메뉴 건너뛰기




Volumn 8, Issue 2, 2007, Pages 136-140

When loss is gain: Reduced presenilin proteolytic function leads to increased Aβ42/Aβ40. Talking Point on the role of presenilin mutations in Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ANTERIOR PHARYNX DEFECTIVE 1 PROTEIN; ASPARTIC ACID; BETA SECRETASE; EPIDERMAL GROWTH FACTOR RECEPTOR 4; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; GROWTH HORMONE RECEPTOR; HERMES ANTIGEN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; NECTIN 1; NERVE CELL ADHESION MOLECULE; NEU DIFFERENTIATION FACTOR; NICASTRIN; NONSTEROID ANTIINFLAMMATORY AGENT; PRESENILIN 1; PRESENILIN 2; PROTEIN PS2; PROTEINASE; TAU PROTEIN; UVOMORULIN;

EID: 33947242870     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400896     Document Type: Review
Times cited : (171)

References (54)
  • 1
    • 3343005434 scopus 로고    scopus 로고
    • PS1 activates P13K thus inhibiting GSK-3 activity and tau overphosphorylation: Effects of FAD mutations
    • Baki L, Shioi J, Wen P, Shao Z, Schwarzman A, Gama-Sosa M, Neve R, Robakis NK (2004) PS1 activates P13K thus inhibiting GSK-3 activity and tau overphosphorylation: Effects of FAD mutations. EMBO J23: 2586-2596
    • (2004) EMBO , vol.J23 , pp. 2586-2596
    • Baki, L.1    Shioi, J.2    Wen, P.3    Shao, Z.4    Schwarzman, A.5    Gama-Sosa, M.6    Neve, R.7    Robakis, N.K.8
  • 2
    • 30344465740 scopus 로고    scopus 로고
    • Regulation of CRE-dependent transcription by presenilins: Prospects for therapy of Alzheimer's disease
    • Beglopoulos V, Shen J (2006) Regulation of CRE-dependent transcription by presenilins: Prospects for therapy of Alzheimer's disease. Trends Pharmacol Sci 27: 33-40
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 33-40
    • Beglopoulos, V.1    Shen, J.2
  • 4
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimerís disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • Borchelt DR et al (1996) Familial Alzheimerís disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17: 1005-1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1
  • 5
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • Citron M et al (1997) Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat Med 3: 67-72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1
  • 9
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases: New features and familiar faces
    • Esler WP, Wolfe MS (2001) A portrait of Alzheimer secretases: New features and familiar faces. Science 293: 1449-1454
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 11
    • 29644431788 scopus 로고    scopus 로고
    • γ-secretase substrate selectivity can be modulated directly via interaction with a nucleotide binding site
    • Fraering PC, Ye W, Lavoie MJ, Ostaszewski BL, Selkoe DJ, Wolfe MS (2005) γ-secretase substrate selectivity can be modulated directly via interaction with a nucleotide binding site. J Biol Chem 280: 41987-41996
    • (2005) J Biol Chem , vol.280 , pp. 41987-41996
    • Fraering, P.C.1    Ye, W.2    Lavoie, M.J.3    Ostaszewski, B.L.4    Selkoe, D.J.5    Wolfe, M.S.6
  • 12
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis R et al(2002) aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev Cell 3: 85-97
    • (2002) Dev Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 13
    • 33645937614 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase on plasma membrane and endosomes is functionally distinct
    • Fukumori A et al(2006) Presenilin-dependent γ-secretase on plasma membrane and endosomes is functionally distinct, Biochemistry 45: 4907-4914
    • (2006) Biochemistry , vol.45 , pp. 4907-4914
    • Fukumori, A.1
  • 14
    • 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 β-amyloid precursor protein are processed to amyloid β-proteins 40 and 42. Biochemistry 43: 13532-13540
    • (2004) Biochemistry , vol.43 , pp. 13532-13540
    • Funamoto, S.1    Morishima-Kawashima, M.2    Tanimura, Y.3    Hirotani, N.4    Saido, T.C.5    Ihara, Y.6
  • 15
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte C, Tsunozaki M, Hale VA, Priess JR (2002) APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc Natl Acad Sci USA 99: 775-779
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 17
    • 17844390391 scopus 로고    scopus 로고
    • Analysis of Notch function in presomitic mesoderm suggests a γ-secretase-independent role for presenilins in somite differentiation
    • Huppert SS, Ilagan MX, De Strooper B, Kopan R (2005) Analysis of Notch function in presomitic mesoderm suggests a γ-secretase-independent role for presenilins in somite differentiation. Dev Cell 8: 677-688
    • (2005) Dev Cell , vol.8 , pp. 677-688
    • Huppert, S.S.1    Ilagan, M.X.2    De Strooper, B.3    Kopan, R.4
  • 18
    • 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
    • Kakuda N, Funamoto S, Yagishita S, Takami M, Osawa S, Dohmae N, Ihara Y (2006) Equimolar production of amyloid β-protein and amyloid precursor protein intracellular domain from β-carboxyl-terminal fragment by γ-secretase. J Biol Chem 281: 14776-14786
    • (2006) J Biol Chem , vol.281 , pp. 14776-14786
    • Kakuda, N.1    Funamoto, S.2    Yagishita, S.3    Takami, M.4    Osawa, S.5    Dohmae, N.6    Ihara, Y.7
  • 19
    • 0037145062 scopus 로고    scopus 로고
    • Presenilin couples the paired phosphorylation of β-catenin independent of axin. Implications for β-catenin activation in tumorigenesis
    • Kang D, Soriano S, Xia X, Eberhart C, De Strooper B, Zheng H, Koo E (2002) Presenilin couples the paired phosphorylation of β-catenin independent of axin. Implications for β-catenin activation in tumorigenesis. Cell 110: 751
    • (2002) Cell , vol.110 , pp. 751
    • Kang, D.1    Soriano, S.2    Xia, X.3    Eberhart, C.4    De Strooper, B.5    Zheng, H.6    Koo, E.7
  • 21
    • 2942557122 scopus 로고    scopus 로고
    • γ-Secretase: Proteasome of the membrane?
    • Kopan R, Ilagan MX (2004) γ-Secretase: Proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 22
    • 0037590902 scopus 로고    scopus 로고
    • Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities
    • Lai MT et al (2003) Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities. J Biol Chem 278: 22475-22481
    • (2003) J Biol Chem , vol.278 , pp. 22475-22481
    • Lai, M.T.1
  • 23
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E et al (1995) Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269: 973-977
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1
  • 25
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li YM et al(2000) Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405: 689-694
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1
  • 27
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Naslund J, Haroutunian V, Mohs R, Davis KL, Davies P, Greengard P, Buxbaum JD (2000) Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283: 1571-1577
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 31
    • 0032708117 scopus 로고    scopus 로고
    • Antisense-induced reduction of presenilin 1 expression selectively increases the production of amyloid β42 in transfected cells
    • Refolo LM, Eckman C, Prada CM, Yager D, Sambamurti K, Mehta N, Hardy J, Younkin SG (1999) Antisense-induced reduction of presenilin 1 expression selectively increases the production of amyloid β42 in transfected cells. J Neurochem 73: 2383-2388
    • (1999) J Neurochem , vol.73 , pp. 2383-2388
    • Refolo, L.M.1    Eckman, C.2    Prada, C.M.3    Yager, D.4    Sambamurti, K.5    Mehta, N.6    Hardy, J.7    Younkin, S.G.8
  • 32
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev El et al(1995) Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376: 775-778
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, El.1
  • 33
    • 29444442794 scopus 로고    scopus 로고
    • APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy
    • Rovelet-Lecrux A et al(2006) APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nat Genet 38: 24-26
    • (2006) Nat Genet , vol.38 , pp. 24-26
    • Rovelet-Lecrux, A.1
  • 34
    • 0041589353 scopus 로고    scopus 로고
    • Potential link between amyloid β-protein 42 and C-terminal fragment γ 49-99 of β-amyloid precursor protein
    • Sato T et al(2003) Potential link between amyloid β-protein 42 and C-terminal fragment γ 49-99 of β-amyloid precursor protein. J Biol Chem 278: 24294-24301
    • (2003) J Biol Chem , vol.278 , pp. 24294-24301
    • Sato, T.1
  • 35
    • 19444367319 scopus 로고    scopus 로고
    • Blocking the cleavage at midportion between γ- and ε-sites remarkably suppresses the generation of amyloid β-protein
    • Sato T, Tanimura Y, Hirotani N, Saido TC, Morishima-Kawashima M, Ihara Y (2005) Blocking the cleavage at midportion between γ- and ε-sites remarkably suppresses the generation of amyloid β-protein. FEBS Lett 579: 2907-2912
    • (2005) FEBS Lett , vol.579 , pp. 2907-2912
    • Sato, T.1    Tanimura, Y.2    Hirotani, N.3    Saido, T.C.4    Morishima-Kawashima, M.5    Ihara, Y.6
  • 36
    • 11144354609 scopus 로고    scopus 로고
    • Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
    • Saura CA et al(2004) Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration. Neuron 42: 23-36
    • (2004) Neuron , vol.42 , pp. 23-36
    • Saura, C.A.1
  • 37
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimerís disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D et al (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimerís disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 2: 864-870
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 38
    • 0242331600 scopus 로고    scopus 로고
    • A presenilin dimer at the core of the γ-secretase enzyme: Insights from parallel analysis of Notch 1 and APP proteolysis
    • Schroeter EH et al (2003) A presenilin dimer at the core of the γ-secretase enzyme: Insights from parallel analysis of Notch 1 and APP proteolysis. Proc Natl Acad Sci USA 100: 13075-13080
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13075-13080
    • Schroeter, E.H.1
  • 39
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimerís disease
    • Selkoe DJ (1994) Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimerís disease. Annu Rev Cell Biol 10: 373-403
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 40
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ (2002) Alzheimer's disease is a synaptic failure. Science 298: 789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 41
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R et al(1995) Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375: 754-760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 42
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations
    • Song W, Nadeau P, Yuan M, Yang X, Shen J, Yankner BA (1999) Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations. Proc Natl Acad Sci US4 96: 6959-6963
    • (1999) Proc Natl Acad Sci US4 , vol.96 , pp. 6959-6963
    • Song, W.1    Nadeau, P.2    Yuan, M.3    Yang, X.4    Shen, J.5    Yankner, B.A.6
  • 44
    • 33947254814 scopus 로고    scopus 로고
    • Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex
    • Tolia A, Chavez-Gutierrez L, De Strooper B (2006) Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex. J Biol Chem 14: 14
    • (2006) J Biol Chem , vol.14 , pp. 14
    • Tolia, A.1    Chavez-Gutierrez, L.2    De Strooper, B.3
  • 45
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
    • Weggen S et al (2001) A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity. Nature 414: 212-216
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1
  • 46
    • 0037176727 scopus 로고    scopus 로고
    • A novel var ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann A, Eggert S, Reinhard FB, Vogel M, Paliga K, Baier G, Masters CL, Beyreuther K, Evin G (2002) A novel var ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41: 2825-2835
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 47
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B (2002) Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296: 2215-2218
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 48
    • 33646795625 scopus 로고    scopus 로고
    • Shutting down Alzheimer's
    • Wolfe MS (2006) Shutting down Alzheimer's. Sci Am 294: 72-79
    • (2006) Sci Am , vol.294 , pp. 72-79
    • Wolfe, M.S.1
  • 49
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest Alzheimerís γ-secretases are intramembrane-cleaving aspartyl proteases
    • Wolfe MS, Xia W, Moore CL, Leatherwood DD, Ostaszewski B, Donkor IO, Selkoe DJ (1999a) Peptidomimetic probes and molecular modeling suggest Alzheimerís γ-secretases are intramembrane-cleaving aspartyl proteases. Biochemistry 38: 4720-4727
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3    Leatherwood, D.D.4    Ostaszewski, B.5    Donkor, I.O.6    Selkoe, D.J.7
  • 50
    • 0033621152 scopus 로고    scopus 로고
    • Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease
    • Wolfe MS, De Los Angeles J, Miller DD, Xia W, Selkoe DJ (1999b) Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease. Biochemistry 38: 11223-11230
    • (1999) Biochemistry , vol.38 , pp. 11223-11230
    • Wolfe, M.S.1    De Los Angeles, J.2    Miller, D.D.3    Xia, W.4    Selkoe, D.J.5
  • 51
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ (1999c) 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.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 52
    • 33645456502 scopus 로고    scopus 로고
    • DAPT-induced intracellular accumulations of longer amyloid β-proteins: Further implications for the mechanism of intramembrane cleavage by γ-secretase
    • Yagishita S, Morishima-Kawashima M, Tanimura Y, Ishiura S, Ihara Y (2006) DAPT-induced intracellular accumulations of longer amyloid β-proteins: Further implications for the mechanism of intramembrane cleavage by γ-secretase. Biochemistry 45: 3952-3960
    • (2006) Biochemistry , vol.45 , pp. 3952-3960
    • Yagishita, S.1    Morishima-Kawashima, M.2    Tanimura, Y.3    Ishiura, S.4    Ihara, Y.5
  • 53
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu G et al(2000) Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407: 48-54
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 54
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang Z, Nadeau P, Song W, Donoviel D, Yuan M, Bernstein A, Yankner BA (2000) Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nat Cell Biol 2: 463-465
    • (2000) Nat Cell Biol , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donoviel, D.4    Yuan, M.5    Bernstein, A.6    Yankner, B.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.