Interactions of recombinant prions with compounds of therapeutical significance

Biochemical and Biophysical Research Communications

Volumn 344, Issue 2, 2006, Pages 463-470

  Georgieva, Dessislava ^a   Schwark, Daniel ^a   von Bergen, Martin ^b   Redecke, Lars ^a   Genov, Nicolay ^c   Betzel, Christian ^a  

^a UNIVERSITY OF HAMBURG   (Germany)

^b MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

^c INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

Author keywords

Dynamic light scattering; Prion protein; Protein misfolding; Proteinase; Proteolysis; Structural transformation

Indexed keywords

CONGO RED; DOXYCYCLINE HYCLATE; MEPACRINE; PRION PROTEIN; PROMAZINE; QUINIDINE; QUININE; RECOMBINANT PRION PROTEIN; TETRACYCLINE; TRIMETHYLAMINE OXIDE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; BIOACCUMULATION; DESTRUCTION; DRUG ACTIVITY; DRUG MECHANISM; INFECTION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; STIMULATION;

BINDING SITES; DOXYCYCLINE; METHYLAMINES; PRIONS; PROMAZINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; QUINACRINE; QUINOLINES; RECOMBINANT PROTEINS; TETRACYCLINE;

EID: 33646105864     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.03.135     Document Type: Article

References (26)

1. Prusiner S.B. Prions (Nobel Lecture). Proc. Natl. Acad. Sci. USA 95 (1998) 13363-13383
2. Parchi P., and Gambetti P. Human prion diseases. Curr. Opin. Neurol. 8 (1995) 193-286
3. Garcia F.L., Zahn R., Riek R., and Wüthrich K. NMR structure of the bovine prion protein. Proc. Natl. Acad. Sci. USA 97 (2000) 8334-8339
4. Will R.G., Ironside J.W., Zeidler M., Cousens S.N., Estibeiro K., Alperovitch A., Poser S., Pocchiari M., Hofman A., and Smith P.G. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347 (1996) 921-925
5. Lorenz H., Windle O., and Kretzschmar H.A. Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J. Biol. Chem. 277 (2002) 8508-8516
6. Viles J.H., Cohen F.E., Prusiner S.B., Goodin D.B., Wright P.E., and Dyson H.J. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA 96 (1999) 2042-2047
7. Pauly P.C., and Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273 (1998) 33107-33110
8. Rachidi W., Vilette D., Guiraud P., Arlotto M., Riondel J., Laude H., Lehmann S., and Favier A. Expression of prion protein increases cellular copper binding and antioxidant enzyme activitiy but not copper delivery. J. Biol. Chem. 278 (2003) 9064-9072
9. Sigurdsson E.M., Brown D.R., Alim M.A., Scholtzova H., Carp R., Meeker H.C., Prelli F., Frangione B., and Wisniewski T. Copper helation delays the onset of prion disease. J. Biol. Chem. 278 (2003) 46199-46202
10. Zahn R., Von Schroetter Ch., and Wüthrich K. Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett. 417 (1997) 400-404
11. Georgieva D., Koker M., Redecke L., Perbandt M., Clos J., Bredehorst R., Genov N., and Betzel Ch. Oligomerization of the proteolytic products is an intrinsic property of prion proteins. Biochem. Biophys. Res. Commun. 323 (2004) 1278-1286
12. Genov N., Shopova M., Boteva R., Jori G., and Ricchelli F. Chemical photochemical and spectroscopic characterization of an alkaline proteinase from Bacillus subtilis variant DY. Biochem. J. 207 (1982) 201-207
13. Karadjova M., Bakurdjieva A., and Velcheva P. On the composition of the enzyme preparation E-30 - characteristics of the proteolitic enzymes in it. Compt. Rend. Bulg. Acad. Sci. 23 (1970) 431-434
14. Follette P. Prion disease treatment's early promise unravels. Science 299 (2003) 191-192
15. Barret A., Tagliavini F., Forloni G., Bate C., Salmona M., Colombo L., De Luigi A., Limido L., Suardi S., Rossi G., Auvre F., Adjou K.T., Sales N., Williams A., Lasmezas C., and Deslys J.P. Evaluation of quinacrine treatment for prion diseases. J. Virol. 77 (2003) 8462-8469
16. Korth C., May B.C.H., Cohen F.E., and Prusiner S.B. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. USA 98 (2001) 9836-9841
17. Nakajima M., Yamada T., Kusuhara T., Furukawa H., Takahashi M., Yamauchi A., and Kataoka Y. Results of quinacrine administration to patients with Creutzfeldt-Jakob disease. Dement. Geriatr. Cogn. Disord. 17 (2004) 158-163
18. Murakami-Kubo I., Doh-ura K., Ishikawa K., Kawatake S., Sasaki K., Kira J.-I., Ohta S., and Iwaki T. Quinoline derivatives are therapeutic candidates for transmissible spongiform encephalopathies. J. Virol. 78 (2004) 1281-1288
19. Tatzelt J., Prusiner S.B., and Welch W.J. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15 (1996) 6363-6373
20. Forloni G., Iussich S., Awan T., Colombo L., Angeretti N., Girola L., Bertani I., Poli G., Caramelli M., Bruzzone M.G., Farina L., Rossi G., Giaccone G., Ironside J.W., Bugiani O., Salmona M., and Tagliavini F. Tetracyclines affect prion infectivity. Proc. Natl. Acad. Sci. USA 99 (2002) 10849-10854
21. Tremblay P., Meiner Z., Galou M., Heinrich C., Petromilli C., Lisse T., Cayetano J., Torchia M., Mobley W., Bujard H., DeArmond S.J., and Prusiner S.B. Doxycycline control of prion protein transgene expression modulates prion disease in mice. Proc. Natl. Acad. Sci. USA 95 (1998) 12580-12585
22. Koster T., Singh K., Zimmermann M., and Gruys E. Emerging therapeutic agents for transmissible spongiform encephalopathies: a review. J. Veter. Pharmacol. Therapeut. 26 (2003) 315-326
23. Sellarajah S., Lekishvili T., Bowring C., Thompsett A.R., Rudyk H., Birkett C.R., Brown D.R., and Gilbert I.H. Synthesis of analogues of Congo red and evaluation of their anti-prion activity. J. Med. Chem. 47 (2004) 5515-5534
24. Vogther M., Grimme S., Elshorst B., Jacobs D.M., Fiebig K., Griesinger C., and Zahn R. Antimalarial drug quinacrine binds to C-terminal helix of cellular prion protein. J. Med. Chem. 46 (2003) 3563-3564
25. Zahn R., Liu A., Luhrs T., Riek R., Von Schroetter Ch., Garcia F.L., Billeter M., Calzolai L., Wider G., and Wütrich K. NMR solution structure of the human prion protein. Proc. Natl. Acad. Sci. USA 97 (2000) 145-150
26. James T.L., Liu H., Ulyanov N., Farr-Jones S., Zhang H., Donne D.G., Kaneko K., Groth D., Mehlhorn I., Prusiner S.B., and Cohen F.E. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94 (1997) 10086-10091