Impact of methionine oxidation as an initial event on the pathway of human prion protein conversion

References

• Weissmann C. The Ninth Datta Lecture. Molecular biology of transmissible spongiform encephalopathies. FEBS Lett 1996; 389:3 - 11; http://dx.doi.org/10.1016/0014-5793(96)00610-2; PMID: 8682199
   PubMed Web of Science ®Google Scholar
• Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A 2000; 97:145 - 50; http://dx.doi.org/10.1073/pnas.97.1.145; PMID: 10618385
   PubMed Web of Science ®Google Scholar
• Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci U S A 1993; 90:10962 - 6; PMID: 7902575
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; PMID: 6801762
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Molecular biology of prion diseases. Science 1991; 252:1515 - 22; http://dx.doi.org/10.1126/science.1675487; PMID: 1675487
   PubMed Web of Science ®Google Scholar
• Weissmann C, Aguzzi A. Bovine spongiform encephalopathy and early onset variant Creutzfeldt-Jakob disease. Curr Opin Neurobiol 1997; 7:695 - 700; http://dx.doi.org/10.1016/S0959-4388(97)80091-8; PMID: 9384548
   PubMed Web of Science ®Google Scholar
• Milhavet O, Lehmann S. Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res Brain Res Rev 2002; 38:328 - 39; http://dx.doi.org/10.1016/S0165-0173(01)00150-3; PMID: 11890980
   PubMed Web of Science ®Google Scholar
• Brown DR. Neurodegeneration and oxidative stress: prion disease results from loss of antioxidant defence. Folia Neuropathol 2005; 43:229 - 43; PMID: 16416388
   PubMed Web of Science ®Google Scholar
• Stadtman ER. Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 2001; 928:22 - 38; http://dx.doi.org/10.1111/j.1749-6632.2001.tb05632.x; PMID: 11795513
   PubMed Web of Science ®Google Scholar
• Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci U S A 2001; 98:12920 - 5; PMID: 11606777
   PubMed Web of Science ®Google Scholar
• Cui ZJ, Han ZQ, Li ZY. Modulating protein activity and cellular function by methionine residue oxidation. Amino Acids 2012; 43:505 - 17; PMID: 22146868
   PubMed Web of Science ®Google Scholar
• Nadal RC, Abdelraheim SR, Brazier MW, Rigby SE, Brown DR, Viles JH. Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals. Free Radic Biol Med 2007; 42:79 - 89; http://dx.doi.org/10.1016/j.freeradbiomed.2006.09.019; PMID: 17157195
   PubMed Web of Science ®Google Scholar
• Canello T, Engelstein R, Moshel O, Xanthopoulos K, Juanes ME, Langeveld J, Sklaviadis T, Gasset M, Gabizon R. Methionine sulfoxides on PrPSc: a prion-specific covalent signature. Biochemistry 2008; 47:8866 - 73; http://dx.doi.org/10.1021/bi800801f; PMID: 18680312
   PubMed Web of Science ®Google Scholar
• Silva CJ, Onisko BC, Dynin I, Erickson ML, Vensel WH, Requena JR, Antaki EM, Carter JM. Assessing the role of oxidized methionine at position 213 in the formation of prions in hamsters. Biochemistry 2010; 49:1854 - 61; http://dx.doi.org/10.1021/bi901850n; PMID: 20121218
   PubMed Web of Science ®Google Scholar
• Colombo G, Meli M, Morra G, Gabizon R, Gasset M. Methionine sulfoxides on prion protein Helix-3 switch on the α-fold destabilization required for conversion. PLoS One 2009; 4:e4296; http://dx.doi.org/10.1371/journal.pone.0004296; PMID: 19172188
   PubMed Web of Science ®Google Scholar
• DeMarco ML, Daggett V. Local environmental effects on the structure of the prion protein. C R Biol 2005; 328:847 - 62; http://dx.doi.org/10.1016/j.crvi.2005.05.001; PMID: 16286076
   PubMed Web of Science ®Google Scholar
• Lisa S, Meli M, Cabello G, Gabizon R, Colombo G, Gasset M. The structural intolerance of the PrP α-fold for polar substitution of the helix-3 methionines. Cell Mol Life Sci 2010; 67:2825 - 38; http://dx.doi.org/10.1007/s00018-010-0363-1; PMID: 20454997
   PubMed Web of Science ®Google Scholar
• Wolschner C, Giese A, Kretzschmar HA, Huber R, Moroder L, Budisa N. Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proc Natl Acad Sci U S A 2009; 106:7756 - 61; http://dx.doi.org/10.1073/pnas.0902688106; PMID: 19416900
   PubMed Web of Science ®Google Scholar
• Younan ND, Nadal RC, Davies P, Brown DR, Viles JH. Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway. J Biol Chem 2012; 287:28263 - 75; PMID: 22654104
   PubMed Web of Science ®Google Scholar
• Hart T, Hosszu LL, Trevitt CR, Jackson GS, Waltho JP, Collinge J, Clarke AR. Folding kinetics of the human prion protein probed by temperature jump. Proc Natl Acad Sci U S A 2009; 106:5651 - 6; http://dx.doi.org/10.1073/pnas.0811457106; PMID: 19321423
   PubMed Web of Science ®Google Scholar
• Redecke L, von Bergen M, Clos J, Konarev PV, Svergun DI, Fittschen UE, Broekaert JA, Bruns O, Georgieva D, Mandelkow E, et al. Structural characterization of β-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro.. J Struct Biol 2007; 157:308 - 20; PMID: 17023178
   PubMed Web of Science ®Google Scholar
• Requena JR, Dimitrova MN, Legname G, Teijeira S, Prusiner SB, Levine RL. Oxidation of methionine residues in the prion protein by hydrogen peroxide. Arch Biochem Biophys 2004; 432:188 - 95; http://dx.doi.org/10.1016/j.abb.2004.09.012; PMID: 15542057
   PubMed Web of Science ®Google Scholar
• Wong BS, Wang H, Brown DR, Jones IM. Selective oxidation of methionine residues in prion proteins. Biochem Biophys Res Commun 1999; 259:352 - 5; PMID: 10362513
   PubMed Web of Science ®Google Scholar
• Abdelraheim SR, Královicová S, Brown DR. Hydrogen peroxide cleavage of the prion protein generates a fragment able to initiate polymerisation of full length prion protein. Int J Biochem Cell Biol 2006; 38:1429 - 40; http://dx.doi.org/10.1016/j.biocel.2006.02.007; PMID: 16595185
   PubMed Web of Science ®Google Scholar
• Nyström S, Mishra R, Hornemann S, Aguzzi A, Nilsson KPR, Hammarström P. Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway. J Biol Chem 2012; 287:25975 - 84; http://dx.doi.org/10.1074/jbc.M112.372136; PMID: 22669942
   PubMed Web of Science ®Google Scholar
• Windl O, Dempster M, Estibeiro JP, Lathe R, de Silva R, Esmonde T, Will R, Springbett A, Campbell TA, Sidle KC, et al. Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene. Hum Genet 1996; 98:259 - 64; http://dx.doi.org/10.1007/s004390050204; PMID: 8707291
   PubMed Web of Science ®Google Scholar
• Redecke L, Binder S, Elmallah MIY, Broadbent R, Tilkorn C, Schulz B, May P, Goos A, Eich A, Rübhausen M, et al. UV-light-induced conversion and aggregation of prion proteins. Free Radic Biol Med 2009; 46:1353 - 61; http://dx.doi.org/10.1016/j.freeradbiomed.2009.02.013; PMID: 19249347
   PubMed Web of Science ®Google Scholar
• Rezaei H, Eghiaian F, Perez J, Doublet B, Choiset Y, Haertle T, Grosclaude J. Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J Mol Biol 2005; 347:665 - 79; http://dx.doi.org/10.1016/j.jmb.2005.01.043; PMID: 15755458
   PubMed Web of Science ®Google Scholar
• Jeganathan S, Hascher A, Chinnathambi S, Biernat J, Mandelkow EM, Mandelkow E. Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation. J Biol Chem 2008; 283:32066 - 76; PMID: 18725412
   PubMed Web of Science ®Google Scholar
• Nyström S, Mishra R, Hornemann S, Aguzzi A, Nilsson KPR, Hammarström P. Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway. J Biol Chem 2012; 287:25975 - 84; PMID: 22669942
   PubMed Web of Science ®Google Scholar
• Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim PE, Groth DF, Glenner GG. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983; 35:349 - 58; PMID: 6418385
   PubMed Web of Science ®Google Scholar
• Rehders D, Claasen B, Redecke L, Buschke A, Reibe C, Jehmlich N, von Bergen M, Betzel C, Meyer B. Peptide NMHRYPNQ of the cellular prion protein (PrP(C)) inhibits aggregation and is a potential key for understanding prion-prion interactions. J Mol Biol 2009; 392:198 - 207; http://dx.doi.org/10.1016/j.jmb.2009.07.014; PMID: 19607841
   PubMed Web of Science ®Google Scholar
• Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003; 26:267 - 98; http://dx.doi.org/10.1146/annurev.neuro.26.010302.081142; PMID: 12704221
   PubMed Web of Science ®Google Scholar
• Simoneau S, Rezaei H, Salès N, Kaiser-Schulz G, Lefebvre-Roque M, Vidal C, Fournier JG, Comte J, Wopfner F, Grosclaude J, et al. In vitro and in vivo neurotoxicity of prion protein oligomers. PLoS Pathog 2007; 3:e125; http://dx.doi.org/10.1371/journal.ppat.0030125; PMID: 17784787
   PubMed Web of Science ®Google Scholar
• Walsh DM, Selkoe DJ. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 2004; 11:213 - 28; http://dx.doi.org/10.2174/0929866043407174; PMID: 15182223
   PubMed Web of Science ®Google Scholar
• Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300:486 - 9; http://dx.doi.org/10.1126/science.1079469; PMID: 12702875
   PubMed Web of Science ®Google Scholar
• Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416:535 - 9; http://dx.doi.org/10.1038/416535a; PMID: 11932745
   PubMed Web of Science ®Google Scholar
• Winner B, Jappelli R, Maji SK, Desplats PA, Boyer L, Aigner S, Hetzer C, Loher T, Vilar M, Campioni S, et al. In vivo demonstration that alpha-synuclein oligomers are toxic. Proc Natl Acad Sci U S A 2011; 108:4194 - 9; http://dx.doi.org/10.1073/pnas.1100976108; PMID: 21325059
   PubMed Web of Science ®Google Scholar
• Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, Caughey B. The most infectious prion protein particles. Nature 2005; 437:257 - 61; http://dx.doi.org/10.1038/nature03989; PMID: 16148934
   PubMed Web of Science ®Google Scholar
• Dobson CM. Protein folding and misfolding. Nature 2003; 426:884 - 90; http://dx.doi.org/10.1038/nature02261; PMID: 14685248
   PubMed Web of Science ®Google Scholar
• Chernoff YO. Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition?. Curr Opin Chem Biol 2004; 8:665 - 71; http://dx.doi.org/10.1016/j.cbpa.2004.09.002; PMID: 15556413
   PubMed Web of Science ®Google Scholar
• Eichner T, Radford SE. A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 2011; 43:8 - 18; http://dx.doi.org/10.1016/j.molcel.2011.05.012; PMID: 21726806
   PubMed Web of Science ®Google Scholar
• Wolfe KJ, Cyr DM. Amyloid in neurodegenerative diseases: friend or foe?. Semin Cell Dev Biol 2011; 22:476 - 81; http://dx.doi.org/10.1016/j.semcdb.2011.03.011; PMID: 21458579
   PubMed Web of Science ®Google Scholar
• Duennwald ML. Polyglutamine misfolding in yeast: toxic and protective aggregation. Prion 2011; 5:285 - 90; PMID: 22052348
   PubMed Web of Science ®Google Scholar
• Barten DM, Albright CF. Therapeutic strategies for Alzheimer’s disease. Mol Neurobiol 2008; 37:171 - 86; http://dx.doi.org/10.1007/s12035-008-8031-2; PMID: 18581273
   PubMed Web of Science ®Google Scholar
• Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, et al. A causative link between the structure of aberrant protein oligomers and their toxicity. Nat Chem Biol 2010; 6:140 - 7; PMID: 20081829
   PubMed Web of Science ®Google Scholar
• Binger KJ, Griffin MD, Heinemann SH, Howlett GJ. Methionine-oxidized amyloid fibrils are poor substrates for human methionine sulfoxide reductases A and B2. Biochemistry 2010; 49:2981 - 3; http://dx.doi.org/10.1021/bi902203m; PMID: 20218727
   PubMed Web of Science ®Google Scholar
• O’Sullivan DB, Jones CE, Abdelraheim SR, Thompsett AR, Brazier MW, Toms H, Brown DR, Viles JH. NMR characterization of the pH 4 β-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility. Biochem J 2007; 401:533 - 40; http://dx.doi.org/10.1042/BJ20060668; PMID: 16958619
   PubMed Web of Science ®Google Scholar
• Bocharova OV, Breydo L, Salnikov VV, Baskakov IV. Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry 2005; 44:6776 - 87; http://dx.doi.org/10.1021/bi050251q; PMID: 15865423
   PubMed Web of Science ®Google Scholar
• Sun Y, Breydo L, Makarava N, Yang Q, Bocharova OV, Baskakov IV. Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. J Biol Chem 2007; 282:9090 - 7; http://dx.doi.org/10.1074/jbc.M608623200; PMID: 17244617
   PubMed Web of Science ®Google Scholar
• Alonso DO, DeArmond SJ, Cohen FE, Daggett V. Mapping the early steps in the pH-induced conformational conversion of the prion protein. Proc Natl Acad Sci U S A 2001; 98:2985 - 9; http://dx.doi.org/10.1073/pnas.061555898; PMID: 11248018
   PubMed Web of Science ®Google Scholar
• Kaimann T, Metzger S, Kuhlmann K, Brandt B, Birkmann E, Höltje HD, Riesner D. Molecular model of an α-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. J Mol Biol 2008; 376:582 - 96; PMID: 18158160
   PubMed Web of Science ®Google Scholar
• Sideri TC, Koloteva-Levine N, Tuite MF, Grant CM. Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem 2011; 286:38924 - 31; PMID: 21832086
   PubMed Web of Science ®Google Scholar
• Dong J, Atwood CS, Anderson VE, Siedlak SL, Smith MA, Perry G, Carey PR. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 2003; 42:2768 - 73; http://dx.doi.org/10.1021/bi0272151; PMID: 12627941
   PubMed Web of Science ®Google Scholar
• Yamin G, Glaser CB, Uversky VN, Fink AL. Certain metals trigger fibrillation of methionine-oxidized α-synuclein. J Biol Chem 2003; 278:27630 - 5; http://dx.doi.org/10.1074/jbc.M303302200; PMID: 12754258
   PubMed Web of Science ®Google Scholar
• Georgieva D, Koker M, Redecke L, Perbandt M, Clos J, Bredehorst R, Genov N, Betzel C. Oligomerization of the proteolytic products is an intrinsic property of prion proteins. Biochem Biophys Res Commun 2004; 323:1278 - 86; http://dx.doi.org/10.1016/j.bbrc.2004.08.230; PMID: 15451435
   PubMed Web of Science ®Google Scholar