메뉴 건너뛰기




Volumn 64, Issue 5, 2005, Pages 378-385

Decreased neprilysin immunoreactivity in Alzheimer disease, but not in pathological aging

Author keywords

Alzheimer disease; Amyloid; Neprilysin; Neurofibrillary tangles; Pathological aging; Senile plaques; Synaptic markers; Tau

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; MEMBRANE METALLOENDOPEPTIDASE; SYNAPTOPHYSIN; TAU PROTEIN;

EID: 20944435413     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnen/64.5.378     Document Type: Article
Times cited : (77)

References (46)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 2002;297:353-56
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0027410176 scopus 로고
    • Beta A4 deposits are constant in the brain of the oldest old: An immunocytochemical study of 20 French centenarians
    • Delaere P, He Y, Fayet G, Duyckaerts C, Hauw JJ. Beta A4 deposits are constant in the brain of the oldest old: An immunocytochemical study of 20 French centenarians. Neurobiol Aging 1993;14:191-94
    • (1993) Neurobiol Aging , vol.14 , pp. 191-194
    • Delaere, P.1    He, Y.2    Fayet, G.3    Duyckaerts, C.4    Hauw, J.J.5
  • 3
    • 0029895870 scopus 로고    scopus 로고
    • Neuropathology in controls and demented subjects from the Baltimore Longitudinal Study of Aging
    • Troncoso JC, Martin LJ, Dal Forno D, Kawas CH. Neuropathology in controls and demented subjects from the Baltimore Longitudinal Study of Aging. Neurobiol Aging 1996;17:365-71
    • (1996) Neurobiol Aging , vol.17 , pp. 365-371
    • Troncoso, J.C.1    Martin, L.J.2    Dal Forno, D.3    Kawas, C.H.4
  • 4
    • 0026512066 scopus 로고
    • Identification of normal and pathologic aging in prospectively studied nondemented elderly humans
    • Dickson DW, Crystal HA, Mattiace LA, et al. Identification of normal and pathologic aging in prospectively studied nondemented elderly humans. Neurobiol Aging 1992;13:179-89
    • (1992) Neurobiol Aging , vol.13 , pp. 179-189
    • Dickson, D.W.1    Crystal, H.A.2    Mattiace, L.A.3
  • 5
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J, Dickson DW, Trojanowski JQ, Lee VM. The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp Neurol 1999;815:328-37
    • (1999) Exp Neurol , vol.815 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 7
    • 0011959766 scopus 로고
    • Apolipoprotein-E immunoreactivity is increased in deposits of Alzheimer's disease, but not pathologic aging or diffuse Lewy body disease
    • Iqbal H, Mortimer JA, Winblad B, Wisniewski HM, eds. New York: John Wiley & Sons
    • Dickson DW, Ivanushkin A, Heitner J, Yen S-H, Davies P. Apolipoprotein-E immunoreactivity is increased in deposits of Alzheimer's disease, but not pathologic aging or diffuse Lewy body disease. In: Iqbal H, Mortimer JA, Winblad B, Wisniewski HM, eds. Research Advances in Alzheimer's Disease and Related Disorders. New York: John Wiley & Sons, 1995:371-83
    • (1995) Research Advances in Alzheimer's Disease and Related Disorders , pp. 371-383
    • Dickson, D.W.1    Ivanushkin, A.2    Heitner, J.3    Yen, S.-H.4    Davies, P.5
  • 8
    • 0030250714 scopus 로고    scopus 로고
    • Glycation and microglial reaction in lesions of Alzheimer's disease
    • Dickson DW, Sinicropi S, Yen S-H, et al. Glycation and microglial reaction in lesions of Alzheimer's disease. Neurobiol Aging 1996;17:733-43
    • (1996) Neurobiol Aging , vol.17 , pp. 733-743
    • Dickson, D.W.1    Sinicropi, S.2    Yen, S.-H.3
  • 9
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • Dickson DW. The pathogenesis of senile plaques. J Neuropathol Exp Neurol 1997;56:321-39
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 10
    • 0028179341 scopus 로고
    • Chemical characterization of Abeta 17-42 peptide: A component of diffuse amyloid deposits of Alzheimer disease
    • Gowing E, Roher AE, Woods AS, et al. Chemical characterization of Abeta 17-42 peptide: A component of diffuse amyloid deposits of Alzheimer disease. J Biol Chem 1994;269:10987-90
    • (1994) J Biol Chem , vol.269 , pp. 10987-10990
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3
  • 11
    • 0030300022 scopus 로고    scopus 로고
    • The 'nonamyloidogenic' p3 fragment (amyloid beta17-42) is a major constituent of Down's syndrome cerebellar preamyloid
    • Lalowski M, Golabek A, Lemere CA, et al. The 'nonamyloidogenic' p3 fragment (amyloid beta17-42) is a major constituent of Down's syndrome cerebellar preamyloid. J Biol Chem 1996;271:33623-31
    • (1996) J Biol Chem , vol.271 , pp. 33623-33631
    • Lalowski, M.1    Golabek, A.2    Lemere, C.A.3
  • 12
    • 0035477333 scopus 로고    scopus 로고
    • The cell biology of Alzheimer's disease: Uncovering the secrets of secretases
    • Walter J, Kaether C, Steiner H, Haass C. The cell biology of Alzheimer's disease: Uncovering the secrets of secretases. Curr Opin Neurobiol 2001;11:585-90
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 585-590
    • Walter, J.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 13
    • 0036718272 scopus 로고    scopus 로고
    • Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto H, Cheung BS, Hyman BT, Irizarry MC. Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch Neurol 2002;59:1381-89
    • (2002) Arch Neurol , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 14
    • 0037236622 scopus 로고    scopus 로고
    • Elevated beta-secretase expression and enzymatic activity detected in sporadic Alzheimer disease
    • Yang L, Lindholm BK, Yan R, et al. Elevated beta-secretase expression and enzymatic activity detected in sporadic Alzheimer disease. Nat Med 2003;9:3-4
    • (2003) Nat Med , vol.9 , pp. 3-4
    • Yang, L.1    Lindholm, B.K.2    Yan, R.3
  • 15
    • 18544410708 scopus 로고    scopus 로고
    • The plasmin system is induced by and degrades amyloid-beta aggregates
    • Tucker HM, Kihiko M, Caldwell JN, et al. The plasmin system is induced by and degrades amyloid-beta aggregates. J Neurosci 2000;20:3937-46
    • (2000) J Neurosci , vol.20 , pp. 3937-3946
    • Tucker, H.M.1    Kihiko, M.2    Caldwell, J.N.3
  • 16
    • 0037192120 scopus 로고    scopus 로고
    • Differential effects of proteases involved in intracellular degradation of amyloid-β-protein between detergent-soluble and -insoluble pools in CHO-695 cells
    • Sudoh S, Frosch MR Wolf BA. Differential effects of proteases involved in intracellular degradation of amyloid-β-protein between detergent-soluble and -insoluble pools in CHO-695 cells. Biochem 2002;41:1091-99
    • (2002) Biochem , vol.41 , pp. 1091-1099
    • Sudoh, S.1    Frosch, M.R.2    Wolf, B.A.3
  • 17
    • 0037947406 scopus 로고    scopus 로고
    • Amyloid-beta peptide levels in brain are inversely correlated with insulysin activity levels in vivo
    • Miller BC, Eckman EA, Sambamurti K, et al. Amyloid-beta peptide levels in brain are inversely correlated with insulysin activity levels in vivo. Proc Natl Acad Sci USA 2003;100:6221-26
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6221-6226
    • Miller, B.C.1    Eckman, E.A.2    Sambamurti, K.3
  • 18
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme
    • Eckman EA, Reed DK, Eckman CB. Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme. J Biol Chem 2001;276:24540-48
    • (2001) J Biol Chem , vol.276 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 19
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman EA, Watson M, Marlow L, Sambamurti K, Eckman CB. Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J Biol Chem 2003;278:2081-84
    • (2003) J Biol Chem , vol.278 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 20
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathologic deposition
    • Iwata N, Tsubuki S, Takaki Y, et al. Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathologic deposition. Nat Med 2000;6:143-50
    • (2000) Nat Med , vol.6 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 21
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopeptidases: NEP, ECE, KELL and PEX
    • Turner AJ, Tanzawa K. Mammalian membrane metallopeptidases: NEP, ECE, KELL and PEX. FASEB J 1997;11:355-64
    • (1997) FASEB J , vol.11 , pp. 355-364
    • Turner, A.J.1    Tanzawa, K.2
  • 22
    • 0035112440 scopus 로고    scopus 로고
    • The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function
    • Turner AJ, Isaac RE, Coates D. The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function. Bioessays 2001;23:261-69
    • (2001) Bioessays , vol.23 , pp. 261-269
    • Turner, A.J.1    Isaac, R.E.2    Coates, D.3
  • 23
    • 0036077536 scopus 로고    scopus 로고
    • Beta-amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases?
    • Carson JA, Turner AJ. Beta-amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases? J Neurochem 2002;81:1-8
    • (2002) J Neurochem , vol.81 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 24
    • 19044378626 scopus 로고    scopus 로고
    • Abeta-degrading endopeptidase neprilysin in mouse brain: Synaptic and axonal localization inversely correlating with Abeta pathology
    • Fukami S, Watanabe K, Iwata N, et al. Abeta-degrading endopeptidase neprilysin in mouse brain: Synaptic and axonal localization inversely correlating with Abeta pathology. Neurosci Res 2002;43:39-56
    • (2002) Neurosci Res , vol.43 , pp. 39-56
    • Fukami, S.1    Watanabe, K.2    Iwata, N.3
  • 25
    • 0028952265 scopus 로고
    • Endopeptidase-2411 is the integral membrane peptidase initiating degradation of somatostatin in the hippocampus
    • Barnes K, Doherty S, Turner AJ. Endopeptidase-2411 is the integral membrane peptidase initiating degradation of somatostatin in the hippocampus. J Neurochem 1995;64:1826-32
    • (1995) J Neurochem , vol.64 , pp. 1826-1832
    • Barnes, K.1    Doherty, S.2    Turner, A.J.3
  • 26
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of Abeta-degrading endopeptidase neprilysin in mouse hippocampus upon aging
    • Iwata N, Takaki Y, Fukami S, Tsubuki S, Saido TC. Region-specific reduction of Abeta-degrading endopeptidase neprilysin in mouse hippocampus upon aging. J Neurosci Res 2002;70:493-500
    • (2002) J Neurosci Res , vol.70 , pp. 493-500
    • Iwata, N.1    Takaki, Y.2    Fukami, S.3    Tsubuki, S.4    Saido, T.C.5
  • 27
    • 0037468588 scopus 로고    scopus 로고
    • Aging-related downregulation of neprilysin: A putative beta-amyloid-degrading enzyme in transgenic Tg2576 Alzheimer-like mouse brain is accompanied by an astroglial upregulation in the vicinity of beta-amyloid plaques
    • Apelt J, Ach K, Schliebs R. Aging-related downregulation of neprilysin: A putative beta-amyloid-degrading enzyme in transgenic Tg2576 Alzheimer-like mouse brain is accompanied by an astroglial upregulation in the vicinity of beta-amyloid plaques. Neurosci Lett 2003;339:183-86
    • (2003) Neurosci Lett , vol.339 , pp. 183-186
    • Apelt, J.1    Ach, K.2    Schliebs, R.3
  • 28
    • 0035900189 scopus 로고    scopus 로고
    • Relationship between beta amyloid peptide generating molecules and neprilysin in Alzheimer disease and normal brain
    • Yasojima K, McGeer EG, McGeer PL. Relationship between beta amyloid peptide generating molecules and neprilysin in Alzheimer disease and normal brain. Brain Res 2001;919:115-21
    • (2001) Brain Res , vol.919 , pp. 115-121
    • Yasojima, K.1    McGeer, E.G.2    McGeer, P.L.3
  • 29
    • 0011023561 scopus 로고    scopus 로고
    • Amyloid, PHF-tau, ubiquitin and synaptic markers in the progression of Alzheimer's disease: Immunochemical analysis of frontal cortex from prospectively studied elderly humans
    • Iqbal K, Sisodia SS, Winblad B, eds. New York: John Wiley & Sons, Ltd
    • Wang DS, Cochran E, Bennett DM, Eckman EC, Dickson DW, Amyloid, PHF-tau, ubiquitin and synaptic markers in the progression of Alzheimer's disease: Immunochemical analysis of frontal cortex from prospectively studied elderly humans. In: Iqbal K, Sisodia SS, Winblad B, eds. Alzheimer's Disease: Advances in Etiology, Pathogenesis and Therapeutics. New York: John Wiley & Sons, Ltd, 2001:165-80
    • (2001) Alzheimer's Disease: Advances in Etiology, Pathogenesis and Therapeutics , pp. 165-180
    • Wang, D.S.1    Cochran, E.2    Bennett, D.M.3    Eckman, E.C.4    Dickson, D.W.5
  • 30
    • 85039401011 scopus 로고    scopus 로고
    • Bethesda, MD: Research Services Branch, National Institute of Mental Health. November 17
    • Image J. Bethesda, MD: Research Services Branch, National Institute of Mental Health. November 17, 2004. Available at: http://rsb.info.nih.gov/ij/
    • (2004)
    • Image, J.1
  • 31
    • 0034327279 scopus 로고    scopus 로고
    • Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1
    • Johnson GD, Ahn K. Development of an internally quenched fluorescent substrate selective for endothelin-converting enzyme-1. Anal Biochem 2000;286:112-18
    • (2000) Anal Biochem , vol.286 , pp. 112-118
    • Johnson, G.D.1    Ahn, K.2
  • 32
    • 1842608886 scopus 로고    scopus 로고
    • Decreases in soluble α-synuclein in frontal cortex correlate with cognitive decline in the elderly
    • Wang DS, Bennett DA, Mufson E, Cochran E, Dickson DW. Decreases in soluble α-synuclein in frontal cortex correlate with cognitive decline in the elderly. Neurosci Lett 2004;359:104-8
    • (2004) Neurosci Lett , vol.359 , pp. 104-108
    • Wang, D.S.1    Bennett, D.A.2    Mufson, E.3    Cochran, E.4    Dickson, D.W.5
  • 33
    • 0033766102 scopus 로고    scopus 로고
    • Inhibitor potencies and substrate preference for endothelin-converting enzyme-1 are dramatically affected by pH
    • Fahnoe DC, Knapp J, Johnson GD, Ahn K. Inhibitor potencies and substrate preference for endothelin-converting enzyme-1 are dramatically affected by pH. J Cardiovasc Pharmacol 2000;36(suppl 1):S22-25
    • (2000) J Cardiovasc Pharmacol , vol.36 , Issue.1 SUPPL.
    • Fahnoe, D.C.1    Knapp, J.2    Johnson, G.D.3    Ahn, K.4
  • 34
    • 0034889802 scopus 로고    scopus 로고
    • Contribution of asymmetric synapse loss to lateralizing clinical deficits in frontotemporal dementias
    • Lipton AM, Cullum CM, Satumtira S, et al. Contribution of asymmetric synapse loss to lateralizing clinical deficits in frontotemporal dementias. Arch Neurol 2001;58:1233-39
    • (2001) Arch Neurol , vol.58 , pp. 1233-1239
    • Lipton, A.M.1    Cullum, C.M.2    Satumtira, S.3
  • 35
    • 0034530036 scopus 로고    scopus 로고
    • Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
    • Tokyo
    • Takaki Y, Iwata N, Tsubuki S, et al. Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain. J Biochem (Tokyo) 2000;128:897-902
    • (2000) J Biochem , vol.128 , pp. 897-902
    • Takaki, Y.1    Iwata, N.2    Tsubuki, S.3
  • 36
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher AE, Lowenson JD, Clarke S, et al. Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 1993;268: 3072-83
    • (1993) J Biol Chem , vol.268 , pp. 3072-3083
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 37
    • 0028915895 scopus 로고
    • Amyloid beta protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ42(43)
    • Gravina SA, Ho L, Eckman CB, et al. Amyloid beta protein (Aβ) in Alzheimer's disease brain. Biochemical and immunocytochemical analysis with antibodies specific for forms ending at Aβ40 or Aβ42(43). J Biol Chem 1995;270:7013-16
    • (1995) J Biol Chem , vol.270 , pp. 7013-7016
    • Gravina, S.A.1    Ho, L.2    Eckman, C.B.3
  • 41
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 1998;95:6448-53
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 42
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300:486-89
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 44
    • 0034703979 scopus 로고    scopus 로고
    • Linkage of plasma Aβ42 to a quantitative locus on chromosome 10 in late-onset alzheimer's disease pedigrees
    • Ertekin-Taner N, Graff-Radford N, Younkin LH, et al. Linkage of plasma Aβ42 to a quantitative locus on chromosome 10 in late-onset alzheimer's disease pedigrees. Science 2000;290:2303-4
    • (2000) Science , vol.290 , pp. 2303-2304
    • Ertekin-Taner, N.1    Graff-Radford, N.2    Younkin, L.H.3
  • 45
    • 0034704198 scopus 로고    scopus 로고
    • Evidence for genetic linkage of Alzheimer's disease to chromosome 10q
    • Bertram L, Blacker D, Mullin K, et al. Evidence for genetic linkage of Alzheimer's disease to chromosome 10q. Science 2000;290:2302-3
    • (2000) Science , vol.290 , pp. 2302-2303
    • Bertram, L.1    Blacker, D.2    Mullin, K.3
  • 46
    • 18244373040 scopus 로고    scopus 로고
    • Aβ degradation by endothelin-converting enzymes
    • Saido TC, ed. Georgetown, TX: Landes Bioscience
    • Eckman EA, Eckman CB. Aβ degradation by endothelin-converting enzymes. In: Saido TC, ed. Aβ Metabolism and Alzheimer's Disease. Georgetown, TX: Landes Bioscience, 2003:81-94
    • (2003) Aβ Metabolism and Alzheimer's Disease , pp. 81-94
    • Eckman, E.A.1    Eckman, C.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.