Plasminogen

References

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 144
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363 - 13383
   PubMed Web of Science ®Google Scholar
• Basler K, Oesch B, Scott M, Westaway D, Walchli M, Groth DF, et al. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 1986; 46:417 - 428
   PubMed Web of Science ®Google Scholar
• Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, et al. Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90:10962 - 10966
   PubMed Web of Science ®Google Scholar
• Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS. Secondary structure analysis of the scrapie-associated protein PrP 27–30 in water by infrared spectroscopy. Biochemistry 1991; 30:7672 - 7680
   PubMed Web of Science ®Google Scholar
• Bueler H, Aguzzi A, Sailer A, Greiner RA, Autenried P, Aguet M, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73:1339 - 1347
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Molecular biology of prion diseases. Science 1991; 252:1515 - 1522
   PubMed Web of Science ®Google Scholar
• Cohen FE, Prusiner SB. Pathologic conformations of prion proteins. Annu Rev Biochem 1998; 67:793 - 819
   PubMed Web of Science ®Google Scholar
• Kim J, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 2010; 285:14083 - 14087
   PubMed Web of Science ®Google Scholar
• Makarava N, Kovacs GG, Bocharova O, Savtchenko R, Alexeeva I, Budka H, et al. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 2010; 119:177 - 187
   PubMed Web of Science ®Google Scholar
• Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J Biol Chem 2005; 280:26873 - 26879
   PubMed Web of Science ®Google Scholar
• Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003; 425:717 - 720
   PubMed Web of Science ®Google Scholar
• Wong C, Xiong LW, Horiuchi M, Raymond L, Wehrly K, Chesebro B, et al. Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein. EMBO J 2001; 20:377 - 386
   PubMed Web of Science ®Google Scholar
• DebBurman SK, Raymond GJ, Caughey B, Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc Natl Acad Sci USA 1997; 94:13938 - 13943
   PubMed Web of Science ®Google Scholar
• Dandoy-Dron F, Bogdanova A, Beringue V, Bailly Y, Tovey MG, Laude H, et al. Infection by ME7 prion is not modified in transgenic mice expressing the yeast chaperone Hsp104 in neurons. Neurosci Lett 2006; 405:181 - 185
   PubMed Web of Science ®Google Scholar
• Kenward N, Hope J, Landon M, Mayer RJ. Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain. J Neurochem 1994; 62:1870 - 1877
   PubMed Web of Science ®Google Scholar
• Shyu WC, Kao MC, Chou WY, Hsu YD, Soong BW. Creutzfeldt-Jakob disease: heat shock protein 70 mRNA levels in mononuclear blood cells and clinical study. J Neurol 2000; 247:929 - 934
   PubMed Web of Science ®Google Scholar
• Fernandez-Funez P, Casas-Tinto S, Zhang Y, Gomez-Velazquez M, Morales-Garza MA, Cepeda-Nieto AC, et al. In vivo generation of neurotoxic prion protein: Role for Hsp70 in accumulation of misfolded isoforms. PLoS Genet 2009; 5:1000507
   PubMed Web of Science ®Google Scholar
• Ehlers B, Diringer H. Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J Gen Virol 1984; 65:1325 - 1330
   PubMed Web of Science ®Google Scholar
• Kimberlin RH, Walker CA. Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate and some other polyanions. Antimicrob Agents Chemother 1986; 30:409 - 413
   PubMed Web of Science ®Google Scholar
• Caughey B, Raymond GJ. Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J Virol 1993; 67:643 - 650
   PubMed Web of Science ®Google Scholar
• Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 2007; 104:9741 - 9746
   PubMed Web of Science ®Google Scholar
• Ryou C, Prusiner SB, Legname G. Cooperative binding of dominant-negative prion protein to kringle domains. J Mol Biol 2003; 329:323 - 333
   PubMed Web of Science ®Google Scholar
• Cuccioloni M, Amici M, Eleuteri AM, Biagetti M, Barocci S, Angeletti M. Binding of recombinant PrPc to human plasminogen: Kinetic and thermodynamic study using a resonant mirror biosensor. Proteins 2005; 58:728 - 734
   PubMed Web of Science ®Google Scholar
• Ellis V, Daniels M, Misra R, Brown DR. Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry 2002; 41:6891 - 6896
   PubMed Web of Science ®Google Scholar
• Epple G, Langfeld K, Baier M, Holzhütter HG, Schleuning WD, Köttgen E, et al. Both lysine-clusters of the NH2-terminal prion-protein fragment PrP23–110 are essential for t-PA mediated plasminogen activation. Thromb Haemost 2004; 91:465 - 471
   PubMed Web of Science ®Google Scholar
• Epple G, Schleuning WD, Kettelgerdes G, Kottgen E, Geßner R, Praus M. Prion protein stimulates tissue-type plasminogen activator-mediated plasmin generation via a lysine-binding site on kringle 2. J Thromb Haemost 2004; 2:962 - 968
   PubMed Web of Science ®Google Scholar
• Kornblatt JA, Marchal S, Razaei H, Balny C. Characterization of a complex formed between human plasminogen and recombinant sheep prion: pressure and thermal sensitivity of complex formation. Cell Mol Biol (Noisy-le-grand) 2004; 50:387 - 396
   PubMed Web of Science ®Google Scholar
• Praus M, Kettelgerdes G, Baier M, Holzhütter HG, Jungblut PR, Maissen M, et al. Stimulation of plasminogen activation by recombinant cellular prion protein is conserved in the NH2-terminal fragment PrP23–110. Thromb Haemost 2003; 89:812 - 819
   PubMed Web of Science ®Google Scholar
• Fischer MB, Roeckl C, Parizek P, Schwarz HP, Aguzzi A. Binding of disease-associated prion protein to plasminogen. Nature 2000; 408:479 - 483
   PubMed Web of Science ®Google Scholar
• Maissen M, Roeckl C, Glatzel M, Goldmann W, Aguzzi A. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 2001; 357:2026 - 2028
   PubMed Web of Science ®Google Scholar
• Hatcher K, Zheng J, Chen SG. Cryptic peptides of the kringle domains preferentially bind to disease-associated prion protein. J Alz Dis 2009; 16:421 - 431
   PubMed Web of Science ®Google Scholar
• Negredo C, Monks E, Sweeney T. A novel real-time ultrasonic method for prion protein detection using plasminogen as a capture molecule. BMC Biotechnol 2007; 7:43
   PubMed Web of Science ®Google Scholar
• Shaked Y, Engelstein R, Gabizon R. The binding of prion proteins to serum components is affected by detergent extraction conditions. J Neurochem 2002; 82:1 - 5
   PubMed Web of Science ®Google Scholar
• Mays CE, Ryou C. Plasminogen stimulates propagation of protease-resistant prion protein in vitro. FASEB J 2010; 24:5102 - 5112
   PubMed Web of Science ®Google Scholar
• Salmona M, Capobianco R, Colombo L, De Luigi A, Rossi G, Mangieri M, et al. Role of plasminogen in propagation of scrapie. J Virol 2005; 79:11225 - 11230
   PubMed Web of Science ®Google Scholar
• Xanthopoulos K, Paspaltsis I, Apostolidou V, Petrakis S, Siao CJ, Kalpatsanidis A, et al. Tissue plasminogen activator in brain tissues infected with transmissible spongiform encephalopathies. Neurobiol Dis 2005; 20:519 - 527
   PubMed Web of Science ®Google Scholar
• Bugge TH, Flick MJ, Daugherty CC, Degen JL. Plasminogen deficiency causes severe thrombosis but is compatible with development and reproduction. Genes Dev 1995; 9:794 - 807
   PubMed Web of Science ®Google Scholar
• Ploplis VA, Carmeliet P, Vazirzadeh S, Van Vlaenderen I, Moons L, Plow EF, et al. Effects of disruption of the plasminogen gene on thrombosis, growth and health in mice. Circulation 1995; 92:2585 - 2593
   PubMed Web of Science ®Google Scholar
• Degen JL, Drew AF, Palumbo JS, Kombrinck KW, Bezerra JA, Danton MJS, et al. Genetic manipulation of fibrinogen and fibrinolysis in mice. Ann NY Acad Sci 2001; 936:276 - 290
   PubMed Web of Science ®Google Scholar
• Castellino FJ, McCance SG. The kringle domains of human plasminogen. Ciba Found Symp 1997; 212:46 - 60
   PubMedGoogle Scholar
• Trevitt CR, Collinge J. A systematic review of prion therapeutics in experimental models. Brain 2006; 129:2241 - 2265
   PubMed Web of Science ®Google Scholar