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Regulation of amyloid-β production by the prion protein

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Pages 217-222 | Received 26 Oct 2011, Accepted 08 Dec 2011, Published online: 01 Jul 2012

References

  • Burns A, Iliffe S. Alzheimer’s disease. BMJ 2009; 338:b158; http://dx.doi.org/10.1136/bmj.b158; PMID: 19196745
  • Mount C, Downton C. Alzheimer disease: progress or profit?. Nat Med 2006; 12:780 - 4; http://dx.doi.org/10.1038/nm0706-780; PMID: 16829947
  • Morrissette DA, Parachikova A, Green KN, LaFerla FM. Relevance of transgenic mouse models to human Alzheimer disease. J Biol Chem 2009; 284:6033 - 7; http://dx.doi.org/10.1074/jbc.R800030200; PMID: 18948253
  • Jorm AF, Korten AE, Henderson AS. The prevalence of dementia: a quantitative integration of the literature. Acta Psychiatr Scand 1987; 76:465 - 79; http://dx.doi.org/10.1111/j.1600-0447.1987.tb02906.x; PMID: 3324647
  • Vardy ER, Catto AJ, Hooper NM. Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer’s disease. Trends Mol Med 2005; 11:464 - 72; http://dx.doi.org/10.1016/j.molmed.2005.08.004; PMID: 16153892
  • Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta- and gamma-secretases. FEBS Lett 2000; 483:6 - 10; http://dx.doi.org/10.1016/S0014-5793(00)02076-7; PMID: 11033346
  • Pimplikar SW. Reassessing the amyloid cascade hypothesis of Alzheimer’s disease. Int J Biochem Cell Biol 2009; 41:1261 - 8; http://dx.doi.org/10.1016/j.biocel.2008.12.015; PMID: 19124085
  • Fukumoto H, Cheung BS, Hyman BT, Irizarry MC. Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch Neurol 2002; 59:1381 - 9; http://dx.doi.org/10.1001/archneur.59.9.1381; PMID: 12223024
  • Li R, Lindholm K, Yang LB, Yue X, Citron M, Yan R, et al. Amyloid beta peptide load is correlated with increased beta-secretase activity in sporadic Alzheimer’s disease patients. Proc Natl Acad Sci U S A 2004; 101:3632 - 7; http://dx.doi.org/10.1073/pnas.0205689101; PMID: 14978286
  • Aguzzi A, Sigurdson C, Heikenwaelder M. Molecular mechanisms of prion pathogenesis. Annu Rev Pathol 2008; 3:11 - 40; http://dx.doi.org/10.1146/annurev.pathmechdis.3.121806.154326; PMID: 18233951
  • Hainfellner JA, Wanschitz J, Jellinger K, Liberski PP, Gullotta F, Budka H. Coexistence of Alzheimer-type neuropathology in Creutzfeldt-Jakob disease. Acta Neuropathol 1998; 96:116 - 22; http://dx.doi.org/10.1007/s004010050870; PMID: 9705125
  • Voigtländer T, Klöppel S, Birner P, Jarius C, Flicker H, Verghese-Nikolakaki S, et al. Marked increase of neuronal prion protein immunoreactivity in Alzheimer’s disease and human prion diseases. Acta Neuropathol 2001; 101:417 - 23; PMID: 11484812
  • Del Bo R, Scarlato M, Ghezzi S, Martinelli-Boneschi F, Fenoglio C, Galimberti G, et al. Is M129V of PRNP gene associated with Alzheimer’s disease? A case-control study and a meta-analysis. Neurobiol Aging 2006; 27:770 - , e1-770, e5; http://dx.doi.org/10.1016/j.neurobiolaging.2005.05.025; PMID: 16099550
  • Bertram L, McQueen MB, Mullin K, Blacker D, Tanzi RE. Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Genet 2007; 39:17 - 23; http://dx.doi.org/10.1038/ng1934; PMID: 17192785
  • Dermaut B, Croes EA, Rademakers R, Van den Broeck M, Cruts M, Hofman A, et al. PRNP Val129 homozygosity increases risk for early-onset Alzheimer’s disease. Ann Neurol 2003; 53:409 - 12; http://dx.doi.org/10.1002/ana.10507; PMID: 12601712
  • Riemenschneider M, Klopp N, Xiang W, Wagenpfeil S, Vollmert C, Müller U, et al. Prion protein codon 129 polymorphism and risk of Alzheimer disease. Neurology 2004; 63:364 - 6; PMID: 15277640
  • Parkin ET, Watt NT, Hussain I, Eckman EA, Eckman CB, Manson JC, et al. Cellular prion protein regulates beta-secretase cleavage of the Alzheimer’s amyloid precursor protein. Proc Natl Acad Sci U S A 2007; 104:11062 - 7; http://dx.doi.org/10.1073/pnas.0609621104; PMID: 17573534
  • Hooper NM, Turner AJ. A new take on prions: preventing Alzheimer’s disease. Trends Biochem Sci 2008; 33:151 - 5; http://dx.doi.org/10.1016/j.tibs.2008.01.004; PMID: 18343669
  • Andersen OM, Reiche J, Schmidt V, Gotthardt M, Spoelgen R, Behlke J, et al. Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein. Proc Natl Acad Sci U S A 2005; 102:13461 - 6; http://dx.doi.org/10.1073/pnas.0503689102; PMID: 16174740
  • Spoelgen R, von Arnim CA, Thomas AV, Peltan ID, Koker M, Deng A, et al. Interaction of the cytosolic domains of sorLA/LR11 with the amyloid precursor protein (APP) and beta-secretase beta-site APP-cleaving enzyme. J Neurosci 2006; 26:418 - 28; http://dx.doi.org/10.1523/JNEUROSCI.3882-05.2006; PMID: 16407538
  • Sannerud R, Declerck I, Peric A, Raemaekers T, Menendez G, Zhou L, et al. ADP ribosylation factor 6 (ARF6) controls amyloid precursor protein (APP) processing by mediating the endosomal sorting of BACE1. Proc Natl Acad Sci U S A 2011; 108:E559 - 68; http://dx.doi.org/10.1073/pnas.1100745108; PMID: 21825135
  • He X, Li F, Chang WP, Tang J. GGA proteins mediate the recycling pathway of memapsin 2 (BACE). J Biol Chem 2005; 280:11696 - 703; http://dx.doi.org/10.1074/jbc.M411296200; PMID: 15615712
  • Wahle T, Thal DR, Sastre M, Rentmeister A, Bogdanovic N, Famulok M, et al. GGA1 is expressed in the human brain and affects the generation of amyloid beta-peptide. J Neurosci 2006; 26:12838 - 46; http://dx.doi.org/10.1523/JNEUROSCI.1982-06.2006; PMID: 17151287
  • Griffiths HH, Whitehouse IJ, Baybutt H, Brown D, Kellett KA, Jackson CD, et al. Prion protein interacts with BACE1 protein and differentially regulates its activity toward wild type and Swedish mutant amyloid precursor protein. J Biol Chem 2011; 286:33489 - 500; http://dx.doi.org/10.1074/jbc.M111.278556; PMID: 21795680
  • 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. Nat Med 1995; 1:1291 - 6; http://dx.doi.org/10.1038/nm1295-1291; PMID: 7489411
  • Koo EH, Squazzo SL. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem 1994; 269:17386 - 9; PMID: 8021238
  • Benjannet S, Elagoz A, Wickham L, Mamarbachi M, Munzer JS, Basak A, et al. Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production. J Biol Chem 2001; 276:10879 - 87; http://dx.doi.org/10.1074/jbc.M009899200; PMID: 11152688
  • Creemers JW, Ines Dominguez D, Plets E, Serneels L, Taylor NA, Multhaup G, et al. Processing of beta-secretase by furin and other members of the proprotein convertase family. J Biol Chem 2001; 276:4211 - 7; http://dx.doi.org/10.1074/jbc.M006947200; PMID: 11071887
  • Capell A, Steiner H, Willem M, Kaiser H, Meyer C, Walter J, et al. Maturation and pro-peptide cleavage of beta-secretase. J Biol Chem 2000; 275:30849 - 54; http://dx.doi.org/10.1074/jbc.M003202200; PMID: 10801872
  • Huse JT, Pijak DS, Leslie GJ, Lee VM, Doms RW. Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer’s disease beta-secretase. J Biol Chem 2000; 275:33729 - 37; http://dx.doi.org/10.1074/jbc.M004175200; PMID: 10924510
  • Hébert SS, Bourdages V, Godin C, Ferland M, Carreau M, Lévesque G. Presenilin-1 interacts directly with the beta-site amyloid protein precursor cleaving enzyme (BACE1). Neurobiol Dis 2003; 13:238 - 45; http://dx.doi.org/10.1016/S0969-9961(03)00035-4; PMID: 12901838
  • Scherzer CR, Offe K, Gearing M, Rees HD, Fang G, Heilman CJ, et al. Loss of apolipoprotein E receptor LR11 in Alzheimer disease. Arch Neurol 2004; 61:1200 - 5; http://dx.doi.org/10.1001/archneur.61.8.1200; PMID: 15313836
  • Eggert S, Paliga K, Soba P, Evin G, Masters CL, Weidemann A, et al. The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. J Biol Chem 2004; 279:18146 - 56; http://dx.doi.org/10.1074/jbc.M311601200; PMID: 14970212
  • Li Q, Südhof TC. Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1. J Biol Chem 2004; 279:10542 - 50; http://dx.doi.org/10.1074/jbc.M310001200; PMID: 14699153
  • Kitazume S, Tachida Y, Oka R, Shirotani K, Saido TC, Hashimoto Y. Alzheimer’s beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc Natl Acad Sci USA 2001; 98:13554 - 9; http://dx.doi.org/10.1073/pnas.241509198; PMID: 11698669
  • von Arnim CA, Kinoshita A, Peltan ID, Tangredi MM, Herl L, Lee BM, et al. The low density lipoprotein receptor-related protein (LRP) is a novel beta-secretase (BACE1) substrate. J Biol Chem 2005; 280:17777 - 85; http://dx.doi.org/10.1074/jbc.M414248200; PMID: 15749709
  • Griffiths HH, Morten IJ, Hooper NM. Emerging and potential therapies for Alzheimer’s disease. Expert Opin Ther Targets 2008; 12:693 - 704; http://dx.doi.org/10.1517/14728222.12.6.693; PMID: 18479216
  • 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 2004; 113:1456 - 64; PMID: 15146243
  • Altmeppen HC, Prox J, Puig B, Kluth MA, Bernreuther C, Thurm D, et al. Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo. Mol Neurodegener 2011; 6:36; http://dx.doi.org/10.1186/1750-1326-6-36; PMID: 21619641
  • 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 2010; 30:4833 - 44; http://dx.doi.org/10.1523/JNEUROSCI.5221-09.2010; PMID: 20371803
  • 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 2009; 284:22590 - 600; http://dx.doi.org/10.1074/jbc.M109.032599; PMID: 19564338
  • Cissé MA, Sunyach C, Lefranc-Jullien S, Postina R, Vincent B, Checler F. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J Biol Chem 2005; 280:40624 - 31; http://dx.doi.org/10.1074/jbc.M506069200; PMID: 16236709
  • Vincent B, Paitel E, Frobert Y, Lehmann S, Grassi J, Checler F. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J Biol Chem 2000; 275:35612 - 6; http://dx.doi.org/10.1074/jbc.M004628200; PMID: 10952979
  • Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 2001; 276:37743 - 6; PMID: 11477090
  • Mucke L, Masliah E, Yu GQ, Mallory M, Rockenstein EM, Tatsuno G, et al. High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci 2000; 20:4050 - 8; PMID: 10818140
  • Calella AM, Farinelli M, Nuvolone M, Mirante O, Moos R, Falsig J, et al. Prion protein and Abeta-related synaptic toxicity impairment. EMBO Mol Med 2010; 2:306 - 14; http://dx.doi.org/10.1002/emmm.201000082; PMID: 20665634
  • Gimbel DA, Nygaard HB, Coffey EE, Gunther EC, Laurén J, Gimbel ZA, et al. Memory impairment in transgenic Alzheimer mice requires cellular prion protein. J Neurosci 2010; 30:6367 - 74; http://dx.doi.org/10.1523/JNEUROSCI.0395-10.2010; PMID: 20445063
  • Schwarze-Eicker K, Keyvani K, Görtz N, Westaway D, Sachser N, Paulus W. Prion protein (PrPc) promotes beta-amyloid plaque formation. Neurobiol Aging 2005; 26:1177 - 82; http://dx.doi.org/10.1016/j.neurobiolaging.2004.10.004; PMID: 15917101
  • Cissé M, Sanchez PE, Kim DH, Ho K, Yu GQ, Mucke L. Ablation of cellular prion protein does not ameliorate abnormal neural network activity or cognitive dysfunction in the J20 line of human amyloid precursor protein transgenic mice. J Neurosci 2011; 31:10427 - 31; http://dx.doi.org/10.1523/JNEUROSCI.1459-11.2011; PMID: 21775587
  • Thinakaran G, Teplow DB, Siman R, Greenberg B, Sisodia SS. Metabolism of the “Swedish” amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the “beta-secretase” site occurs in the golgi apparatus. J Biol Chem 1996; 271:9390 - 7; PMID: 8621605
  • 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 1999; 286:735 - 41; http://dx.doi.org/10.1126/science.286.5440.735; PMID: 10531052
  • Yan R, Han P, Miao H, Greengard P, Xu H. The transmembrane domain of the Alzheimer’s beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate. J Biol Chem 2001; 276:36788 - 96; http://dx.doi.org/10.1074/jbc.M104350200; PMID: 11466313
  • Duyckaerts C, Potier MC, Delatour B. Alzheimer disease models and human neuropathology: similarities and differences. Acta Neuropathol 2008; 115:5 - 38; http://dx.doi.org/10.1007/s00401-007-0312-8; PMID: 18038275
  • Kokjohn TA, Roher AE. Amyloid precursor protein transgenic mouse models and Alzheimer’s disease: understanding the paradigms, limitations, and contributions. Alzheimers Dement 2009; 5:340 - 7; http://dx.doi.org/10.1016/j.jalz.2009.03.002; PMID: 19560104
  • Schieb H, Kratzin H, Jahn O, Möbius W, Rabe S, Staufenbiel M, et al. Beta-amyloid peptide variants in brains and cerebrospinal fluid from amyloid precursor protein (APP) transgenic mice: comparison with human Alzheimer amyloid. J Biol Chem 2011; 286:33747 - 58; http://dx.doi.org/10.1074/jbc.M111.246561; PMID: 21795681
  • Rezaie P, Pontikis CC, Hudson L, Cairns NJ, Lantos PL. Expression of cellular prion protein in the frontal and occipital lobe in Alzheimer’s disease, diffuse Lewy body disease, and in normal brain: an immunohistochemical study. J Histochem Cytochem 2005; 53:929 - 40; http://dx.doi.org/10.1369/jhc.4A6551.2005; PMID: 16055747
  • Meyne F, Gloeckner SF, Ciesielczyk B, Heinemann U, Krasnianski A, Meissner B, et al. Total prion protein levels in the cerebrospinal fluid are reduced in patients with various neurological disorders. J Alzheimers Dis 2009; 17:863 - 73; PMID: 19542614
  • Velayos JL, Irujo A, Cuadrado-Tejedor M, Paternain B, Moleres FJ, Ferrer V. The cellular prion protein and its role in Alzheimer disease. Prion 2009; 3:110 - 7; http://dx.doi.org/10.4161/pri.3.2.9135; PMID: 19556894
  • Whitehouse IJ, Jackson C, Turner AJ, Hooper NM. Prion protein is reduced in aging and in sporadic but not in familial Alzheimer’s disease. J Alzheimers Dis 2010; 22:1023 - 31; PMID: 20930299
  • Saijo E, Scheff SW, Telling GC. Unaltered prion protein expression in Alzheimer disease patients. Prion 2011; 5:109 - 16; http://dx.doi.org/10.4161/pri.5.2.16355; PMID: 21654203
  • Fukumoto H, Rosene DL, Moss MB, Raju S, Hyman BT, Irizarry MC. Beta-secretase activity increases with aging in human, monkey, and mouse brain. Am J Pathol 2004; 164:719 - 25; http://dx.doi.org/10.1016/S0002-9440(10)63159-8; PMID: 14742275
  • Vassallo N, Herms J. Cellular prion protein function in copper homeostasis and redox signalling at the synapse. J Neurochem 2003; 86:538 - 44; http://dx.doi.org/10.1046/j.1471-4159.2003.01882.x; PMID: 12859667
  • Guillot-Sestier MV, Sunyach C, Druon C, Scarzello S, Checler F. The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J Biol Chem 2009; 284:35973 - 86; http://dx.doi.org/10.1074/jbc.M109.051086; PMID: 19850936
  • Halliwell B. Oxidative stress and neurodegeneration: where are we now?. J Neurochem 2006; 97:1634 - 58; http://dx.doi.org/10.1111/j.1471-4159.2006.03907.x; PMID: 16805774
  • Lee HG, Perry G, Moreira PI, Garrett MR, Liu Q, Zhu X, et al. Tau phosphorylation in Alzheimer’s disease: pathogen or protector?. Trends Mol Med 2005; 11:164 - 9; http://dx.doi.org/10.1016/j.molmed.2005.02.008; PMID: 15823754
  • Zhu X, Su B, Wang X, Smith MA, Perry G. Causes of oxidative stress in Alzheimer disease. Cell Mol Life Sci 2007; 64:2202 - 10; http://dx.doi.org/10.1007/s00018-007-7218-4; PMID: 17605000
  • Chung E, Ji Y, Sun Y, Kascsak RJ, Kascsak RB, Mehta PD, et al. Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an Alzheimer’s disease model mouse. BMC Neurosci 2010; 11:130; http://dx.doi.org/10.1186/1471-2202-11-130; PMID: 20946660
  • Freir DB, Nicoll AJ, Klyubin I, Panico S, Mc Donald JM, Risse E, et al. Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites. Nat Commun 2011; 2:336; http://dx.doi.org/10.1038/ncomms1341; PMID: 21654636
  • Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009; 457:1128 - 32; http://dx.doi.org/10.1038/nature07761; PMID: 19242475
  • Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, et al. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 2006; 440:352 - 7; http://dx.doi.org/10.1038/nature04533; PMID: 16541076
  • Roychaudhuri R, Yang M, Hoshi MM, Teplow DB. Amyloid beta-protein assembly and Alzheimer disease. J Biol Chem 2009; 284:4749 - 53; http://dx.doi.org/10.1074/jbc.R800036200; PMID: 18845536
  • Forloni G, Balducci C. β-amyloid oligomers and prion protein: Fatal attraction?. Prion 2011; 5:10 - 5; http://dx.doi.org/10.4161/pri.5.1.14367; PMID: 21150333
  • Kessels HW, Nguyen LN, Nabavi S, Malinow R. The prion protein as a receptor for amyloid-beta. Nature 2010; 466:E3 - 4, discussion E4-5; http://dx.doi.org/10.1038/nature09217; PMID: 20703260
  • Alier K, Ma L, Yang J, Westaway D, Jhamandas JH. Aβ inhibition of ionic conductance in mouse basal forebrain neurons is dependent upon the cellular prion protein PrPC. J Neurosci 2011; 31:16292 - 7; http://dx.doi.org/10.1523/JNEUROSCI.4367-11.2011; PMID: 22072680

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