vol.283 , pp. 20096-20105
    • Chavez-Gutierrez, L.1    Tolia, A.2    Maes, E.3    Li, T.4    Wong, P.C.5    De Strooper, B.6
  • 11
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease
    • DOI 10.1038/sj.embor.7400897, PII 7400897
    • De Strooper B (2007) Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep 8: 141-146 (Pubitemid 46420841)
    • (2007) EMBO Reports , vol.8 , Issue.2 , pp. 141-146
    • De Strooper, B.1
  • 12
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and gamma-secretases in cell biology and disease
    • De Strooper B, Annaert W (2010) Novel research horizons for presenilins and gamma-secretases in cell biology and disease. Annu Rev Cell Dev Biol 26: 235-260
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 14
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper B, Vassar R, Golde T (2010) The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat Rev Neurol 6: 99-107
    • (2010) Nat Rev Neurol , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 17
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 22: 1302-1306 (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 18
    • 77953525683 scopus 로고    scopus 로고
    • Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis
    • Fukumori A, Fluhrer R, Steiner H, Haass C (2010) Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis. J Neurosci 30: 7853-7862
    • (2010) J Neurosci , vol.30 , pp. 7853-7862
    • Fukumori, A.1    Fluhrer, R.2    Steiner, H.3    Haass, C.4
  • 19
    • 6344265522 scopus 로고    scopus 로고
    • Truncated carboxyl-terminal fragments of β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42
    • Funamoto S, Morishima-Kawashima M, Tanimura Y, Hirotani N, Saido TC, Ihara Y (2004) Truncated carboxyl-terminal fragments of beta-amyloid precursor protein are processed to amyloid betaproteins 40 and 42. Biochemistry 43: 13532-13540 (Pubitemid 39391154)
    • (2004) Biochemistry , vol.43 , Issue.42 , pp. 13532-13540
    • Funamoto, S.1    Morishima-Kawashima, M.2    Tanimura, Y.3    Hirotani, N.4    Saido, T.C.5    Ihara, Y.6
  • 21
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 23
    • 77954602182 scopus 로고    scopus 로고
    • A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity
    • Heilig EA, Xia W, Shen J, Kelleher III RJ (2010) A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of gamma-secretase activity. J Biol Chem 285: 22350-22359
    • (2010) J Biol Chem , vol.285 , pp. 22350-22359
    • Heilig, E.A.1    Xia, W.2    Shen, J.3    Kelleher Iii, R.J.4
  • 25
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1021/bi00069a001
    • Jarrett JT, Berger EP, Lansbury Jr. PT (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 26
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett JT, Lansbury Jr PT (1993) Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055-1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 27
    • 33744957163 scopus 로고    scopus 로고
    • Equimolar production of amyloid β-protein and amyloid precursor protein intracellular domain from β-carboxyl-terminal fragment by γ-secretase
    • DOI 10.1074/jbc.M513453200
    • Kakuda N, Funamoto S, Yagishita S, Takami M, Osawa S, Dohmae N, Ihara Y (2006) Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from betacarboxyl- terminal fragment by gamma-secretase. J Biol Chem 281: 14776-14786 (Pubitemid 43855183)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14776-14786
    • Kakuda, N.1    Funamoto, S.2    Yagishita, S.3    Takami, M.4    Osawa, S.5    Dohmae, N.6    Ihara, Y.7
  • 28
    • 78449272415 scopus 로고    scopus 로고
    • Genetics. Gamma-secretase and human disease
    • Kelleher 3rd RJ, Shen J (2010) Genetics. Gamma-secretase and human disease. Science 330: 1055-1056
    • (2010) Science , vol.330 , pp. 1055-1056
    • Kelleher III, R.J.1    Shen, J.2
  • 35
    • 0033537921 scopus 로고    scopus 로고
    • Enhancement of amyloid β 42 secretion by 28 different presenilin 1 mutations of familial Alzheimer's disease
    • DOI 10.1016/S0304-3940(99)00187-1, PII S0304394099001871
    • Murayama O, Tomita T, Nihonmatsu N, Murayama M, Sun X, Honda T, Iwatsubo T, Takashima A (1999) Enhancement of amyloid beta 42 secretion by 28 different presenilin 1 mutations of familial Alzheimer's disease. Neurosci Lett 265: 61-63 (Pubitemid 29210198)
    • (1999) Neuroscience Letters , vol.265 , Issue.1 , pp. 61-63
    • Murayama, O.1    Tomita, T.2    Nihonmatsu, N.3    Murayama, M.4    Sun, X.5    Honda, T.6    Iwatsubo, T.7    Takashima, A.8
  • 36
    • 0037117314 scopus 로고    scopus 로고
    • FAD-linked mutations in presenilin 1 alter the length of Aβ peptides derived from βAPP transmembrane domain mutants
    • DOI 10.1016/S0925-4439(01)00098-9, PII S0925443901000989
    • Murphy MP, Uljon SN, Golde TE, Wang R (2002) FAD-linked mutations in presenilin 1 alter the length of Abeta peptides derived from betaAPP transmembrane domain mutants. Biochim Biophys Acta 1586: 199-209 (Pubitemid 34311835)
    • (2002) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1586 , Issue.2 , pp. 199-209
    • Murphy M.Paul1    Uljon, S.N.2    Golde, T.E.3    Wang, R.4
  • 37
    • 79851473226 scopus 로고    scopus 로고
    • Gamma-secretase modulators as potential disease modifying anti-alzheimer's drugs
    • Oehlrich D, Berthelot DJ, Gijsen HJ (2011) Gamma-secretase modulators as potential disease modifying anti-alzheimer's drugs. J Med Chem 54: 669-698
    • (2011) J Med Chem , vol.54 , pp. 669-698
    • Oehlrich, D.1    Berthelot, D.J.2    Gijsen, H.J.3
  • 38
    • 38149013121 scopus 로고    scopus 로고
    • Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation
    • Page RM, Baumann K, Tomioka M, Perez-Revuelta BI, Fukumori A, Jacobsen H, Flohr A, Luebbers T, Ozmen L, Steiner H, Haass C (2008) Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation. J Biol Chem 283: 677-683
    • (2008) J Biol Chem , vol.283 , pp. 677-683
    • Page, R.M.1    Baumann, K.2    Tomioka, M.3    Perez-Revuelta, B.I.4    Fukumori, A.5    Jacobsen, H.6    Flohr, A.7    Luebbers, T.8    Ozmen, L.9    Steiner, H.10    Haass, C.11
  • 42
    • 80054976611 scopus 로고    scopus 로고
    • Dissociation between the processivity and total activity of gamma-secretase: Implications for the mechanism of Alzheimer's disease-causing presenilin mutations
    • Quintero-Monzon O, Martin MM, Fernandez MA, Cappello CA, Krzysiak AJ, Osenkowski P, Wolfe MS (2011) Dissociation between the processivity and total activity of gamma-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations. Biochemistry 50: 9023-9035
    • (2011) Biochemistry , vol.50 , pp. 9023-9035
    • Quintero-Monzon, O.1    Martin, M.M.2    Fernandez, M.A.3    Cappello, C.A.4    Krzysiak, A.J.5    Osenkowski, P.6    Wolfe, M.S.7
  • 44
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • DOI 10.1093/embo-reports/kve180
    • Sastre M, Steiner H, Fuchs K, Capell A, Multhaup G, Condron MM, Teplow DB, Haass C (2001) Presenilin-dependent gammasecretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep 2: 835-841 (Pubitemid 32982753)
    • (2001) EMBO Reports , vol.2 , Issue.9 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 49
    • 33847169885 scopus 로고    scopus 로고
    • Decreased Aβ secretion by cells expressing familial Alzheimer's disease-linked mutant presenilin 1
    • DOI 10.1016/j.neures.2006.12.005, PII S0168010206003245
    • Shimojo M, Sahara N, Murayama M, Ichinose H, Takashima A (2007) Decreased Abeta secretion by cells expressing familial Alzheimer's disease-linked mutant presenilin 1. Neurosci Res 57: 446-453 (Pubitemid 46283080)
    • (2007) Neuroscience Research , vol.57 , Issue.3 , pp. 446-453
    • Shimojo, M.1    Sahara, N.2    Murayama, M.3    Ichinose, H.4    Takashima, A.5
  • 50
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • DOI 10.1074/jbc.M405768200
    • Shirotani K, Edbauer D, Prokop S, Haass C, Steiner H (2004) Identification of distinct gamma-secretase complexes with different APH-1 variants. J Biol Chem 279: 41340-41345 (Pubitemid 39313572)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 52
    • 70350451482 scopus 로고    scopus 로고
    • Gamma-secretase: Successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment
    • Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S, Ihara Y (2009) Gamma-secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J Neurosci 29: 13042-13052
    • (2009) J Neurosci , vol.29 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6    Ihara, Y.7
  • 53
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • DOI 10.1016/j.cell.2005.02.008
    • Tanzi RE, Bertram L (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120: 545-555 (Pubitemid 40269768)
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 54
    • 63649118865 scopus 로고    scopus 로고
    • Structure and function of gammasecretase
    • Tolia A, De Strooper B (2009) Structure and function of gammasecretase. Semin Cell Dev Biol 20: 211-218
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 211-218
    • Tolia, A.1    De Strooper, B.2
  • 55
    • 50349097998 scopus 로고    scopus 로고
    • Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of gamma-secretase
    • Tolia A, Horre K, De Strooper B (2008) Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of gamma-secretase. J Biol Chem 283: 19793-19803
    • (2008) J Biol Chem , vol.283 , pp. 19793-19803
    • Tolia, A.1    Horre, K.2    De Strooper, B.3
  • 56
    • 53749105377 scopus 로고    scopus 로고
    • Presenilins: Members of the {gamma}-secretase quartets, but part-time soloists too
    • Wakabayashi T, De Strooper B (2008) Presenilins: members of the {gamma}-secretase quartets, but part-time soloists too. Physiology (Bethesda) 23: 194-204
    • (2008) Physiology (Bethesda) , vol.23 , pp. 194-204
    • Wakabayashi, T.1    De Strooper, B.2
  • 58
    • 33744952846 scopus 로고    scopus 로고
    • Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology
    • DOI 10.1074/jbc.M512574200
    • Wang R, Wang B, He W, Zheng H (2006) Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology. J Biol Chem 281: 15330-15336 (Pubitemid 43855123)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15330-15336
    • Wang, R.1    Wang, B.2    He, W.3    Zheng, H.4
  • 59
    • 77953782609 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domains of presenilin 1: Participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase
    • Watanabe N, Image II I, Takagi S, Tominaga A, Image Image I, Tomita T, Iwatsubo T (2010) Functional analysis of the transmembrane domains of presenilin 1: participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of gamma-secretase. J Biol Chem 285: 19738-19746
    • (2010) J Biol Chem , vol.285 , pp. 19738-19746
    • Watanabe, N.1    Image, I.I.I.2    Takagi, S.3    Tominaga, A.4    Image Image, I.5    Tomita, T.6    Iwatsubo, T.7
  • 61
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with notch processing
    • DOI 10.1021/bi015794o
    • Weidemann A, Eggert S, Reinhard FB, Vogel M, Paliga K, Baier G, Masters CL, Beyreuther K, Evin G (2002) A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41: 2825-2835 (Pubitemid 34168952)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.M.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 62
    • 67649488309 scopus 로고    scopus 로고
    • Abeta43 is more frequent than Abeta40 in amyloid plaque cores from Alzheimer disease brains
    • Welander H, Franberg J, Graff C, Sundstrom E, Winblad B, Tjernberg LO (2009) Abeta43 is more frequent than Abeta40 in amyloid plaque cores from Alzheimer disease brains. J Neurochem 110: 697-706
    • (2009) J Neurochem , vol.110 , pp. 697-706
    • Welander, H.1    Franberg, J.2    Graff, C.3    Sundstrom, E.4    Winblad, B.5    Tjernberg, L.O.6
  • 63
    • 2442421944 scopus 로고    scopus 로고
    • Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons
    • DOI 10.1083/jcb.200403061
    • Wilson CA, Murphy DD, Giasson BI, Zhang B, Trojanowski JQ, Lee VM (2004) Degradative organelles containing mislocalized alphaand beta-synuclein proliferate in presenilin-1 null neurons. J Cell Biol 165: 335-346 (Pubitemid 38649909)
    • (2004) Journal of Cell Biology , vol.165 , Issue.3 , pp. 335-346
    • Wilson, C.A.1    Murphy, D.D.2    Giasson, B.I.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 65
    • 33947242870 scopus 로고    scopus 로고
    • When loss is gain: Reduced presenilin proteolytic function leads to increased Aβ42/Aβ40. Talking Point on the role of presenilin mutations in Alzheimer disease
    • DOI 10.1038/sj.embor.7400896, PII 7400896
    • Wolfe MS (2007) When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep 8: 136-140 (Pubitemid 46420840)
    • (2007) EMBO Reports , vol.8 , Issue.2 , pp. 136-140
    • Wolfe, M.S.1
  • 66
    • 38149056617 scopus 로고    scopus 로고
    • Abeta46 is processed to Abeta40 and Abeta43, but not to Abeta42, in the low density membrane domains
    • Yagishita S, Morishima-Kawashima M, Ishiura S, Ihara Y (2008) Abeta46 is processed to Abeta40 and Abeta43, but not to Abeta42, in the low density membrane domains. J Biol Chem 283: 733-738
    • (2008) J Biol Chem , vol.283 , pp. 733-738
    • Yagishita, S.1    Morishima-Kawashima, M.2    Ishiura, S.3    Ihara, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.