Vitamin D₂ interacts with Human PrP^c (90–231) and breaks PrP^c oligomerization in vitro

References

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; http://dx.doi.org/10.1126/science.6801762; PMID: 6801762
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci U S A 1998; 95:13363 - 83; http://dx.doi.org/10.1073/pnas.95.23.13363; PMID: 9811807
   PubMed Web of Science ®Google Scholar
• Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. Structural clues to prion replication. Science 1994; 264:530 - 1; http://dx.doi.org/10.1126/science.7909169; PMID: 7909169
   PubMed Web of Science ®Google Scholar
• Castilla J, Saá P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121:195 - 206; http://dx.doi.org/10.1016/j.cell.2005.02.011; PMID: 15851027
   PubMed Web of Science ®Google Scholar
• Castilla J, Saá P, Soto C. Detection of prions in blood. Nat Med 2005; 11:982 - 5; PMID: 16127436
   PubMed Web of Science ®Google Scholar
• Brown DR, Wong BS, Hafiz F, Clive C, Haswell SJ, Jones IM. Normal prion protein has an activity like that of superoxide dismutase. Biochem J 1999; 344:1 - 5; http://dx.doi.org/10.1042/0264-6021:3440001; PMID: 10548526
   PubMed Web of Science ®Google Scholar
• Kuwahara C, Takeuchi AM, Nishimura T, Haraguchi K, Kubosaki A, Matsumoto Y, et al. Prions prevent neuronal cell-line death. Nature 1999; 400:225 - 6; http://dx.doi.org/10.1038/22241; PMID: 10421360
   PubMed Web of Science ®Google Scholar
• Nieznanski K, Choi JK, Chen S, Surewicz K, Surewicz WK. Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity. J Biol Chem 2012; 287:33104 - 8; http://dx.doi.org/10.1074/jbc.C112.400614; PMID: 22915585
   PubMed Web of Science ®Google Scholar
• Hetz C, Maundrell K, Soto C. Is loss of function of the prion protein the cause of prion disorders?. Trends Mol Med 2003; 9:237 - 43; http://dx.doi.org/10.1016/S1471-4914(03)00069-8; PMID: 12829011
   PubMed Web of Science ®Google Scholar
• Rezaei H. Prion protein oligomerization. Curr Alzheimer Res 2008; 5:572 - 8; http://dx.doi.org/10.2174/156720508786898497; PMID: 19075584
   PubMed Web of Science ®Google Scholar
• Kelly JW. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 1998; 8:101 - 6; http://dx.doi.org/10.1016/S0959-440X(98)80016-X; PMID: 9519302
   PubMed Web of Science ®Google Scholar
• Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75:333 - 66; http://dx.doi.org/10.1146/annurev.biochem.75.101304.123901; PMID: 16756495
   PubMed Web of Science ®Google Scholar
• Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, et al. 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
• Soto C, Kascsak RJ, Saborío GP, Aucouturier P, Wisniewski T, Prelli F, et al. Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 2000; 355:192 - 7; http://dx.doi.org/10.1016/S0140-6736(99)11419-3; PMID: 10675119
   PubMed Web of Science ®Google Scholar
• Vidal C, Herzog C, Haeberle AM, Bombarde C, Miquel MC, Carimalo J, et al. Early dysfunction of central 5-HT system in a murine model of bovine spongiform encephalopathy. Neuroscience 2009; 160:731 - 43; http://dx.doi.org/10.1016/j.neuroscience.2009.02.072; PMID: 19285121
   PubMed Web of Science ®Google Scholar
• Cavaliere P, Torrent J, Prigent S, Granata V, Pauwels K, Pastore A, et al. Binding of methylene blue to a surface cleft inhibits the oligomerization and fibrillization of prion protein. Biochim Biophys Acta 2013; 1832:20 - 8; http://dx.doi.org/10.1016/j.bbadis.2012.09.005; PMID: 23022479
   PubMed Web of Science ®Google Scholar
• Muyrers J, Klingenstein R, Stitz L, Korth C. Structure-activity relationship of tocopherol derivatives suggesting a novel non-antioxidant mechanism in antiprion potency. Neurosci Lett 2010; 469:122 - 6; http://dx.doi.org/10.1016/j.neulet.2009.11.057; PMID: 19945507
   PubMed Web of Science ®Google Scholar
• James TL, Liu H, Ulyanov NB, Farr-Jones S, Zhang H, Donne DG, et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci U S A 1997; 94:10086 - 91; http://dx.doi.org/10.1073/pnas.94.19.10086; PMID: 9294167
   PubMed Web of Science ®Google Scholar
• Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, et al. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 1999; 38:5362 - 77; http://dx.doi.org/10.1021/bi982878x; PMID: 10220323
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Molecular biology and pathogenesis of prion diseases. Trends Biochem Sci 1996; 21:482 - 7; http://dx.doi.org/10.1016/S0968-0004(96)10063-3; PMID: 9009832
   PubMed Web of Science ®Google Scholar
• Collinge J. Human prion diseases and bovine spongiform encephalopathy (BSE). Hum Mol Genet 1997; 6:1699 - 705; http://dx.doi.org/10.1093/hmg/6.10.1699; PMID: 9300662
   PubMed Web of Science ®Google Scholar
• Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Prion protein biology. Cell 1998; 93:337 - 48; http://dx.doi.org/10.1016/S0092-8674(00)81163-0; PMID: 9590169
   PubMed Web of Science ®Google Scholar
• James TL, Liu H, Ulyanov NB, Farr-Jones S, Zhang H, Donne DG, et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci U S A 1997; 94:10086 - 91; http://dx.doi.org/10.1073/pnas.94.19.10086; PMID: 9294167
   PubMed Web of Science ®Google Scholar
• Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, et al. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 1999; 38:5362 - 77; http://dx.doi.org/10.1021/bi982878x; PMID: 10220323
   PubMed Web of Science ®Google Scholar
• Huang Z, Gabriel JM, Baldwin MA, Fletterick RJ, Prusiner SB, Cohen FE. Proposed three-dimensional structure for the cellular prion protein. Proc Natl Acad Sci U S A 1994; 91:7139 - 43; http://dx.doi.org/10.1073/pnas.91.15.7139; PMID: 7913747
   PubMed Web of Science ®Google Scholar
• Leclerc E, Peretz D, Ball H, Sakurai H, Legname G, Serban A, et al. Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J 2001; 20:1547 - 54; http://dx.doi.org/10.1093/emboj/20.7.1547; PMID: 11285219
   PubMed Web of Science ®Google Scholar
• Verma A, Sharma S, Ganguly NK, Majumdar S, Guptasarma P, Luthra-Guptasarma M. Identification and characterization of a spontaneously aggregating amyloid-forming variant of human PrP((90-231)) through phage-display screening of variants randomized between residues 101 and 112. Int J Biochem Cell Biol 2008; 40:663 - 76; http://dx.doi.org/10.1016/j.biocel.2007.10.009; PMID: 18023239
   PubMed Web of Science ®Google Scholar
• Moroncini G, Kanu N, Solforosi L, Abalos G, Telling GC, Head M, et al. Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc. Proc Natl Acad Sci U S A 2004; 101:10404 - 9; http://dx.doi.org/10.1073/pnas.0403522101; PMID: 15240877
   PubMed Web of Science ®Google Scholar
• Hanan E, Priola SA, Solomon B. Antiaggregating antibody raised against human PrP 106-126 recognizes pathological and normal isoforms of the whole prion protein. Cell Mol Neurobiol 2001; 21:693 - 703; http://dx.doi.org/10.1023/A:1015199904354; PMID: 12043842
   PubMed Web of Science ®Google Scholar
• Florio T, Paludi D, Villa V, Principe DR, Corsaro A, Millo E, et al. Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J Neurochem 2003; 85:62 - 72; http://dx.doi.org/10.1046/j.1471-4159.2003.01664.x; PMID: 12641727
   PubMed Web of Science ®Google Scholar
• Brown DR, Schmidt B, Kretzschmar HA. Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 1996; 380:345 - 7; http://dx.doi.org/10.1038/380345a0; PMID: 8598929
   PubMed Web of Science ®Google Scholar
• Chabry J, Ratsimanohatra C, Sponne I, Elena PP, Vincent JP, Pillot T. In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. J Neurosci 2003; 23:462 - 9; PMID: 12533606
   PubMed Web of Science ®Google Scholar
• Kanyo ZF, Pan KM, Williamson RA, Burton DR, Prusiner SB, Fletterick RJ, et al. Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change. J Mol Biol 1999; 293:855 - 63; http://dx.doi.org/10.1006/jmbi.1999.3193; PMID: 10543972
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680 - 5; http://dx.doi.org/10.1038/227680a0; PMID: 5432063
   PubMed Web of Science ®Google Scholar
• Blackwood JE, Gladys CL, Loening KI, Petrarca AE, Ruth JE. Unambiguous specification of stereoisomerism about a double bonds. J Am Chem Soc 1968; 90:509 - 10; http://dx.doi.org/10.1021/ja01004a063
   Web of Science ®Google Scholar
• Hunt RD, Garcia FG, Hegsted DM, Kaplinsky N. Vitamin D2 and vitamin D3 in new world primates: influence on calcium absorption. Science 1967; 158:943 - 5; http://dx.doi.org/10.1126/science.157.3791.943
   Web of Science ®Google Scholar
• Steenbock H, Kletzien SWF, Haplin JG. The reaction of the chicken to irradiated ergosterol and irradiated yeast as contrasted with natural vitamin D of fish liver oils. J Biol Chem 1932; 97:249 - 64
   Google Scholar
• Trang HM, Cole DE, Rubin LA, Pierratos A, Siu S, Vieth R. Evidence that vitamin D3 increases serum 25-hydroxyvitamin D more efficiently than does vitamin D2. Am J Clin Nutr 1998; 68:854 - 8; PMID: 9771862
   PubMed Web of Science ®Google Scholar
• Marx SJ, Jones G, Weinstein RS, Chrousos GP, Renquist DM. Differences in mineral metabolism among nonhuman primates receiving diets with only vitamin D3 or only vitamin D2. J Clin Endocrinol Metab 1989; 69:1282 - 90; http://dx.doi.org/10.1210/jcem-69-6-1282; PMID: 2555385
   PubMed Web of Science ®Google Scholar
• Mawer EB, Jones G, Davies M, Still PE, Byford V, Schroeder NJ, et al. Unique 24-hydroxylated metabolites represent a significant pathway of metabolism of vitamin D2 in humans: 24-hydroxyvitamin D2 and 1,24-dihydroxyvitamin D2 detectable in human serum. J Clin Endocrinol Metab 1998; 83:2156 - 66; http://dx.doi.org/10.1210/jc.83.6.2156; PMID: 9626155
   PubMed Web of Science ®Google Scholar
• Holmberg I, Berlin T, Ewerth S, Björkhem I. 25-Hydroxylase activity in subcellular fractions from human liver. Evidence for different rates of mitochondrial hydroxylation of vitamin D2 and D3. Scand J Clin Lab Invest 1986; 46:785 - 90; http://dx.doi.org/10.3109/00365518609084051; PMID: 3026027
   PubMed Web of Science ®Google Scholar
• Guo YD, Strugnell S, Back DW, Jones G. Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. Proc Natl Acad Sci U S A 1993; 90:8668 - 72; http://dx.doi.org/10.1073/pnas.90.18.8668; PMID: 7690968
   PubMed Web of Science ®Google Scholar
• Jones G, Byrnes B, Palma F, Segev D, Mazur Y. Displacement potency of vitamin D2 analogs in competitive protein-binding assays for 25-hydroxyvitamin D3, 24,25-dihydroxyvitamin D3, and 1,25-dihydroxyvitamin D3. J Clin Endocrinol Metab 1980; 50:773 - 5; http://dx.doi.org/10.1210/jcem-50-4-773; PMID: 6965943
   PubMed Web of Science ®Google Scholar
• Hoffmann RW. Allylic 1,3-strain as a controlling factor in stereoselective Transformations. Chem Rev 1989; 89:1841 - 60; http://dx.doi.org/10.1021/cr00098a009
   Web of Science ®Google Scholar
• Wiberg KB, Martin E. Barriers to rotation adjacent to double bonds. J Am Chem Soc 1985; 107:5035 - 41; http://dx.doi.org/10.1021/ja00304a002; PMID: 22175333
   PubMed Web of Science ®Google Scholar
• Tsoukas CD, Provvedini DM, Manolagas SC. 1,25-dihydroxyvitamin D3: a novel immunoregulatory hormone. Science 1984; 224:1438 - 40; http://dx.doi.org/10.1126/science.6427926; PMID: 6427926
   PubMed Web of Science ®Google Scholar
• Lemire JM. Immunomodulatory actions of 1,25-dihydroxyvitamin D3. J Steroid Biochem Mol Biol 1995; 53:599 - 602; http://dx.doi.org/10.1016/0960-0760(95)00106-A; PMID: 7626516
   PubMed Web of Science ®Google Scholar
• Simpson S Jr., Taylor B, Blizzard L, Ponsonby AL, Pittas F, Tremlett H, et al. Higher 25-hydroxyvitamin D is associated with lower relapse risk in multiple sclerosis. Ann Neurol 2010; 68:193 - 203; PMID: 20695012
   PubMed Web of Science ®Google Scholar
• Malmqvist M. BIACORE: an affinity biosensor system for characterization of biomolecular interactions. Biochem Soc Trans 1999; 27:335 - 40; PMID: 10093759
   PubMed Web of Science ®Google Scholar
• Johnsson B, Löfås S, Lindquist G. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal Biochem 1991; 198:268 - 77; http://dx.doi.org/10.1016/0003-2697(91)90424-R; PMID: 1724720
   PubMed Web of Science ®Google Scholar