The fate of the prion protein in the prion/plasminogen complex

Biochemical and Biophysical Research Communications

Volumn 305, Issue 3, 2003, Pages 518-522

  Kornblatt, Jack A ^a   Marchal, Stephane ^b   Rezaei, Human ^c   Kornblatt, M Judith ^a   Balny, Claude ^b   Lange, Reinhard ^b   Debey, Marie Pascale ^d   Bon Hoa, Gaston Hui ^b   Marden, Michael C ^b   Grosclaude, Jeanne ^c  

^a Gina Cody School of Engineering and Computer Science   (Canada)

^b INSERM   (France)

^c INRA Institut National de la Recherche Agronomique   (France)

^d MUSÉUM NATIONAL D'HISTOIRE NATURELLE   (France)

Author keywords

Plasminogen; Prion cleavage; Prion protein

Indexed keywords

PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; PRION PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

EID: 0037902533     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00804-0     Document Type: Article

References (32)

1. Gajdusek D.C. Unconventional viruses and the origin and disappearance of kuru. Science. 197:1977;943-960.
2. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science. 216:1982;136-144.
3. Prusiner S.B., Groth D., Serban A., Koehler R., Foster D., Torchia M., Burton D., Yang S.L., De Armond S.J. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA. 90:1993;10608-10612.
4. Oesch B., Westaway D., Walchli M., McKinley M.P., Kent S.B., Aebersold R., Barry R.A., Tempst P., Teplow D.B., Hood L.E. A cellular gene encodes scrapie PrP (27-30) protein. Cell. 40:1985;735-746.
5. Meyer R.K., McKinley M.P., Bowman K.A., Braunfeld M.B., Barry R.A., Prusiner S.B. Separation and properties of cellular and scrapie prion proteins. Proc. Natl. Acad. Sci. USA. 83:1986;2310-2314.
6. Priola S.A. Prion protein diversity and disease in the transmissible spongiform encephalopathies. Adv. Protein Chem. 57:2001;1-27.
7. Lopez G.F., Zahn R., Riek R., Wuthrich K. NMR structure of the bovine prion protein. Proc. Natl. Acad. Sci. USA. 97:2000;8334-8339.
8. Violand B.N., Byrne R., Castellino F.J. The effect of α, ω amino acids on human plasminogen structure and activation. J. Biol. Chem. 253:1978;5395-5401.
9. Kornblatt J.A., Kornblatt M.J., Clery C., Balny C. The effects of hydrostatic pressure on the conformation of plasminogen. Eur. J. Biochem. 265:1999;120-126.
10. Kornblatt J.A. Understanding the fluorescence changes of human plasminogen when it binds the ligand, 6-aminohexanoate: a synthesis. Biochim. Biophys. Acta. 1481:2000;1-10.
11. Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Lopez G.F., Billeter M., Calzolai L., Wider G., Wuthrich K. NMR solution structure of the human prion protein. Proc. Natl. Acad. Sci. USA. 97:2000;145-150.
12. Riek R., Hornemann S., Wider G., Glockshuber R., Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231). FEBS Lett. 413:1997;282-288.
13. Bachmann F. Haemostasis and Thrombosis. 1994;525-600 Chuchill Livingston, UK.
14. Gong Y., Kim S.O., Felez J., Grella D.K., Castellino F.J., Miles L.A. Conversion of Glu-plasminogen to Lys-plasminogen is necessary for optimal stimulation of plasminogen activation on the endothelial cell surface. J. Biol. Chem. 276:2001;19078-19083.
15. Miles L.A., Dahlberg C.M., Plescia J., Felez J., Kato K., Plow E.F. Role of cell-surface lysines in plasminogen binding to cells: identification of α-enolase as a candidate plasminogen receptor. Biochemistry. 30:1991;1682-1691.
16. Miles L.A., Castellino F.J., Gong Y. Critical role for conversion of glu-plasminogen to lys-plasminogen for optimal stimulation of plasminogen activation on cell surfaces. Trends Cardiovasc. Med. 13:2003;21-30.
17. Fredenburgh J.C., Nesheim M.E. Lys-plasminogen is a significant intermediate in the activation of Glu-plasminogen during fibrinolysis in vitro. J. Biol. Chem. 267:1992;26150-26156.
18. Fischer M.B., Roeckl C., Parizek P., Schwarz H.P., Aguzzi A. Binding of disease-associated prion protein to plasminogen. Nature. 408:2000;479-483.
19. Ellis V., Daniels M., Misra R., Brown D.R. Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry. 41:2002;6891-6896.
20. Maissen M., Roeckl C., Glatzel M., Goldmann W., Aguzzi A. Plasminogen binds to disease-associated prion protein of multiple species. Lancet. 357:2001;2026-2028.
21. Rezaei H., Marc D., Choiset Y., Takahashi M., Hui Bon H.G., Haertle T., Grosclaude J., Debey P. High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 267:2000;2833-2839.
22. Castellino F.J., Powell J.R. Human plasminogen. Methods Enzymol. 80(Pt C):1981;365-378.
23. Kornblatt J.A., Rajotte I., Heitz F. Reaction of canine plasminogen with 6-aminohexanoate: a thermodynamic study combining fluorescence, circular dichroism, and isothermal titration calorimetry. Biochemistry. 40:2001;3639-3647.
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
25. Shaked Y., Engelstein R., Gabizon R. The binding of prion proteins to serum components is affected by detergent extraction conditions. J. Neurochem. 82:2002;1-5.
26. Horrevoets A.J.G., Pannekoek H., Nesheim M.E. Production and characterization of recombinant human plasminogen (S741C-fluorescein). A novel approach to study zymogen activation without generation of active protease. J. Biol. Chem. 272:1997;2176-2182.
27. Foltmann B. A review on prorennin and rennin. C.R. Trav. Lab Carlsberg. 35:1966;143-231.
28. Gertler A., Walsh K.A., Neurath H. Catalysis by chymotrypsinogen. Demonstration of an acyl-zymogen intermediate. Biochemistry. 13:1974;1302-1310.
29. Markus G., Evers J.L., Hobika G.H. Comparison of some properties of native (Glu) and modified (Lys) human plasminogen. J. Biol. Chem. 253:1978;733-739.
30. Estelles A., Aznar J., Gilabert J. A qualitative study of soluble fibrin monomer complexes in normal labour and abruptio placentae. Thromb. Res. 18:1980;513-519.
31. Rabbani S.A., Mazar A.P. The role of the plasminogen activation system in angiogenesis and metastasis. Surg. Oncol. Clin. N. Am. 10:2001;393-415.
32. Bass R., Ellis V. Cellular mechanisms regulating non-haemostatic plasmin generation. Biochem. Soc. Trans. 30:2002;189-194.