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Volumn 9, Issue 2, 2012, Pages 165-177

Alpha-secretase cleavage of the amyloid precursor protein: Proteolysis regulated by signaling pathways and protein trafficking

Author keywords

Alzheimer's disease; Ectodomain shedding; Metalloprotease; Neurodegeneration; Protein trafficking; Regulated intramembrane proteolysis; Secretases; Signaling pathways

Indexed keywords

ADAM PROTEIN; ADAM10 ENDOPEPTIDASE; ADAM17 PROTEIN; ADAM9 PROTEIN; ADENYLATE CYCLASE; AF 267B; ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE 1; CEVIMELINE; CHOLINERGIC RECEPTOR STIMULATING AGENT; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIACYLGLYCEROL; EHT 0202; ETAZOLATE; G PROTEIN COUPLED RECEPTOR; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; MITOGEN ACTIVATED PROTEIN KINASE; NERVE GROWTH FACTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C; PROTEIN KINASE C; SIRTUIN 1; TISSUE INHIBITOR OF METALLOPROTEINASE 3; UNCLASSIFIED DRUG;

EID: 84857775196     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/156720512799361655     Document Type: Review
Times cited : (63)

References (162)
  • 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 (NY 297: 353-6 (2002).
    • (2002) Science (NY , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid betapeptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid betapeptide. Nature reviews 8: 101-12 (2007).
    • (2007) Nature Reviews , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 3
    • 42149130900 scopus 로고    scopus 로고
    • BACE1 structure and function in health and Alzheimer's disease
    • Cole SL, Vassar R. BACE1 structure and function in health and Alzheimer's disease. Current Alzheimer research 5: 100-20 (2008).
    • (2008) Current Alzheimer Research , vol.5 , pp. 100-120
    • Cole, S.L.1    Vassar, R.2
  • 4
    • 33747347875 scopus 로고    scopus 로고
    • Transcriptional and translational regulation of BACE1 expression--implications for Alzheimer's disease
    • Rossner S, Sastre M, Bourne K, Lichtenthaler SF. Transcriptional and translational regulation of BACE1 expression--implications for Alzheimer's disease. Progress in neurobiology 79: 95-111 (2006).
    • (2006) Progress in Neurobiology , vol.79 , pp. 95-111
    • Rossner, S.1    Sastre, M.2    Bourne, K.3    Lichtenthaler, S.F.4
  • 5
    • 79955663580 scopus 로고    scopus 로고
    • Regulated Intramembrane Proteolysis - Lessons from Amyloid Precursor Protein Processing
    • Lichtenthaler SF, Haass C, Steiner H. Regulated Intramembrane Proteolysis - Lessons from Amyloid Precursor Protein Processing. J Neurochem 117: 779-796 (2011).
    • (2011) J Neurochem , vol.117 , pp. 779-796
    • Lichtenthaler, S.F.1    Haass, C.2    Steiner, H.3
  • 6
    • 44449159903 scopus 로고    scopus 로고
    • P3 peptide, a truncated form of A beta devoid of synaptotoxic effect, does not assemble into soluble oligomers
    • Dulin F, Leveille F, Ortega JB, Mornon JP, Buisson A, Callebaut I, et al. P3 peptide, a truncated form of A beta devoid of synaptotoxic effect, does not assemble into soluble oligomers. FEBS Lett 582: 1865-70 (2008).
    • (2008) FEBS Lett , vol.582 , pp. 1865-1870
    • Dulin, F.1    Leveille, F.2    Ortega, J.B.3    Mornon, J.P.4    Buisson, A.5    Callebaut, I.6
  • 7
    • 0029935765 scopus 로고    scopus 로고
    • Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons
    • Simons M, Destrooper B, Multhaup G, Tienari PJ, Dotti CG, Beyreuther K. Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons. J Neurosci 16: 899-908 (1996).
    • (1996) J Neurosci , vol.16 , pp. 899-908
    • Simons, M.1    Destrooper, B.2    Multhaup, G.3    Tienari, P.J.4    Dotti, C.G.5    Beyreuther, K.6
  • 8
    • 63649141727 scopus 로고    scopus 로고
    • The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: Physiological and cellular functions
    • Reiss K, Saftig P. The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: Physiological and cellular functions. Semin Cell Dev Biol 20: 126-37 (2009).
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 10
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich S, Kojro E, Postina R, Gilbert S, Pfeiffer R, Jasionowski M, et al. Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Nat Acad Sci USA 96: 3922-7 (1999).
    • (1999) Proc Nat Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6
  • 11
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme
    • Slack BE, Ma LK, Seah CC. Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme. J. Biochem 357: 787-94 (2001).
    • (2001) J. Biochem. , vol.357 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 12
    • 0033569653 scopus 로고    scopus 로고
    • Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein
    • Koike H, Tomioka S, Sorimachi H, Saido TC, Maruyama K, Okuyama A, et al. Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein. J Biochem 343 Pt 2: 371-5 (1999).
    • (1999) J Biochem , vol.343 , Issue.PART 2 , pp. 371-375
    • Koike, H.1    Tomioka, S.2    Sorimachi, H.3    Saido, T.C.4    Maruyama, K.5    Okuyama, A.6
  • 13
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, Peschon JJ, et al. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273: 27765-7. (1998).
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6
  • 14
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts
    • Hartmann D, de Strooper B, Serneels L, Craessaerts K, Herreman A, Annaert W, et al. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. Hum Mol Genet 11: 2615-24 (2002).
    • (2002) Hum Mol Genet , vol.11 , pp. 2615-2624
    • Hartmann, D.1    de Strooper, B.2    Serneels, L.3    Craessaerts, K.4    Herreman, A.5    Annaert, W.6
  • 15
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • Weskamp G, Cai H, Brodie TA, Higashyama S, Manova K, Ludwig T, et al. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol Cell Biol 22: 1537-44 (2002).
    • (2002) Mol Cell Biol , vol.22 , pp. 1537-1544
    • Weskamp, G.1    Cai, H.2    Brodie, T.A.3    Higashyama, S.4    Manova, K.5    Ludwig, T.6
  • 17
    • 69249128689 scopus 로고    scopus 로고
    • Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein
    • Taylor DR, Parkin ET, Cocklin SL, Ault JR, Ashcroft AE, Turner AJ, et al. Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein. J Biol Chem 284: 22590-600 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 22590-22600
    • Taylor, D.R.1    Parkin, E.T.2    Cocklin, S.L.3    Ault, J.R.4    Ashcroft, A.E.5    Turner, A.J.6
  • 18
    • 3042643033 scopus 로고    scopus 로고
    • The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein
    • Allinson TM, Parkin ET, Condon TP, Schwager SL, Sturrock ED, Turner AJ, et al. The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein. Eur J Biochem 271: 2539-47 (2004).
    • (2004) Eur J Biochem , vol.271 , pp. 2539-2547
    • Allinson, T.M.1    Parkin, E.T.2    Condon, T.P.3    Schwager, S.L.4    Sturrock, E.D.5    Turner, A.J.6
  • 19
    • 21444459918 scopus 로고    scopus 로고
    • P2Y2 nucleotide receptors enhance alpha-secretasedependent amyloid precursor protein processing
    • Camden JM, Schrader AM, Camden RE, Gonzalez FA, Erb L, Seye CI, et al. P2Y2 nucleotide receptors enhance alpha-secretasedependent amyloid precursor protein processing. J Biol Chem 280: 18696-702 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 18696-18702
    • Camden, J.M.1    Schrader, A.M.2    Camden, R.E.3    Gonzalez, F.A.4    Erb, L.5    Seye, C.I.6
  • 20
    • 61349099466 scopus 로고    scopus 로고
    • The effects of alpha-secretase ADAM10 on the proteolysis of neuregulin-1
    • Freese C, Garratt AN, Fahrenholz F, Endres K. The effects of alpha-secretase ADAM10 on the proteolysis of neuregulin-1. FEBS J 276: 1568-80 (2009).
    • (2009) FEBS J , vol.276 , pp. 1568-1580
    • Freese, C.1    Garratt, A.N.2    Fahrenholz, F.3    Endres, K.4
  • 21
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons
    • Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart JW, et al. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J 29: 3020-32 (2010).
    • (2010) EMBO J , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5    Ellwart, J.W.6
  • 22
    • 77950613181 scopus 로고    scopus 로고
    • The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex
    • Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, et al. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci 30: 4833-44 (2010).
    • (2010) J Neurosci , vol.30 , pp. 4833-4844
    • Jorissen, E.1    Prox, J.2    Bernreuther, C.3    Weber, S.4    Schwanbeck, R.5    Serneels, L.6
  • 23
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • Postina R, Schroeder A, Dewachter I, Bohl J, Schmitt U, Kojro E, et al. A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin Invest 113: 1456-64 (2004).
    • (2004) J Clin Invest , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3    Bohl, J.4    Schmitt, U.5    Kojro, E.6
  • 24
    • 33645799439 scopus 로고    scopus 로고
    • The neuropeptide PACAP promotes the alphasecretase pathway for processing the Alzheimer amyloid precursor protein
    • Kojro E, Postina R, Buro C, Meiringer C, Gehrig-Burger K, Fahrenholz F. The neuropeptide PACAP promotes the alphasecretase pathway for processing the Alzheimer amyloid precursor protein. FASEB J 20: 512-4 (2006).
    • (2006) FASEB J , vol.20 , pp. 512-514
    • Kojro, E.1    Postina, R.2    Buro, C.3    Meiringer, C.4    Gehrig-Burger, K.5    Fahrenholz, F.6
  • 25
    • 78650166808 scopus 로고    scopus 로고
    • alpha-secretase in Alzheimer's disease: Molecular identity, regulation and therapeutic potential
    • [Lichtenthaler SF. alpha-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potential. Journal of neurochemistry 116: 10-21 (2011).
    • (2011) Journal of Neurochemistry , vol.116 , pp. 10-21
    • Lichtenthaler, S.F.1
  • 26
    • 42149110867 scopus 로고    scopus 로고
    • Part-time alpha-secretases: The functional biology of ADAM 9, 10 and 17
    • Deuss M, Reiss K, Hartmann D. Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17. Curr Alzheim Res 5: 187-201 (2008).
    • (2008) Curr Alzheim Res , vol.5 , pp. 187-201
    • Deuss, M.1    Reiss, K.2    Hartmann, D.3
  • 27
    • 79959196089 scopus 로고    scopus 로고
    • Determination of the Proteolytic Cleavage Sites of the Amyloid Precursor-Like Protein 2 by the Proteases ADAM10, BACE1 and a-Secretase
    • Hogl S, Kuhn PH, Colombo A, Lichtenthaler SF. Determination of the Proteolytic Cleavage Sites of the Amyloid Precursor-Like Protein 2 by the Proteases ADAM10, BACE1 and a-Secretase. PLOS One 6: e21337 (2011).
    • (2011) PLOS One , vol.6
    • Hogl, S.1    Kuhn, P.H.2    Colombo, A.3    Lichtenthaler, S.F.4
  • 28
    • 77949595824 scopus 로고    scopus 로고
    • Upregulation of the alpha-secretase ADAM10--risk or reason for hope?
    • Endres K, Fahrenholz F. Upregulation of the alpha-secretase ADAM10--risk or reason for hope? FEBS J 277: 1585-96 (2010).
    • (2010) FEBS J , vol.277 , pp. 1585-1596
    • Endres, K.1    Fahrenholz, F.2
  • 29
    • 63949088562 scopus 로고    scopus 로고
    • Function, regulation and therapeutic properties of beta-secretase (BACE1)
    • Willem M, Lammich S, Haass C. Function, regulation and therapeutic properties of beta-secretase (BACE1). Semin Cell Dev Biol 20: 175-82 (2009).
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 175-182
    • Willem, M.1    Lammich, S.2    Haass, C.3
  • 30
    • 24644483112 scopus 로고    scopus 로고
    • Genomic structure and functional characterization of the human ADAM10 promoter
    • Prinzen C, Muller U, Endres K, Fahrenholz F, Postina R. Genomic structure and functional characterization of the human ADAM10 promoter. FASEB J 19: 1522-4 (2005).
    • (2005) FASEB J , vol.19 , pp. 1522-1524
    • Prinzen, C.1    Muller, U.2    Endres, K.3    Fahrenholz, F.4    Postina, R.5
  • 32
    • 67649359888 scopus 로고    scopus 로고
    • Upregulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin
    • Tippmann F, Hundt J, Schneider A, Endres K, Fahrenholz F. Upregulation of the alpha-secretase ADAM10 by retinoic acid receptors and acitretin. FASEB J 23: 1643-1654 (2009).
    • (2009) FASEB J , vol.23 , pp. 1643-1654
    • Tippmann, F.1    Hundt, J.2    Schneider, A.3    Endres, K.4    Fahrenholz, F.5
  • 33
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • Donmez G, Wang D, Cohen DE, Guarente L. SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10. Cell 142: 320-32 (2010).
    • (2010) Cell , vol.142 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 34
    • 77952337371 scopus 로고    scopus 로고
    • Expression of the anti-amyloidogenic secretase ADAM10 is suppressed by its 5'-untranslated region
    • Lammich S, Buell D, Zilow S, Ludwig AK, Nuscher B, Lichtenthaler SF, et al. Expression of the anti-amyloidogenic secretase ADAM10 is suppressed by its 5'-untranslated region. J Biol Chem 285: 15753-60 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 15753-15760
    • Lammich, S.1    Buell, D.2    Zilow, S.3    Ludwig, A.K.4    Nuscher, B.5    Lichtenthaler, S.F.6
  • 35
    • 0029863203 scopus 로고    scopus 로고
    • Metabolism of Alzheimer beta-amyloid precursor protein: Regulation by protein kinase A in intact cells and in a cell-free system
    • Xu H, Sweeney D, Greengard P, Gandy S. Metabolism of Alzheimer beta-amyloid precursor protein: regulation by protein kinase A in intact cells and in a cell-free system. Proc Nat Acad Sci USA 93: 4081-4 (1996).
    • (1996) Proc Nat Acad Sci USA , vol.93 , pp. 4081-4084
    • Xu, H.1    Sweeney, D.2    Greengard, P.3    Gandy, S.4
  • 36
    • 0032436113 scopus 로고    scopus 로고
    • Posttranscriptional contribution of a cAMP-dependent pathway to the formation of alpha- and beta/gamma-secretases-derived products of beta APP maturation in human cells expressing wild-type and Swedish mutated beta APP
    • Marambaud P, Chevallier N, Ancolio K, Checler F. Posttranscriptional contribution of a cAMP-dependent pathway to the formation of alpha- and beta/gamma-secretases-derived products of beta APP maturation in human cells expressing wild-type and Swedish mutated beta APP. Mol Med 4: 715-23. (1998).
    • (1998) Mol Med , vol.4 , pp. 715-723
    • Marambaud, P.1    Chevallier, N.2    Ancolio, K.3    Checler, F.4
  • 37
    • 0029805807 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the proteasome: A contribution to the alphasecretase pathway in human cells
    • Marambaud P, Wilk S, Checler F. Protein kinase A phosphorylation of the proteasome: a contribution to the alphasecretase pathway in human cells. J Neurochem 67: 2616-9 (1996).
    • (1996) J Neurochem , vol.67 , pp. 2616-2619
    • Marambaud, P.1    Wilk, S.2    Checler, F.3
  • 38
    • 36749037180 scopus 로고    scopus 로고
    • Role of the APP non-amyloidogenic signaling pathway and targeting alphasecretase as an alternative drug target for treatment of Alzheimer's disease
    • Bandyopadhyay S, Goldstein LE, Lahiri DK, Rogers JT. Role of the APP non-amyloidogenic signaling pathway and targeting alphasecretase as an alternative drug target for treatment of Alzheimer's disease. Curr Med Chem 14: 2848-64 (2007).
    • (2007) Curr Med Chem , vol.14 , pp. 2848-2864
    • Bandyopadhyay, S.1    Goldstein, L.E.2    Lahiri, D.K.3    Rogers, J.T.4
  • 39
    • 63849136153 scopus 로고    scopus 로고
    • Protein kinase Cisoforms: Multi-functional regulators of cell life and death
    • Reyland ME. Protein kinase Cisoforms: Multi-functional regulators of cell life and death. Front Biosci 14: 2386-99 (2009).
    • (2009) Front Biosci , vol.14 , pp. 2386-2399
    • Reyland, M.E.1
  • 40
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch RM, Slack BE, Wurtman RJ, Growdon JH. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science (NY 258: 304-7 (1992).
    • (1992) Science (NY , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 41
    • 0028935040 scopus 로고
    • Tyrosine phosphorylation-dependent stimulation of amyloid precursor protein secretion by the m3 muscarinic acetylcholine receptor
    • Slack BE, Breu J, Petryniak MA, Srivastava K, Wurtman RJ. Tyrosine phosphorylation-dependent stimulation of amyloid precursor protein secretion by the m3 muscarinic acetylcholine receptor. J Biol Chem 270: 8337-44 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 8337-8344
    • Slack, B.E.1    Breu, J.2    Petryniak, M.A.3    Srivastava, K.4    Wurtman, R.J.5
  • 42
    • 55249118679 scopus 로고    scopus 로고
    • Novel selective allosteric activator of the M1 muscarinic acetylcholine receptor regulates amyloid processing and produces antipsychotic-like activity in rats
    • Jones CK, Brady AE, Davis AA, Xiang Z, Bubser M, Tantawy MN, et al. Novel selective allosteric activator of the M1 muscarinic acetylcholine receptor regulates amyloid processing and produces antipsychotic-like activity in rats. J Neurosci 28: 10422-33 (2008).
    • (2008) J Neurosci , vol.28 , pp. 10422-10433
    • Jones, C.K.1    Brady, A.E.2    Davis, A.A.3    Xiang, Z.4    Bubser, M.5    Tantawy, M.N.6
  • 44
    • 0037183770 scopus 로고    scopus 로고
    • Effect of a 5- HT(2C) serotonin agonist, dexnorfenfluramine, on amyloid precursor protein metabolism in guinea pigs
    • Arjona AA, Pooler AM, Lee RK, Wurtman RJ. Effect of a 5- HT(2C) serotonin agonist, dexnorfenfluramine, on amyloid precursor protein metabolism in guinea pigs. Brain Res 951: 135-40 (2002).
    • (2002) Brain Res , vol.951 , pp. 135-140
    • Arjona, A.A.1    Pooler, A.M.2    Lee, R.K.3    Wurtman, R.J.4
  • 45
    • 0030028598 scopus 로고    scopus 로고
    • Serotonin 5- HT2a and 5-HT2c receptors stimulate amyloid precursor protein ectodomain secretion
    • Nitsch RM, Deng M, Growdon JH, Wurtman RJ. Serotonin 5- HT2a and 5-HT2c receptors stimulate amyloid precursor protein ectodomain secretion. J Biol Chem 271: 4188-94 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 4188-4194
    • Nitsch, R.M.1    Deng, M.2    Growdon, J.H.3    Wurtman, R.J.4
  • 46
    • 0032577677 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein secretion by glutamate receptors in human Ntera 2 neurons
    • Jolly-Tornetta C, Gao ZY, Lee VM, Wolf BA. Regulation of amyloid precursor protein secretion by glutamate receptors in human Ntera 2 neurons. J Biol Chem 273: 14015-21 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 14015-14021
    • Jolly-Tornetta, C.1    Gao, Z.Y.2    Lee, V.M.3    Wolf, B.A.4
  • 47
    • 0029147583 scopus 로고
    • Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors
    • Lee RK, Wurtman RJ, Cox AJ, Nitsch RM. Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors. Proc Nat Acad Sci USA 92: 8083-7 (1995).
    • (1995) Proc Nat Acad Sci USA , vol.92 , pp. 8083-8087
    • Lee, R.K.1    Wurtman, R.J.2    Cox, A.J.3    Nitsch, R.M.4
  • 48
    • 0025296205 scopus 로고
    • Processing of Alzheimer beta/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation
    • Buxbaum JD, Gandy SE, Cicchetti P, Ehrlich ME, Czernik AJ, Fracasso RP, et al. Processing of Alzheimer beta/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation. Proc Nat Acad Sci USA 87: 6003-6 (1990).
    • (1990) Proc Nat Acad Sci USA , vol.87 , pp. 6003-6006
    • Buxbaum, J.D.1    Gandy, S.E.2    Cicchetti, P.3    Ehrlich, M.E.4    Czernik, A.J.5    Fracasso, R.P.6
  • 50
    • 0027332657 scopus 로고
    • Inhibition of beta-amyloid production by activation of protein kinase C
    • Gabuzda D, Busciglio J, Yankner BA. Inhibition of beta-amyloid production by activation of protein kinase C. J Neurochem 61: 2326-9 (1993).
    • (1993) J Neurochem , vol.61 , pp. 2326-2329
    • Gabuzda, D.1    Busciglio, J.2    Yankner, B.A.3
  • 51
    • 3242757474 scopus 로고    scopus 로고
    • Differential involvement of protein kinase C alpha and epsilon in the regulated secretion of soluble amyloid precursor protein
    • Lanni C, Mazzucchelli M, Porrello E, Govoni S, Racchi M. Differential involvement of protein kinase C alpha and epsilon in the regulated secretion of soluble amyloid precursor protein. Eur J Biochem 271: 3068-75 (2004).
    • (2004) Eur J Biochem , vol.271 , pp. 3068-3075
    • Lanni, C.1    Mazzucchelli, M.2    Porrello, E.3    Govoni, S.4    Racchi, M.5
  • 52
    • 33644532847 scopus 로고    scopus 로고
    • Expression cloning screen for modifiers of amyloid precursor protein shedding
    • Schobel S, Neumann S, Seed B, Lichtenthaler SF. Expression cloning screen for modifiers of amyloid precursor protein shedding. Int J Dev Neurosci 24: 141-8 (2006).
    • (2006) Int J Dev Neurosci , vol.24 , pp. 141-148
    • Schobel, S.1    Neumann, S.2    Seed, B.3    Lichtenthaler, S.F.4
  • 53
    • 0028965767 scopus 로고
    • Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an Nterminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts
    • Kinouchi T, Sorimachi H, Maruyama K, Mizuno K, Ohno S, Ishiura S, et al. Conventional protein kinase C (PKC)-alpha and novel PKC epsilon, but not -delta, increase the secretion of an Nterminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts. FEBS Lett 364: 203-6 (1995).
    • (1995) FEBS Lett , vol.364 , pp. 203-206
    • Kinouchi, T.1    Sorimachi, H.2    Maruyama, K.3    Mizuno, K.4    Ohno, S.5    Ishiura, S.6
  • 54
    • 0032498135 scopus 로고    scopus 로고
    • Specific role for protein kinase C alpha in the constitutive and regulated secretion of amyloid precursor protein in human skin fibroblasts
    • Benussi L, Govoni S, Gasparini L, Binetti G, Trabucchi M, Bianchetti A, et al. Specific role for protein kinase C alpha in the constitutive and regulated secretion of amyloid precursor protein in human skin fibroblasts. Neuroscience letters 240: 97-101 (1998).
    • (1998) Neuroscience Letters , vol.240 , pp. 97-101
    • Benussi, L.1    Govoni, S.2    Gasparini, L.3    Binetti, G.4    Trabucchi, M.5    Bianchetti, A.6
  • 55
    • 0031453010 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway
    • Mills J, Laurent Charest D, Lam F, Beyreuther K, Ida N, Pelech SL, et al. Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway. J Neurosci 17: 9415-22 (1997).
    • (1997) J Neurosci , vol.17 , pp. 9415-9422
    • Mills, J.1    Laurent, C.D.2    Lam, F.3    Beyreuther, K.4    Ida, N.5    Pelech, S.L.6
  • 56
    • 0031952526 scopus 로고    scopus 로고
    • Regulation of secretion of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade
    • Desdouits-Magnen J, Desdouits F, Takeda S, Syu LJ, Saltiel AR, Buxbaum JD, et al. Regulation of secretion of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade. J Neurochem 70: 524-30 (1998).
    • (1998) J Neurochem , vol.70 , pp. 524-530
    • Desdouits-Magnen, J.1    Desdouits, F.2    Takeda, S.3    Syu, L.J.4    Saltiel, A.R.5    Buxbaum, J.D.6
  • 57
    • 0031751761 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-dependent and protein kinase C-dependent pathways link the m1 muscarinic receptor to beta-amyloid precursor protein secretion
    • Haring R, Fisher A, Marciano D, Pittel Z, Kloog Y, Zuckerman A, et al. Mitogen-activated protein kinase-dependent and protein kinase C-dependent pathways link the m1 muscarinic receptor to beta-amyloid precursor protein secretion. J Neurochem 71: 2094-103 (1998).
    • (1998) J Neurochem , vol.71 , pp. 2094-2103
    • Haring, R.1    Fisher, A.2    Marciano, D.3    Pittel, Z.4    Kloog, Y.5    Zuckerman, A.6
  • 58
    • 44649149519 scopus 로고    scopus 로고
    • RNA interference silencing of DRAL affects processing of amyloid precursor protein
    • Tanahashi H, Yoshioka K. RNA interference silencing of DRAL affects processing of amyloid precursor protein. Neurosci Lett 439: 293-7 (2008).
    • (2008) Neurosci Lett , vol.439 , pp. 293-297
    • Tanahashi, H.1    Yoshioka, K.2
  • 59
    • 0037472674 scopus 로고    scopus 로고
    • New amide-bearing benzolactam-based protein kinase C modulators induce enhanced secretion of the amyloid precursor protein metabolite sAPPalpha
    • Kozikowski AP, Nowak I, Petukhov PA, Etcheberrigaray R, Mohamed A, Tan M, et al. New amide-bearing benzolactam-based protein kinase C modulators induce enhanced secretion of the amyloid precursor protein metabolite sAPPalpha. J Med Chem 46: 364-73 (2003).
    • (2003) J Med Chem , vol.46 , pp. 364-373
    • Kozikowski, A.P.1    Nowak, I.2    Petukhov, P.A.3    Etcheberrigaray, R.4    Mohamed, A.5    Tan, M.6
  • 61
    • 71749109421 scopus 로고    scopus 로고
    • Reduction of beta-amyloid levels by novel protein kinase C(epsilon) activators
    • Nelson TJ, Cui C, Luo Y, Alkon DL. Reduction of beta-amyloid levels by novel protein kinase C(epsilon) activators. J Biolo Chem 284: 34514-21 (2009).
    • (2009) J Biolo Chem , vol.284 , pp. 34514-34521
    • Nelson, T.J.1    Cui, C.2    Luo, Y.3    Alkon, D.L.4
  • 62
    • 0037097492 scopus 로고    scopus 로고
    • Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase C(alpha), src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C
    • Canet-Aviles RM, Anderton M, Hooper NM, Turner AJ, Vaughan PF. Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase C(alpha), src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C. Brain Res Mol Brain Res 102: 62-72 (2002).
    • (2002) Brain Res Mol Brain Res , vol.102 , pp. 62-72
    • Canet-Aviles, R.M.1    Anderton, M.2    Hooper, N.M.3    Turner, A.J.4    Vaughan, P.F.5
  • 63
    • 21244448835 scopus 로고    scopus 로고
    • Short-term interleukin-1(beta) increases the release of secreted APP(alpha) via MEK1/2-dependent and JNK-dependent alpha-secretase cleavage in neuroglioma U251 cells
    • Ma G, Chen S, Wang X, Ba M, Yang H, Lu G. Short-term interleukin-1(beta) increases the release of secreted APP(alpha) via MEK1/2-dependent and JNK-dependent alpha-secretase cleavage in neuroglioma U251 cells. J Neurosci Res 80: 683-92 (2005).
    • (2005) J Neurosci Res , vol.80 , pp. 683-692
    • Ma, G.1    Chen, S.2    Wang, X.3    Ba, M.4    Yang, H.5    Lu, G.6
  • 64
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intraneuronal beta-amyloid and requires mitogen-activated protein kinase signaling
    • Gasparini L, Gouras GK, Wang R, Gross RS, Beal MF, Greengard P, et al. Stimulation of beta-amyloid precursor protein trafficking by insulin reduces intraneuronal beta-amyloid and requires mitogen-activated protein kinase signaling. J Neurosci 21: 2561-70 (2001).
    • (2001) J Neurosci , vol.21 , pp. 2561-2570
    • Gasparini, L.1    Gouras, G.K.2    Wang, R.3    Gross, R.S.4    Beal, M.F.5    Greengard, P.6
  • 65
    • 0034012017 scopus 로고    scopus 로고
    • Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway
    • Solano DC, Sironi M, Bonfini C, Solerte SB, Govoni S, Racchi M. Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway. FASEB J 14: 1015-22 (2000).
    • (2000) FASEB J , vol.14 , pp. 1015-1022
    • Solano, D.C.1    Sironi, M.2    Bonfini, C.3    Solerte, S.B.4    Govoni, S.5    Racchi, M.6
  • 66
    • 0026750650 scopus 로고
    • Phosphorylation of Alzheimer amyloid precursor protein by protein kinase C
    • Suzuki T, Nairn AC, Gandy SE, Greengard P. Phosphorylation of Alzheimer amyloid precursor protein by protein kinase C. Neuroscience 48: 755-61 (1992).
    • (1992) Neuroscience , vol.48 , pp. 755-761
    • Suzuki, T.1    Nairn, A.C.2    Gandy, S.E.3    Greengard, P.4
  • 68
    • 0028057224 scopus 로고
    • Selective ectodomain phosphorylation and regulated cleavage of beta-amyloid precursor protein
    • Hung AY, Selkoe DJ. Selective ectodomain phosphorylation and regulated cleavage of beta-amyloid precursor protein. EMBO J 13: 534-42 (1994).
    • (1994) EMBO J , vol.13 , pp. 534-542
    • Hung, A.Y.1    Selkoe, D.J.2
  • 69
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme
    • Reddy P, Slack JL, Davis R, Cerretti DP, Kozlosky CJ, Blanton RA, et al. Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J Biol Chem 275: 14608-14 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 14608-14614
    • Reddy, P.1    Slack, J.L.2    Davis, R.3    Cerretti, D.P.4    Kozlosky, C.J.5    Blanton, R.A.6
  • 71
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation
    • Xu P, Derynck R. Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation. Mol Cell 37: 551-66 (2010).
    • (2010) Mol Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 72
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking
    • Soond SM, Everson B, Riches DW, Murphy G. ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking. J Cell Sci 118: 2371-80 (2005).
    • (2005) J Cell Sci , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 73
    • 0028859466 scopus 로고
    • Regulated formation of Golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein
    • Xu HX, Greengard P, Gandy S. Regulated formation of Golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein. J Biol Chem 270: 23243-5 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 23243-23245
    • Xu, H.X.1    Greengard, P.2    Gandy, S.3
  • 74
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A, König G, Bunke D, Fischer P, Salbaum JM, Masters CL, et al. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57: 115-26 (1989).
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    König, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6
  • 75
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with betasecretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky DM, Moore DB, Milla ME, Doms RW, Lee VM. Protein kinase C-dependent alpha-secretase competes with betasecretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J Biolo Chem 275: 2568-75. (2000).
    • (2000) J Biolo Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 76
    • 35748982195 scopus 로고    scopus 로고
    • Cutting proteins within lipid bilayers: Rhomboid structure and mechanism
    • Lemberg MK, Freeman M. Cutting proteins within lipid bilayers: rhomboid structure and mechanism. Mol Cell 28: 930-40 (2007).
    • (2007) Mol Cell , vol.28 , pp. 930-940
    • Lemberg, M.K.1    Freeman, M.2
  • 77
    • 63649164073 scopus 로고    scopus 로고
    • Trafficking, a key player in regulated intramembrane proteolysis
    • Sannerud R, Annaert W. Trafficking, a key player in regulated intramembrane proteolysis. Semin Cell Dev Biol 20: 183-90 (2009).
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 183-190
    • Sannerud, R.1    Annaert, W.2
  • 78
    • 0026721943 scopus 로고
    • Beta-amyloid precursor protein cleavage by a membrane-bound protease
    • Sisodia SS. Beta-amyloid precursor protein cleavage by a membrane-bound protease. Proc Natl Acad Sci USA 89: 6075-9 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 79
    • 0042733013 scopus 로고    scopus 로고
    • Rab5-stimulated up-regulation of the endocytic pathway increases intracellular beta-cleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production
    • Grbovic OM, Mathews PM, Jiang Y, Schmidt SD, Dinakar R, Summers-Terio NB, et al. Rab5-stimulated up-regulation of the endocytic pathway increases intracellular beta-cleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production. J Biol Chem 278: 31261-8 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 31261-31268
    • Grbovic, O.M.1    Mathews, P.M.2    Jiang, Y.3    Schmidt, S.D.4    Dinakar, R.5    Summers-Terio, N.B.6
  • 80
    • 11444267601 scopus 로고    scopus 로고
    • Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases
    • Nixon RA. Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases. Neurobiol aging 26: 373-82 (2005).
    • (2005) Neurobiol Aging , vol.26 , pp. 373-382
    • Nixon, R.A.1
  • 81
    • 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 Biological Chem 269: 17386-9 (1994).
    • (1994) J Biological Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 83
    • 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 160: 113-23 (2003).
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 84
    • 34547136377 scopus 로고    scopus 로고
    • Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein
    • Carey RM, Balcz BA, Lopez-Coviella I, Slack BE. Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein. BMC Cell Biol 6: 30 (2005).
    • (2005) BMC Cell Biol , vol.6 , pp. 30
    • Carey, R.M.1    Balcz, B.A.2    Lopez-Coviella, I.3    Slack, B.E.4
  • 85
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor mediated endocytosis demonstrates generation of amyloid beta -protein at the cell surface
    • Chyung JH, Selkoe DJ. Inhibition of receptor mediated endocytosis demonstrates generation of amyloid beta -protein at the cell surface. J Biol Chem 278: 51035-43 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 86
    • 47249093676 scopus 로고    scopus 로고
    • A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein
    • Schobel S, Neumann S, Hertweck M, Dislich B, Kuhn PH, Kremmer E, et al. A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein. J Biol Chem 283: 14257-14268 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 14257-14268
    • Schobel, S.1    Neumann, S.2    Hertweck, M.3    Dislich, B.4    Kuhn, P.H.5    Kremmer, E.6
  • 87
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, Wouters F, et al. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci 28: 2874-82 (2008).
    • (2008) J Neurosci , vol.28 , pp. 2874-2882
    • Schneider, A.1    Rajendran, L.2    Honsho, M.3    Gralle, M.4    Donnert, G.5    Wouters, F.6
  • 88
    • 45549102847 scopus 로고    scopus 로고
    • Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes
    • Lee J, Retamal C, Cuitino L, Caruano-Yzermans A, Shin JE, van Kerkhof P, et al. Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes. J Biol Chem 283: 11501-8 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 11501-11508
    • Lee, J.1    Retamal, C.2    Cuitino, L.3    Caruano-Yzermans, A.4    Shin, J.E.5    van Kerkhof, P.6
  • 89
    • 33646349010 scopus 로고    scopus 로고
    • Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein
    • Neumann S, Schobel S, Jager S, Trautwein A, Haass C, Pietrzik CU, et al. Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein. J Biol Chem 281: 7583-94 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 7583-7594
    • Neumann, S.1    Schobel, S.2    Jager, S.3    Trautwein, A.4    Haass, C.5    Pietrzik, C.U.6
  • 91
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • Trommsdorff M, Borg JP, Margolis B, Herz J. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J Biol Chem 273: 33556-60 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 92
    • 0035503797 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: Role of the intracellular adapter protein Fe65
    • Kinoshita A, Whelan CM, Smith CJ, Mikhailenko I, Rebeck GW, Strickland DK, et al. Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65. J Neurosci 21: 8354-61 (2001).
    • (2001) J Neurosci , vol.21 , pp. 8354-8361
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Mikhailenko, I.4    Rebeck, G.W.5    Strickland, D.K.6
  • 93
    • 0036846405 scopus 로고    scopus 로고
    • The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
    • Pietrzik CU, Busse T, Merriam DE, Weggen S, Koo EH. The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing. Embo J 21: 5691-700 (2002).
    • (2002) Embo J , vol.21 , pp. 5691-5700
    • Pietrzik, C.U.1    Busse, T.2    Merriam, D.E.3    Weggen, S.4    Koo, E.H.5
  • 94
    • 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 24: 4259-65 (2004).
    • (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
  • 95
    • 0034629292 scopus 로고    scopus 로고
    • Modulation of beta-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease
    • Ulery PG, Beers J, Mikhailenko I, Tanzi RE, Rebeck GW, Hyman BT, et al. Modulation of beta-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease. J Biol Chem 275: 7410-5 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 7410-7415
    • Ulery, P.G.1    Beers, J.2    Mikhailenko, I.3    Tanzi, R.E.4    Rebeck, G.W.5    Hyman, B.T.6
  • 96
    • 33750190414 scopus 로고    scopus 로고
    • Ectodomain shedding of the amyloid precursor protein: Cellular control mechanisms and novel modifiers
    • Lichtenthaler SF. Ectodomain shedding of the amyloid precursor protein: cellular control mechanisms and novel modifiers. Neurodegenerative diseases 3: 262-9 (2006).
    • (2006) Neurodegenerative Diseases , vol.3 , pp. 262-269
    • Lichtenthaler, S.F.1
  • 97
    • 56549111118 scopus 로고    scopus 로고
    • VPS10P-domain receptors - regulators of neuronal viability and function
    • Willnow TE, Petersen CM, Nykjaer A. VPS10P-domain receptors - regulators of neuronal viability and function. Nat Rev Neurosci 9: 899-909 (2008).
    • (2008) Nat Rev Neurosci , vol.9 , pp. 899-909
    • Willnow, T.E.1    Petersen, C.M.2    Nykjaer, A.3
  • 98
    • 33845767391 scopus 로고    scopus 로고
    • Novel modulators of amyloid-beta precursor protein processing
    • Tang BL, Liou YC. Novel modulators of amyloid-beta precursor protein processing. J Neurochem 100: 314-23 (2007).
    • (2007) J Neurochem , vol.100 , pp. 314-323
    • Tang, B.L.1    Liou, Y.C.2
  • 99
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science (NY 286: 735-41. (1999).
    • (1999) Science (NY , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6
  • 100
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass C, Lemere CA, Capell A, Citron M, Seubert P, Schenk D, et al. The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nature medicine 1: 1291-6 (1995).
    • (1995) Nature Medicine , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6
  • 101
    • 0027526419 scopus 로고
    • Release of excess amyloid b protein from a mutant amyloid b protein precursor
    • Cai XD, Golde TE, Younkin SG. Release of excess amyloid b protein from a mutant amyloid b protein precursor. Science (NY 259: 514-6 (1993).
    • (1993) Science (NY , vol.259 , pp. 514-516
    • Cai, X.D.1    Golde, T.E.2    Younkin, S.G.3
  • 102
    • 0026745610 scopus 로고
    • Mutation of the b-amyloid precursor protein in familial Alzheimer's disease increases b-protein production
    • Citron M, Oltersdorf T, Haass C, McConlogue L, Hung AY, Seubert P, et al. Mutation of the b-amyloid precursor protein in familial Alzheimer's disease increases b-protein production. Nature 360: 672-4 (1992).
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6
  • 103
    • 0028982840 scopus 로고
    • Decreased alpha-secretase-cleaved amyloid precursor protein as a diagnostic marker for Alzheimer's disease
    • Lannfelt L, Basun H, Wahlund LO, Rowe BA, Wagner SL. Decreased alpha-secretase-cleaved amyloid precursor protein as a diagnostic marker for Alzheimer's disease. Nature medicine 1: 829-32 (1995).
    • (1995) Nature Medicine , vol.1 , pp. 829-832
    • Lannfelt, L.1    Basun, H.2    Wahlund, L.O.3    Rowe, B.A.4    Wagner, S.L.5
  • 104
    • 33847171931 scopus 로고    scopus 로고
    • Synapse-associated protein-97 mediates alpha-secretase ADAM10 trafficking and promotes its activity
    • Marcello E, Gardoni F, Mauceri D, Romorini S, Jeromin A, Epis R, et al. Synapse-associated protein-97 mediates alpha-secretase ADAM10 trafficking and promotes its activity. J Neurosci 27: 1682-91 (2007).
    • (2007) J Neurosci , vol.27 , pp. 1682-1691
    • Marcello, E.1    Gardoni, F.2    Mauceri, D.3    Romorini, S.4    Jeromin, A.5    Epis, R.6
  • 105
    • 65549119787 scopus 로고    scopus 로고
    • Synaptic NMDA receptor activation stimulates alpha-secretase amyloid precursor protein processing and inhibits amyloid-beta production
    • Hoey SE, Williams RJ, Perkinton MS. Synaptic NMDA receptor activation stimulates alpha-secretase amyloid precursor protein processing and inhibits amyloid-beta production. J Neurosci 29: 4442-60 (2009).
    • (2009) J Neurosci , vol.29 , pp. 4442-4460
    • Hoey, S.E.1    Williams, R.J.2    Perkinton, M.S.3
  • 106
    • 26844574739 scopus 로고    scopus 로고
    • NMDA receptor activation inhibits alpha-secretase and promotes neuronal amyloid-beta production
    • Lesne S, Ali C, Gabriel C, Croci N, MacKenzie ET, Glabe CG, et al. NMDA receptor activation inhibits alpha-secretase and promotes neuronal amyloid-beta production. J Neurosci 25: 9367-77 (2005).
    • (2005) J Neurosci , vol.25 , pp. 9367-9377
    • Lesne, S.1    Ali, C.2    Gabriel, C.3    Croci, N.4    Mackenzie, E.T.5    Glabe, C.G.6
  • 108
    • 78049476184 scopus 로고    scopus 로고
    • Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer's disease
    • Epis R, Marcello E, Gardoni F, Vastagh C, Malinverno M, Balducci C, et al. Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer's disease. Brain 133: 3323-35 (2010).
    • (2010) Brain , vol.133 , pp. 3323-3335
    • Epis, R.1    Marcello, E.2    Gardoni, F.3    Vastagh, C.4    Malinverno, M.5    Balducci, C.6
  • 109
    • 77951223411 scopus 로고    scopus 로고
    • An arginine stretch limits ADAM10 exit from the endoplasmic reticulum
    • Marcello E, Gardoni F, Di Luca M, Perez-Otano I. An arginine stretch limits ADAM10 exit from the endoplasmic reticulum. J Biol Chem 285: 10376-84 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 10376-10384
    • Marcello, E.1    Gardoni, F.2    Di Luca, M.3    Perez-Otano, I.4
  • 110
    • 77951223411 scopus 로고    scopus 로고
    • An arginine stretch limits ADAM10 exit from the endoplasmic reticulum
    • Marcello E, Gardoni F, Di Luca M, Perez-Otano I. An arginine stretch limits ADAM10 exit from the endoplasmic reticulum. J Biol Chem 285: 10376-84 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 10376-10384
    • Marcello, E.1    Gardoni, F.2    Di Luca, M.3    Perez-Otano, I.4
  • 111
    • 34547893833 scopus 로고    scopus 로고
    • Enhancement of alpha-secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin
    • Hiraoka Y, Ohno M, Yoshida K, Okawa K, Tomimoto H, Kita T, et al. Enhancement of alpha-secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin. J Neurochem 102: 1595-605 (2007).
    • (2007) J Neurochem , vol.102 , pp. 1595-15605
    • Hiraoka, Y.1    Ohno, M.2    Yoshida, K.3    Okawa, K.4    Tomimoto, H.5    Kita, T.6
  • 112
  • 113
    • 70549109094 scopus 로고    scopus 로고
    • Nardilysin regulates axonal maturation and myelination in the central and peripheral nervous system
    • Ohno M, Hiraoka Y, Matsuoka T, Tomimoto H, Takao K, Miyakawa T, et al. Nardilysin regulates axonal maturation and myelination in the central and peripheral nervous system. Nat Neurosci 12: 1506-13 (2009).
    • (2009) Nat Neurosci , vol.12 , pp. 1506-1513
    • Ohno, M.1    Hiraoka, Y.2    Matsuoka, T.3    Tomimoto, H.4    Takao, K.5    Miyakawa, T.6
  • 114
    • 33750060301 scopus 로고    scopus 로고
    • Nardilysin enhances ectodomain shedding of heparin-binding epidermal growth factor-like growth factor through activation of tumor necrosis factor-alpha-converting enzyme
    • Nishi E, Hiraoka Y, Yoshida K, Okawa K, Kita T. Nardilysin enhances ectodomain shedding of heparin-binding epidermal growth factor-like growth factor through activation of tumor necrosis factor-alpha-converting enzyme. J Biol Chem 281: 31164-72 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 31164-31172
    • Nishi, E.1    Hiraoka, Y.2    Yoshida, K.3    Okawa, K.4    Kita, T.5
  • 115
    • 33745209915 scopus 로고    scopus 로고
    • ADAM10 activation is required for green tea (-)- epigallocatechin-3-gallate-induced alpha-secretase cleavage of amyloid precursor protein
    • Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, et al. ADAM10 activation is required for green tea (-)- epigallocatechin-3-gallate-induced alpha-secretase cleavage of amyloid precursor protein. J Biol Chem 281: 16419-27 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 16419-16427
    • Obregon, D.F.1    Rezai-Zadeh, K.2    Bai, Y.3    Sun, N.4    Hou, H.5    Ehrhart, J.6
  • 116
    • 25444500410 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice
    • Rezai-Zadeh K, Shytle D, Sun N, Mori T, Hou H, Jeanniton D, et al. Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J Neurosci 25: 8807-14 (2005).
    • (2005) J Neurosci , vol.25 , pp. 8807-8814
    • Rezai-Zadeh, K.1    Shytle, D.2    Sun, N.3    Mori, T.4    Hou, H.5    Jeanniton, D.6
  • 117
    • 77349109007 scopus 로고    scopus 로고
    • Nanolipidic particles improve the bioavailability and alphasecretase inducing ability of epigallocatechin-3-gallate (EGCG) for the treatment of Alzheimer's disease
    • Smith A, Giunta B, Bickford PC, Fountain M, Tan J, Shytle RD. Nanolipidic particles improve the bioavailability and alphasecretase inducing ability of epigallocatechin-3-gallate (EGCG) for the treatment of Alzheimer's disease. Int J Pharm 389: 207-12 (2010).
    • (2010) Int J Pharm , vol.389 , pp. 207-212
    • Smith, A.1    Giunta, B.2    Bickford, P.C.3    Fountain, M.4    Tan, J.5    Shytle, R.D.6
  • 118
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders A, Gilbert S, Garten W, Postina R, Fahrenholz F. Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J 15: 1837-9 (2001).
    • (2001) FASEB J , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 119
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation
    • Endres K, Anders A, Kojro E, Gilbert S, Fahrenholz F, Postina R. Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur J Biochem 270: 2386-93 (2003).
    • (2003) Eur J Biochem , vol.270 , pp. 2386-2393
    • Endres, K.1    Anders, A.2    Kojro, E.3    Gilbert, S.4    Fahrenholz, F.5    Postina, R.6
  • 120
    • 4544239545 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines
    • Zimmermann M, Gardoni F, Marcello E, Colciaghi F, Borroni B, Padovani A, et al. Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines. J Neurochem 90: 1489-99 (2004).
    • (2004) J Neurochem , vol.90 , pp. 1489-1499
    • Zimmermann, M.1    Gardoni, F.2    Marcello, E.3    Colciaghi, F.4    Borroni, B.5    Padovani, A.6
  • 121
    • 33845291088 scopus 로고    scopus 로고
    • Mitogen activated protein kinase and protein kinase C activation mediate promotion of sAPPalpha secretion by deprenyl
    • Yang HQ, Ba MW, Ren RJ, Zhang YH, Ma JF, Pan J, et al. Mitogen activated protein kinase and protein kinase C activation mediate promotion of sAPPalpha secretion by deprenyl. Neurochem Int 50: 74-82 (2007).
    • (2007) Neurochem Int , vol.50 , pp. 74-82
    • Yang, H.Q.1    Ba, M.W.2    Ren, R.J.3    Zhang, Y.H.4    Ma, J.F.5    Pan, J.6
  • 122
    • 65049087654 scopus 로고    scopus 로고
    • Involvement of protein trafficking in deprenyl-induced alpha-secretase activity regulation in PC12 cells
    • Yang HQ, Sun ZK, Ba MW, Xu J, Xing Y. Involvement of protein trafficking in deprenyl-induced alpha-secretase activity regulation in PC12 cells. Eur J Pharmacol 610: 37-41 (2009).
    • (2009) Eur J Pharmacol , vol.610 , pp. 37-41
    • Yang, H.Q.1    Sun, Z.K.2    Ba, M.W.3    Xu, J.4    Xing, Y.5
  • 123
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM10- dependent cleavage of amyloid precursor protein
    • Xu D, Sharma C, Hemler ME. Tetraspanin12 regulates ADAM10- dependent cleavage of amyloid precursor protein. FASEB J 23: 3674-81 (2009).
    • (2009) FASEB J , vol.23 , pp. 3674-3681
    • Xu, D.1    Sharma, C.2    Hemler, M.E.3
  • 124
    • 61349132079 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase (ADAM)- mediated ectodomain shedding of ADAM10
    • Parkin E, Harris B. A disintegrin and metalloproteinase (ADAM)- mediated ectodomain shedding of ADAM10. J Neurochem 108: 1464-79 (2009).
    • (2009) J Neurochem , vol.108 , pp. 1464-1479
    • Parkin, E.1    Harris, B.2
  • 125
    • 66449103810 scopus 로고    scopus 로고
    • ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase
    • Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Konietzko U, Reiss K, et al. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase. J Biol Chem 284: 11738-47 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Konietzko, U.5    Reiss, K.6
  • 126
    • 0037200076 scopus 로고    scopus 로고
    • Non-steroidal antiinflammatory drugs stimulate secretion of non-amyloidogenic precursor protein
    • Avramovich Y, Amit T, Youdim MB. Non-steroidal antiinflammatory drugs stimulate secretion of non-amyloidogenic precursor protein. J Biol Chem 277: 31466-73 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 31466-31473
    • Avramovich, Y.1    Amit, T.2    Youdim, M.B.3
  • 128
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10
    • 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 Nat Acad Sci USA 98: 5815-20 (2001).
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 129
    • 77954556606 scopus 로고    scopus 로고
    • Statins and the squalene synthase inhibitor zaragozic acid stimulate the non-amyloidogenic pathway of amyloid-beta protein precursor processing by suppression of cholesterol synthesis
    • Kojro E, Fuger P, Prinzen C, Kanarek AM, Rat D, Endres K, et al. Statins and the squalene synthase inhibitor zaragozic acid stimulate the non-amyloidogenic pathway of amyloid-beta protein precursor processing by suppression of cholesterol synthesis. J Alzheimers Dis 20: 1215-31 (2010).
    • (2010) J Alzheimers Dis , vol.20 , pp. 1215-1231
    • Kojro, E.1    Fuger, P.2    Prinzen, C.3    Kanarek, A.M.4    Rat, D.5    Endres, K.6
  • 132
    • 35148831212 scopus 로고    scopus 로고
    • The metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis
    • Hoe HS, Cooper MJ, Burns MP, Lewis PA, van der Brug M, Chakraborty G, et al. The metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis. J Neurosci 27: 10895-905 (2007).
    • (2007) J Neurosci , vol.27 , pp. 10895-10905
    • Hoe, H.S.1    Cooper, M.J.2    Burns, M.P.3    Lewis, P.A.4    van der Brug, M.5    Chakraborty, G.6
  • 133
    • 50349092478 scopus 로고    scopus 로고
    • Regulated proteolysis of APP and ApoE receptors
    • Hoe HS, Rebeck GW. Regulated proteolysis of APP and ApoE receptors. Mol Neurobiol 37: 64-72 (2008).
    • (2008) Mol Neurobiol , vol.37 , pp. 64-72
    • Hoe, H.S.1    Rebeck, G.W.2
  • 134
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • Furukawa K, Sopher BL, Rydel RE, Begley JG, Pham DG, Martin GM, et al. Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain. J Neurochem 67: 1882-96. (1996).
    • (1996) J Neurochem , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3    Begley, J.G.4    Pham, D.G.5    Martin, G.M.6
  • 135
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the betaamyloid precursor protein in normal and amnestic mice
    • Meziane H, Dodart JC, Mathis C, Little S, Clemens J, Paul SM, et al. Memory-enhancing effects of secreted forms of the betaamyloid precursor protein in normal and amnestic mice. Proc Nat Acad Sci USA 95: 12683-8 (1998).
    • (1998) Proc Nat Acad Sci USA , vol.95 , pp. 12683-12688
    • Meziane, H.1    Dodart, J.C.2    Mathis, C.3    Little, S.4    Clemens, J.5    Paul, S.M.6
  • 136
    • 4444255624 scopus 로고    scopus 로고
    • Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: Support for the amyloid hypothesis
    • Stein TD, Anders NJ, DeCarli C, Chan SL, Mattson MP, Johnson JA. Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis. J Neurosci 24: 7707-17 (2004).
    • (2004) J Neurosci , vol.24 , pp. 7707-7717
    • Stein, T.D.1    Anders, N.J.2    Decarli, C.3    Chan, S.L.4    Mattson, M.P.5    Johnson, J.A.6
  • 137
    • 34447640166 scopus 로고    scopus 로고
    • The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice
    • Ring S, Weyer SW, Kilian SB, Waldron E, Pietrzik CU, Filippov MA, et al. The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice. J Neurosci 27: 7817-26 (2007).
    • (2007) J Neurosci , vol.27 , pp. 7817-7826
    • Ring, S.1    Weyer, S.W.2    Kilian, S.B.3    Waldron, E.4    Pietrzik, C.U.5    Filippov, M.A.6
  • 138
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457: 981-9 (2009).
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 140
    • 0033987298 scopus 로고    scopus 로고
    • Levels of alpha- and beta-secretase cleaved amyloid precursor protein in the cerebrospinal fluid of Alzheimer's disease patients
    • Sennvik K, Fastbom J, Blomberg M, Wahlund LO, Winblad B, Benedikz E. Levels of alpha- and beta-secretase cleaved amyloid precursor protein in the cerebrospinal fluid of Alzheimer's disease patients. Neurosci Lett 278: 169-72 (2000).
    • (2000) Neurosci Lett , vol.278 , pp. 169-172
    • Sennvik, K.1    Fastbom, J.2    Blomberg, M.3    Wahlund, L.O.4    Winblad, B.5    Benedikz, E.6
  • 141
    • 0041886881 scopus 로고    scopus 로고
    • Measurement of alpha- and beta-secretase cleaved amyloid precursor protein in cerebrospinal fluid from Alzheimer patients
    • Olsson A, Hoglund K, Sjogren M, Andreasen N, Minthon L, Lannfelt L, et al. Measurement of alpha- and beta-secretase cleaved amyloid precursor protein in cerebrospinal fluid from Alzheimer patients. Exp Neurol 183: 74-80 (2003).
    • (2003) Exp Neurol , vol.183 , pp. 74-80
    • Olsson, A.1    Hoglund, K.2    Sjogren, M.3    Andreasen, N.4    Minthon, L.5    Lannfelt, L.6
  • 142
    • 0036042518 scopus 로고    scopus 로고
    • [alpha]-Secretase ADAM10 as well as [alpha]APPs is reduced in platelets and CSF of Alzheimer disease patients
    • Colciaghi F, Borroni B, Pastorino L, Marcello E, Zimmermann M, Cattabeni F, et al. [alpha]-Secretase ADAM10 as well as [alpha]APPs is reduced in platelets and CSF of Alzheimer disease patients. Mol Med 8: 67-74 (2002).
    • (2002) Mol Med , vol.8 , pp. 67-74
    • Colciaghi, F.1    Borroni, B.2    Pastorino, L.3    Marcello, E.4    Zimmermann, M.5    Cattabeni, F.6
  • 143
    • 70349569016 scopus 로고    scopus 로고
    • Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity
    • Kim M, Suh J, Romano D, Truong MH, Mullin K, Hooli B, et al. Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate {alpha}-secretase activity. Hum Mol Genet 18: 3987-96 (2009).
    • (2009) Hum Mol Genet , vol.18 , pp. 3987-3996
    • Kim, M.1    Suh, J.2    Romano, D.3    Truong, M.H.4    Mullin, K.5    Hooli, B.6
  • 148
    • 36249015501 scopus 로고    scopus 로고
    • Abeta(1-40)-induced secretion of matrix metalloproteinase-9 results in sAPPalpha release by association with cell surface APP
    • Talamagas AA, Efthimiopoulos S, Tsilibary EC, Figueiredo-Pereira ME, Tzinia AK. Abeta(1-40)-induced secretion of matrix metalloproteinase-9 results in sAPPalpha release by association with cell surface APP. Neurobiol Dis 28: 304-15 (2007).
    • (2007) Neurobiol Dis , vol.28 , pp. 304-315
    • Talamagas, A.A.1    Efthimiopoulos, S.2    Tsilibary, E.C.3    Figueiredo-Pereira, M.E.4    Tzinia, A.K.5
  • 149
    • 33646379384 scopus 로고    scopus 로고
    • Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases
    • Ahmad M, Takino T, Miyamori H, Yoshizaki T, Furukawa M, Sato H. Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases. J Biochem 139: 517-26 (2006).
    • (2006) J Biochem , vol.139 , pp. 517-526
    • Ahmad, M.1    Takino, T.2    Miyamori, H.3    Yoshizaki, T.4    Furukawa, M.5    Sato, H.6
  • 151
    • 0038052349 scopus 로고    scopus 로고
    • Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A
    • Higashi S, Miyazaki K. Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A. Biochemistry 42: 6514-26 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6514-6526
    • Higashi, S.1    Miyazaki, K.2
  • 152
    • 33344458827 scopus 로고    scopus 로고
    • M1 receptors play a central role in modulating ADlike pathology in transgenic mice
    • Caccamo A, Oddo S, Billings LM, Green KN, Martinez-Coria H, Fisher A, et al. M1 receptors play a central role in modulating ADlike pathology in transgenic mice. Neuron 49: 671-82 (2006).
    • (2006) Neuron , vol.49 , pp. 671-682
    • Caccamo, A.1    Oddo, S.2    Billings, L.M.3    Green, K.N.4    Martinez-Coria, H.5    Fisher, A.6
  • 153
    • 0033663907 scopus 로고    scopus 로고
    • The selective muscarinic M1 agonist AF102B decreases levels of total Abeta in cerebrospinal fluid of patients with Alzheimer's disease
    • Nitsch RM, Deng M, Tennis M, Schoenfeld D, Growdon JH. The selective muscarinic M1 agonist AF102B decreases levels of total Abeta in cerebrospinal fluid of patients with Alzheimer's disease. Ann Neurol 48: 913-8 (2000).
    • (2000) Ann Neurol , vol.48 , pp. 913-918
    • Nitsch, R.M.1    Deng, M.2    Tennis, M.3    Schoenfeld, D.4    Growdon, J.H.5
  • 154
    • 45249124737 scopus 로고    scopus 로고
    • Etazolate, a neuroprotective drug linking GABA(A) receptor pharmacology to amyloid precursor protein processing
    • Marcade M, Bourdin J, Loiseau N, Peillon H, Rayer A, Drouin D, et al. Etazolate, a neuroprotective drug linking GABA(A) receptor pharmacology to amyloid precursor protein processing. Journal of neurochemistry 106: 392-404 (2008).
    • (2008) Journal of Neurochemistry , vol.106 , pp. 392-404
    • Marcade, M.1    Bourdin, J.2    Loiseau, N.3    Peillon, H.4    Rayer, A.5    Drouin, D.6
  • 155
    • 0031898094 scopus 로고    scopus 로고
    • Vasopressin and bradykinin regulate secretory processing of the amyloid protein precursor of Alzheimer's disease
    • Nitsch RM, Kim C, Growdon JH. Vasopressin and bradykinin regulate secretory processing of the amyloid protein precursor of Alzheimer's disease. Neurochem Res 23: 807-14 (1998).
    • (1998) Neurochem Res , vol.23 , pp. 807-814
    • Nitsch, R.M.1    Kim, C.2    Growdon, J.H.3
  • 156
    • 0030723893 scopus 로고    scopus 로고
    • Rapid stimulation of amyloid precursor protein release by epidermal growth factor: Role of protein kinase C
    • Slack BE, Breu J, Muchnicki L, Wurtman RJ. Rapid stimulation of amyloid precursor protein release by epidermal growth factor: role of protein kinase C. The Biochemical journal 327: 245-9 (1997).
    • (1997) The Biochemical Journal , vol.327 , pp. 245-249
    • Slack, B.E.1    Breu, J.2    Muchnicki, L.3    Wurtman, R.J.4
  • 157
    • 0034818022 scopus 로고    scopus 로고
    • Estrogen induces a rapid secretion of amyloid beta precursor protein via the mitogenactivated protein kinase pathway
    • Manthey D, Heck S, Engert S, Behl C. Estrogen induces a rapid secretion of amyloid beta precursor protein via the mitogenactivated protein kinase pathway. Eur J Biochem 268: 4285-91 (2001).
    • (2001) Eur J Biochem , vol.268 , pp. 4285-4291
    • Manthey, D.1    Heck, S.2    Engert, S.3    Behl, C.4
  • 158
    • 13444282531 scopus 로고    scopus 로고
    • Estrogen stimulates release of secreted amyloid precursor protein from primary rat cortical neurons via protein kinase C pathway
    • Zhang S, Huang Y, Zhu YC, Yao T. Estrogen stimulates release of secreted amyloid precursor protein from primary rat cortical neurons via protein kinase C pathway. Acta Pharmacol Sin 26: 171-6 (2005).
    • (2005) Acta Pharmacol Sin , vol.26 , pp. 171-176
    • Zhang, S.1    Huang, Y.2    Zhu, Y.C.3    Yao, T.4
  • 159
    • 36749016710 scopus 로고    scopus 로고
    • Huperzine A regulates amyloid precursor protein processing via protein kinase C and mitogen-activated protein kinase pathways in neuroblastoma SK-N-SH cells over-expressing wild type human amyloid precursor protein 695
    • Peng Y, Lee DY, Jiang L, Ma Z, Schachter SC, Lemere CA. Huperzine A regulates amyloid precursor protein processing via protein kinase C and mitogen-activated protein kinase pathways in neuroblastoma SK-N-SH cells over-expressing wild type human amyloid precursor protein 695. Neuroscience 150: 386-95 (2007).
    • (2007) Neuroscience , vol.150 , pp. 386-395
    • Peng, Y.1    Lee, D.Y.2    Jiang, L.3    Ma, Z.4    Schachter, S.C.5    Lemere, C.A.6
  • 160
    • 0036813726 scopus 로고    scopus 로고
    • Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor
    • Ling X, Martins RN, Racchi M, Craft S, Helmerhorst E. Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor. J Alzheimers Dis 4: 369-74 (2002).
    • (2002) J Alzheimers Dis , vol.4 , pp. 369-374
    • Ling, X.1    Martins, R.N.2    Racchi, M.3    Craft, S.4    Helmerhorst, E.5
  • 161
    • 34249851328 scopus 로고    scopus 로고
    • IGF-1-induced processing of the amyloid precursor protein family is mediated by different signaling pathways
    • Adlerz L, Holback S, Multhaup G, Iverfeldt K. IGF-1-induced processing of the amyloid precursor protein family is mediated by different signaling pathways. The Journal of biological chemistry 282: 10203-9 (2007).
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 10203-10209
    • Adlerz, L.1    Holback, S.2    Multhaup, G.3    Iverfeldt, K.4
  • 162
    • 33745793612 scopus 로고    scopus 로고
    • Interleukin-1alpha stimulates nonamyloidogenic pathway by alpha-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase
    • Bandyopadhyay S, Hartley DM, Cahill CM, Lahiri DK, Chattopadhyay N, Rogers JT. Interleukin-1alpha stimulates nonamyloidogenic pathway by alpha-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase. J Neurosci Res 84: 106-18 (2006).
    • (2006) J Neurosci Res , vol.84 , pp. 106-118
    • Bandyopadhyay, S.1    Hartley, D.M.2    Cahill, C.M.3    Lahiri, D.K.4    Chattopadhyay, N.5    Rogers, J.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.