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Volumn 287, Issue 11, 2012, Pages 8641-8651

Phosphorylation of amyloid-β peptide at serine 8 attenuates its clearance via insulin-degrading and angiotensin-converting enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEINS; ANGIOTENSIN-CONVERTING ENZYME; CLEARANCE RATES; DEGRADING ENZYMES; DUAL ROLE; EXTRACELLULAR; INSULIN-DEGRADING ENZYMES; MICROGLIAL CELLS; NEURODEGENERATION; PROTEIN KINASE A; PROTEOLYTIC ACTIVITIES; PROTEOLYTIC DEGRADATION; SECRETASES;

EID: 84863236980     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.279133     Document Type: Article
Times cited : (60)

References (75)
  • 1
    • 33750603844 scopus 로고    scopus 로고
    • Alzheimer's centennial legacy: Prospects for rational therapeutic intervention targeting the Aβ amyloid pathway
    • DOI 10.1093/brain/awl251
    • Masters, C. L., and Beyreuther, K. (2006) Alzheimer's centennial legacy: prospects for rational therapeutic intervention targeting the Aβ amyloid pathway. Brain 129, 2823-2839 (Pubitemid 44684506)
    • (2006) Brain , vol.129 , Issue.11 , pp. 2823-2839
    • Masters, C.L.1    Beyreuther, K.2
  • 2
    • 0035081475 scopus 로고    scopus 로고
    • Alzheimer disease results from the cerebral accumulation and cytotoxicity of amyloid-β protein
    • Selkoe, D. J. (2001) Alzheimer disease results from the cerebral accumulation and cytotoxicity of amyloid-β protein. J. Alzheimers Dis. 3, 75-80
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 75-80
    • Selkoe, D.J.1
  • 3
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper, B., Vassar, R., and 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
  • 4
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer disease: Proteolysis holds the key
    • Haass, C., and De Strooper, B. (1999) The presenilins in Alzheimer disease: proteolysis holds the key. Science 286, 916-919
    • (1999) Science , vol.286 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 5
    • 0024582997 scopus 로고
    • Molecular genetic approaches to Alzheimer's disease
    • Tanzi, R. E., St George-Hyslop, P. H., and Gusella, J. F. (1989) Molecular genetic approaches to Alzheimer disease. Trends Neurosci. 12, 152-158 (Pubitemid 19072593)
    • (1989) Trends in Neurosciences , vol.12 , Issue.4 , pp. 152-158
    • Tanzi, R.E.1    St G.-Hyslop, P.H.2    Gusella, J.F.3
  • 9
    • 33745920161 scopus 로고    scopus 로고
    • Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo
    • DOI 10.1038/nm1438, PII NM1438
    • Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., and Holtzman, D. M. (2006) Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo. Nat. Med. 12, 856-861 (Pubitemid 44050079)
    • (2006) Nature Medicine , vol.12 , Issue.7 , pp. 856-861
    • Bateman, R.J.1    Munsell, L.Y.2    Morris, J.C.3    Swarm, R.4    Yarasheski, K.E.5    Holtzman, D.M.6
  • 11
    • 78651273605 scopus 로고    scopus 로고
    • Clearance of amyloid-β peptide across the choroid plexus in Alzheimer disease
    • Alvira-Botero, X., and Carro, E. M. (2010) Clearance of amyloid-β peptide across the choroid plexus in Alzheimer disease. Curr. Aging Sci. 3, 219-229
    • (2010) Curr. Aging Sci. , vol.3 , pp. 219-229
    • Alvira-Botero, X.1    Carro, E.M.2
  • 12
    • 65649105035 scopus 로고    scopus 로고
    • Clearance of amyloid-β peptide across the blood-brain barrier: Implication for therapies in Alzheimer disease
    • Deane, R., Bell, R. D., Sagare, A., and Zlokovic, B. V. (2009) Clearance of amyloid-β peptide across the blood-brain barrier: implication for therapies in Alzheimer disease. CNS Neurol. Disord. Drug Targets 8, 16-30
    • (2009) CNS Neurol. Disord. Drug Targets , vol.8 , pp. 16-30
    • Deane, R.1    Bell, R.D.2    Sagare, A.3    Zlokovic, B.V.4
  • 15
    • 18144453796 scopus 로고    scopus 로고
    • Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer's disease
    • DOI 10.1006/exnr.1997.6738
    • DeWitt, D. A., Perry, G., Cohen, M., Doller, C., and Silver, J. (1998) Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer disease. Exp. Neurol. 149, 329-340 (Pubitemid 28115071)
    • (1998) Experimental Neurology , vol.149 , Issue.2 , pp. 329-340
    • Dewitt, D.A.1    Perry, G.2    Cohen, M.3    Doller, C.4    Silver, J.5
  • 16
    • 36448938207 scopus 로고    scopus 로고
    • Clearance of amyloid-β peptide by neuronal and non-neuronal cells: Proteolytic degradation by secreted and membrane associated proteases
    • DOI 10.2174/156720207782446315
    • Panchal, M., Lazar, N., Munoz, N., Fahy, C., Clamagirand, C., Brouard, J. P., Dubost, L., Cohen, P., Brakch, N., and Rholam, M. (2007) Clearance of amyloid-β peptide by neuronal and non-neuronal cells: proteolytic degradation by secreted and membrane-associated proteases. Curr. Neurovasc. Res. 4, 240-251 (Pubitemid 350171824)
    • (2007) Current Neurovascular Research , vol.4 , Issue.4 , pp. 240-251
    • Panchal, M.1    Lazar, N.2    Munoz, N.3    Fahy, C.4    Clamagirand, C.5    Brouard, J.-P.6    Dubost, L.7    Cohen, P.8    Brakch, N.9    Rholam, M.10
  • 18
    • 19044378626 scopus 로고    scopus 로고
    • Aβ-degrading endopeptidase, neprilysin, in mouse brain: Synaptic and axonal localization inversely correlating with Aβ pathology
    • DOI 10.1016/S0168-0102(02)00015-9, PII S0168010202000159
    • Fukami, S., Watanabe, K., Iwata, N., Haraoka, J., Lu, B., Gerard, N. P., Gerard, C., Fraser, P., Westaway, D., St George-Hyslop, P., and Saido, T. C. (2002) Aβ-degrading endopeptidase, neprilysin, in mouse brain: synaptic and axonal localization inversely correlating with Aβ pathology. Neurosci. Res. 43, 39-56 (Pubitemid 34628582)
    • (2002) Neuroscience Research , vol.43 , Issue.1 , pp. 39-56
    • Fukami, S.1    Watanabe, K.2    Iwata, N.3    Haraoka, J.4    Lu, B.5    Gerard, N.P.6    Gerard, C.7    Fraser, P.8    Westaway, D.9    George-Hyslop, P.St.10    Saido, T.C.11
  • 19
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme
    • Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D., Hartley, D., Chesneau, V., Rosner, M. R., and Selkoe, D. J. (2000) Neurons regulate extracellular levels of amyloid-β protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20, 1657-1665 (Pubitemid 30220363)
    • (2000) Journal of Neuroscience , vol.20 , Issue.5 , pp. 1657-1665
    • Vekrellis, K.1    Ye, Z.2    Qiu, W.Q.3    Walsh, D.4    Hartley, D.5    Chesneau, V.6    Rosner, M.R.7    Selkoe, D.J.8
  • 20
    • 29844432266 scopus 로고    scopus 로고
    • Insulin, insulin-degrading enzyme and amyloid-β peptide in Alzheimer's disease: Review and hypothesis
    • DOI 10.1016/j.neurobiolaging.2005.01.004, PII S0197458005000199
    • Qiu, W. Q., and Folstein, M. F. (2006) Insulin, insulin-degrading enzyme, and amyloid-β peptide in Alzheimer disease: review and hypothesis. Neurobiol. Aging 27, 190-198 (Pubitemid 43038542)
    • (2006) Neurobiology of Aging , vol.27 , Issue.2 , pp. 190-198
    • Qiu, W.Q.1    Folstein, M.F.2
  • 21
    • 0037593593 scopus 로고    scopus 로고
    • Amyloid-β peptide metabolism and Alzheimer's disease
    • DOI 10.1254/fpj.122.5
    • Iwata, N., and Saido, T. C. (2003) Amyloid-β peptide metabolism and Alzheimer disease. Nippon Yakurigaku Zasshi 122, 5-14 (Pubitemid 36834411)
    • (2003) Folia Pharmacologica Japonica , vol.122 , Issue.1 , pp. 5-14
    • Iwata, N.1    Saido, T.C.2
  • 22
    • 14944344493 scopus 로고    scopus 로고
    • Targeting amyloid-degrading enzymes as therapeutic strategies in neurodegeneration
    • DOI 10.1196/annals.1332.001
    • Turner, A. J., Fisk, L., and Nalivaeva, N. N. (2004) Targeting amyloid-degrading enzymes as therapeutic strategies in neurodegeneration. Ann. N.Y. Acad. Sci. 1035, 1-20 (Pubitemid 40362323)
    • (2004) Annals of the New York Academy of Sciences , vol.1035 , pp. 1-20
    • Turner, A.J.1    Fisk, L.2    Nalivaeva, N.N.3
  • 23
    • 27844442718 scopus 로고    scopus 로고
    • Aβ-degrading enzymes: Modulators of Alzheimer's disease pathogenesis and targets for therapeutic intervention
    • DOI 10.1042/BST20051101
    • Eckman, E. A., and Eckman, C. B. (2005) Aβ-degrading enzymes: modulators of Alzheimer disease pathogenesis and targets for therapeutic intervention. Biochem. Soc. Trans. 33, 1101-1105 (Pubitemid 41659123)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.5 , pp. 1101-1105
    • Eckman, E.A.1    Eckman, C.B.2
  • 24
    • 1842367306 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells
    • DOI 10.1074/jbc.272.10.6641
    • Qiu, W. Q., Ye, Z., Kholodenko, D., Seubert, P., and Selkoe, D. J. (1997) Degradation of amyloid-β protein by a metalloprotease secreted by microglia and other neural and non-neural cells. J. Biol. Chem. 272, 6641-6646 (Pubitemid 27118149)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6641-6646
    • Qiu, W.Q.1    Ye, Z.2    Kholodenko, D.3    Seubert, P.4    Selkoe, D.J.5
  • 25
    • 0022208557 scopus 로고
    • Characterization of an insulin degrading enzyme from cultured human lymphocytes
    • Roth, R. A., Mesirow, M. L., Cassell, D. J., Yokono, K., and Baba, S. (1985) Characterization of an insulin-degrading enzyme from cultured human lymphocytes. Diabetes Res. Clin. Pract. 1, 31-39 (Pubitemid 16073181)
    • (1985) Diabetes Research and Clinical Practice , vol.1 , Issue.1 , pp. 31-39
    • Roth, R.A.1    Mesirow, M.L.2    Cassell, D.J.3
  • 26
    • 60349088206 scopus 로고    scopus 로고
    • Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
    • Zhao, J., Li, L., and Leissring, M. A. (2009) Insulin-degrading enzyme is exported via an unconventional protein secretion pathway. Mol. Neurodegener. 4, 4
    • (2009) Mol. Neurodegener. , vol.4 , pp. 4
    • Zhao, J.1    Li, L.2    Leissring, M.A.3
  • 27
    • 75149166216 scopus 로고    scopus 로고
    • Insulin-degrading enzyme sorting in exosomes: A secretory pathway for a key brain amyloid-β degrading protease
    • Bulloj, A., Leal, M. C., Xu, H., Castano, E. M., and Morelli, L. (2009) Insulin-degrading enzyme sorting in exosomes: A secretory pathway for a key brain amyloid-β degrading protease. J. Alzheimers Dis. 19, 79-95
    • (2009) J. Alzheimers Dis. , vol.19 , pp. 79-95
    • Bulloj, A.1    Leal, M.C.2    Xu, H.3    Castano, E.M.4    Morelli, L.5
  • 28
    • 78549284024 scopus 로고    scopus 로고
    • Statins promote the degradation of extracellular amyloid-β peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (IDE) secretion
    • Tamboli, I. Y., Barth, E., Christian, L., Siepmann, M., Kumar, S., Singh, S., Tolksdorf, K., Heneka, M. T., Lütjohann, D., Wunderlich, P., and Walter, J. (2010) Statins promote the degradation of extracellular amyloid-β peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (IDE) secretion. J. Biol. Chem. 285, 37405-37414
    • (2010) J. Biol. Chem. , vol.285 , pp. 37405-37414
    • Tamboli, I.Y.1    Barth, E.2    Christian, L.3    Siepmann, M.4    Kumar, S.5    Singh, S.6    Tolksdorf, K.7    Heneka, M.T.8    Lütjohann, D.9    Wunderlich, P.10    Walter, J.11
  • 29
    • 79959569095 scopus 로고    scopus 로고
    • Functional relevance of a novel SlyX motif in nonconventional secretion of insulin-degrading enzyme
    • Glebov, K., Schütze, S., and Walter, J. (2011) Functional relevance of a novel SlyX motif in nonconventional secretion of insulin-degrading enzyme. J. Biol. Chem. 286, 22711-22715
    • (2011) J. Biol. Chem. , vol.286 , pp. 22711-22715
    • Glebov, K.1    Schütze, S.2    Walter, J.3
  • 31
  • 33
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • DOI 10.1016/S0896-6273(03)00787-6
    • Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., and Selkoe, D. J. (2003) Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093 (Pubitemid 38032786)
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 35
    • 84862833303 scopus 로고    scopus 로고
    • Phosphorylation of amyloid-β (Aβ) peptides: A trigger for formation of toxic aggregates in Alzheimer disease
    • Kumar, S., and Walter, J. (2011) Phosphorylation of amyloid-β (Aβ) peptides: a trigger for formation of toxic aggregates in Alzheimer disease. Aging 3, 803-812
    • (2011) Aging , vol.3 , pp. 803-812
    • Kumar, S.1    Walter, J.2
  • 37
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass, C., and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer amyloid-β peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 39
    • 48949117577 scopus 로고    scopus 로고
    • The role of the cell surface LRP and soluble LRP in blood-brain barrier Aβ clearance in Alzheimer's disease
    • DOI 10.2174/138161208784705487
    • Deane, R., Sagare, A., and Zlokovic, B. V. (2008) The role of the cell-surface LRP and soluble LRP in blood-brain barrier Aβ clearance in Alzheimer disease. Curr. Pharm. Des. 14, 1601-1605 (Pubitemid 352002987)
    • (2008) Current Pharmaceutical Design , vol.14 , Issue.16 , pp. 1601-1605
    • Dearie, R.1    Sagare, A.2    Zlokovic, B.V.3
  • 41
    • 0023869451 scopus 로고
    • Effect of aging on the blood-brain barrier
    • Mooradian, A. D. (1988) Effect of aging on the blood-brain barrier. Neurobiol. Aging 9, 31-39
    • (1988) Neurobiol. Aging , vol.9 , pp. 31-39
    • Mooradian, A.D.1
  • 42
    • 79954509005 scopus 로고    scopus 로고
    • The early involvement of the innate immunity in the pathogenesis of late-onset Alzheimer disease: Neuropathological, epidemiological, and genetic evidence
    • Eikelenboom, P., Veerhuis, R., van Exel, E., Hoozemans, J. J., Rozemuller, A. J., and van Gool, W. A. (2011) The early involvement of the innate immunity in the pathogenesis of late-onset Alzheimer disease: neuropathological, epidemiological, and genetic evidence. Curr. Alzheimer Res. 8, 142-150
    • (2011) Curr. Alzheimer Res. , vol.8 , pp. 142-150
    • Eikelenboom, P.1    Veerhuis, R.2    Van Exel, E.3    Hoozemans, J.J.4    Rozemuller, A.J.5    Van Gool, W.A.6
  • 44
    • 0034711206 scopus 로고    scopus 로고
    • Degradation of amylin by insulin-degrading enzyme
    • DOI 10.1074/jbc.M006170200
    • Bennett, R. G., Duckworth, W. C., and Hamel, F. G. (2000) Degradation of amylin by insulin-degrading enzyme. J. Biol. Chem. 275, 36621-36625 (Pubitemid 32002062)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 36621-36625
    • Bennett, R.G.1    Duckworth, W.C.2    Hamel, F.G.3
  • 45
    • 0035853781 scopus 로고    scopus 로고
    • Insulin and analogue effects on protein degradation in different cell types. Dissociation between binding and activity
    • Fawcett, J., Hamel, F. G., Bennett, R. G., Vajo, Z., and Duckworth, W. C. (2001) Insulin and analogue effects on protein degradation in different cell types. Dissociation between binding and activity. J. Biol. Chem. 276, 11552-11558
    • (2001) J. Biol. Chem. , vol.276 , pp. 11552-11558
    • Fawcett, J.1    Hamel, F.G.2    Bennett, R.G.3    Vajo, Z.4    Duckworth, W.C.5
  • 46
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: Progress and potential
    • DOI 10.1210/er.19.5.608
    • Duckworth, W. C., Bennett, R. G., and Hamel, F. G. (1998) Insulin degradation: progress and potential. Endocr. Rev. 19, 608-624 (Pubitemid 28467714)
    • (1998) Endocrine Reviews , vol.19 , Issue.5 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 47
    • 0035399887 scopus 로고    scopus 로고
    • Insulin-degrading enzyme: Embarking on amyloid destruction
    • Kurochkin, I. V. (2001) Insulin-degrading enzyme: embarking on amyloid destruction. Trends Biochem. Sci. 26, 421-425
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 421-425
    • Kurochkin, I.V.1
  • 48
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • DOI 10.1038/nature05143, PII NATURE05143
    • Shen, Y., Joachimiak, A., Rosner, M. R., and Tang, W. J. (2006) Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 443, 870-874 (Pubitemid 44622699)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rich, R.M.3    Tang, W.-J.4
  • 50
    • 0345826185 scopus 로고    scopus 로고
    • Phosphorylation of Presenilin 1 at the Caspase Recognition Site Regulates Its Proteolytic Processing and the Progression of Apoptosis
    • DOI 10.1074/jbc.M306653200
    • Fluhrer, R., Friedlein, A., Haass, C., and Walter, J. (2004) Phosphorylation of presenilin-1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis. J. Biol. Chem. 279, 1585-1593 (Pubitemid 38084422)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1585-1593
    • Fluhrer, R.1    Friedlein, A.2    Haass, C.3    Walter, J.4
  • 51
    • 33747401659 scopus 로고    scopus 로고
    • Tau phosphorylation and proteolysis: Insights and perspectives
    • Johnson, G. V. (2006) Tau phosphorylation and proteolysis: insights and perspectives. J. Alzheimers Dis. 9, 243-250
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 243-250
    • Johnson, G.V.1
  • 53
    • 0036077536 scopus 로고    scopus 로고
    • Beta-amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases?
    • DOI 10.1046/j.1471-4159.2002.00855.x
    • Carson, J. A., and Turner, A. J. (2002) Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases? J. Neurochem. 81, 1-8 (Pubitemid 34808849)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.1 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 55
    • 36148979336 scopus 로고    scopus 로고
    • In vitro and in vivo degradation of Aβ peptide by peptidases coupled to erythrocytes
    • DOI 10.1016/j.peptides.2007.09.015, PII S0196978107003932
    • Liu, Y., Guan, H., Beckett, T. L., Juliano, M. A., Juliano, L., Song, E. S., Chow, K. M., Murphy, M. P., and Hersh, L. B. (2007) In vitro and in vivo degradation of Aβ peptide by peptidases coupled to erythrocytes. Peptides 28, 2348-2355 (Pubitemid 350116309)
    • (2007) Peptides , vol.28 , Issue.12 , pp. 2348-2355
    • Liu, Y.1    Guan, H.2    Beckett, T.L.3    Juliano, M.A.4    Juliano, L.5    Song, E.S.6    Chow, K.M.7    Murphy, M.P.8    Hersh, L.B.9
  • 56
    • 0029061685 scopus 로고
    • Neutral endopeptidase can hydrolyze β-amyloid(1-40) but shows no effect on β-amyloid precursor protein metabolism
    • Howell, S., Nalbantoglu, J., and Crine, P. (1995) Neutral endopeptidase can hydrolyze β-amyloid(1-40) but shows no effect on β-amyloid precursor protein metabolism. Peptides 16, 647-652
    • (1995) Peptides , vol.16 , pp. 647-652
    • Howell, S.1    Nalbantoglu, J.2    Crine, P.3
  • 57
    • 49549098365 scopus 로고    scopus 로고
    • Aggregation and catabolism of disease-associated intra-Aβ mutations: Reduced proteolysis of Aβ A21G by neprilysin
    • Betts, V., Leissring, M. A., Dolios, G., Wang, R., Selkoe, D. J., and Walsh, D. M. (2008) Aggregation and catabolism of disease-associated intra-Aβ mutations: reduced proteolysis of Aβ A21G by neprilysin. Neurobiol. Dis. 31, 442-450
    • (2008) Neurobiol. Dis. , vol.31 , pp. 442-450
    • Betts, V.1    Leissring, M.A.2    Dolios, G.3    Wang, R.4    Selkoe, D.J.5    Walsh, D.M.6
  • 58
    • 27344441173 scopus 로고    scopus 로고
    • Metabolism of amyloid-β peptide and Alzheimer's disease
    • DOI 10.1016/j.pharmthera.2005.03.010, PII S0163725805000999
    • Iwata, N., Higuchi, M., and Saido, T. C. (2005) Metabolism of amyloid-β peptide and Alzheimer disease. Pharmacol. Ther. 108, 129-148 (Pubitemid 41527082)
    • (2005) Pharmacology and Therapeutics , vol.108 , Issue.2 , pp. 129-148
    • Iwata, N.1    Higuchi, M.2    Saido, T.C.3
  • 59
    • 77956613606 scopus 로고    scopus 로고
    • Plasminogen and plasmin in Alzheimer disease
    • Barker, R., Love, S., and Kehoe, P. G. (2010) Plasminogen and plasmin in Alzheimer disease. Brain Res. 1355, 7-15
    • (2010) Brain Res. , vol.1355 , pp. 7-15
    • Barker, R.1    Love, S.2    Kehoe, P.G.3
  • 60
    • 16844363404 scopus 로고    scopus 로고
    • Tissue plasminogen activator in central nervous system physiology and pathology
    • DOI 10.1160/TH04-12-0838
    • Melchor, J. P., and Strickland, S. (2005) Tissue plasminogen activator in central nervous system physiology and pathology. Thromb Haemost. 93, 655-660 (Pubitemid 40485400)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.4 , pp. 655-660
    • Melchor, J.P.1    Strickland, S.2
  • 61
    • 0037833494 scopus 로고    scopus 로고
    • Emotions are building up in the field of extracellular proteolysis
    • DOI 10.1016/S1471-4914(03)00050-9
    • Madani, R., Nef, S., and Vassalli, J. D. (2003) Emotions are building up in the field of extracellular proteolysis. Trends Mol. Med. 9, 183-185 (Pubitemid 36713386)
    • (2003) Trends in Molecular Medicine , vol.9 , Issue.5 , pp. 183-185
    • Madani, R.1    Nef, S.2    Vassalli, J.-D.3
  • 63
    • 0033788789 scopus 로고    scopus 로고
    • Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition
    • Tucker, H. M., Kihiko-Ehmann, M., Wright, S., Rydel, R. E., and Estus, S. (2000) Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition. J. Neurochem. 75, 2172-2177
    • (2000) J. Neurochem. , vol.75 , pp. 2172-2177
    • Tucker, H.M.1    Kihiko-Ehmann, M.2    Wright, S.3    Rydel, R.E.4    Estus, S.5
  • 66
    • 67649665617 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme levels and activity in Alzheimer disease: Differences in brain and cerebrospinal fluid ACE and association with ACE1 genotypes
    • Miners, S., Ashby, E., Baig, S., Harrison, R., Tayler, H., Speedy, E., Prince, J. A., Love, S., and Kehoe, P. G. (2009) Angiotensin-converting enzyme levels and activity in Alzheimer disease: differences in brain and cerebrospinal fluid ACE and association with ACE1 genotypes. Am. J. Transl. Res. 1, 163-177
    • (2009) Am. J. Transl. Res. , vol.1 , pp. 163-177
    • Miners, S.1    Ashby, E.2    Baig, S.3    Harrison, R.4    Tayler, H.5    Speedy, E.6    Prince, J.A.7    Love, S.8    Kehoe, P.G.9
  • 67
    • 42249095648 scopus 로고    scopus 로고
    • Confronting complexity in late-onset Alzheimer disease: Application of two-stage analysis approach addressing heterogeneity and epistasis
    • DOI 10.1002/gepi.20294
    • Thornton-Wells, T. A., Moore, J. H., Martin, E. R., Pericak-Vance, M. A., and Haines, J. L. (2008) Confronting complexity in late-onset Alzheimer disease: application of two-stage analysis approach addressing heterogeneity and epistasis. Genet. Epidemiol. 32, 187-203 (Pubitemid 351550366)
    • (2008) Genetic Epidemiology , vol.32 , Issue.3 , pp. 187-203
    • Thornton-Wells, T.A.1    Moore, J.H.2    Martin, E.R.3    Pericak-Vance, M.A.4    Haines, J.L.5
  • 71
    • 14944340658 scopus 로고    scopus 로고
    • The N-terminal active centre of human angiotensin-converting enzyme degrades Alzheimer amyloid β-peptide
    • DOI 10.1111/j.1460-9568.2005.03912.x
    • Oba, R., Igarashi, A., Kamata, M., Nagata, K., Takano, S., and Nakagawa, H. (2005) The N-terminal active center of human angiotensin-converting enzyme degrades Alzheimer amyloid-β peptide. Eur. J. Neurosci. 21, 733-740 (Pubitemid 40363508)
    • (2005) European Journal of Neuroscience , vol.21 , Issue.3 , pp. 733-740
    • Oba, R.1    Igarashi, A.2    Kamata, M.3    Nagata, K.4    Takano, S.5    Nakagawa, H.6
  • 72
    • 27844534846 scopus 로고    scopus 로고
    • Amyloid β-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor
    • DOI 10.1074/jbc.M508460200
    • Hemming, M. L., and Selkoe, D. J. (2005) Amyloid-β protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor. J. Biol. Chem. 280, 37644-37650 (Pubitemid 41642372)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37644-37650
    • Hemming, M.L.1    Selkoe, D.J.2
  • 73
    • 0035930538 scopus 로고    scopus 로고
    • Angiotensinconverting enzyme degrades Alzheimer amyloid-β peptide (Aβ); retards Aβ aggregation, deposition, fibril formation; and inhibits cytotoxicity
    • Hu, J., Igarashi, A., Kamata, M., and Nakagawa, H. (2001) Angiotensinconverting enzyme degrades Alzheimer amyloid-β peptide (Aβ); retards Aβ aggregation, deposition, fibril formation; and inhibits cytotoxicity. J. Biol. Chem. 276, 47863-47868
    • (2001) J. Biol. Chem. , vol.276 , pp. 47863-47868
    • Hu, J.1    Igarashi, A.2    Kamata, M.3    Nakagawa, H.4
  • 74
    • 15944383442 scopus 로고    scopus 로고
    • Phosphorylated amyloid-β: The toxic intermediate in Alzheimer disease neurodegeneration
    • Milton, N. G. (2005) Phosphorylated amyloid-β: the toxic intermediate in Alzheimer disease neurodegeneration. Subcell. Biochem. 38, 381- 402
    • (2005) Subcell. Biochem. , vol.38 , pp. 381-402
    • Milton, N.G.1
  • 75
    • 0035807929 scopus 로고    scopus 로고
    • Phosphorylation of amyloid-β at the serine 26 residue by human Cdc2 kinase
    • Milton, N. G. (2001) Phosphorylation of amyloid-β at the serine 26 residue by human Cdc2 kinase. Neuroreport 12, 3839-3844
    • (2001) Neuroreport , vol.12 , pp. 3839-3844
    • Milton, N.G.1


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