In vitro Evaluation of the Anti-prionic Activity of Newly Synthesized Congo Red Derivatives

Arzneimittel-Forschung/Drug Research

Volumn 53, Issue 12, 2003, Pages 875-888

  Poli, Giorgio ^a,c   Ponti, Wilma ^a   Carcassola, Gabriella ^a   Ceciliani, Fabrizio ^a   Colombo, Laura ^b   Dall'Ara, Paola ^a   Gervasoni, Marco ^a   Giannino, Maria Laura ^a   Martino, Piera Anna ^a   Pollera, Claudia ^a   Villa, Stefania ^a   Salmona, Mario ^b  

^a UNIVERSITY OF MILAN   (Italy)

^b MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

^c Sezione di Microbiologia e Immunologia Veterinaria   (Italy)

Author keywords

Bovine spongiform encephalopathy (BSE); CAS 573 58 0; Congo Red, anti prionic activity, in vitro studies; Prion protein

Indexed keywords

3,5 DIAMINONAPHTHALENE 1 SULFONIC ACID; AMINO ACID; AMYLOID; CONGO RED; DYE; GUANIDINE DERIVATIVE; GUANIDINE THIOCYANATE; NAPHTHALENESULFONIC ACID DERIVATIVE; PEPTIDE; PRION PROTEIN; PRION PROTEIN RES; PRION PROTEIN [106-126]; PROTEIN; PROTEINASE; PROTEINASE K; UNCLASSIFIED DRUG;

AMYLOIDOSIS; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BOVINE SPONGIFORM ENCEPHALOPATHY; CELL FREE SYSTEM; CELL LINE; CHEMOLUMINESCENCE; CONTROLLED STUDY; CREUTZFELDT JAKOB DISEASE; CULTURE MEDIUM; DOSE RESPONSE; DRUG ACTIVITY; DRUG MECHANISM; DRUG SYNTHESIS; ELECTRON MICROSCOPY; FIBER; FLOW CYTOMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IMMUNOFLUORESCENCE; IN VITRO STUDY; LIPOPHILICITY; NEUROBLASTOMA CELL; NONHUMAN; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN STABILITY; SCRAPIE; SYRIAN HAMSTER; WESTERN BLOTTING;

EID: 9144223018     PISSN: 00044172     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0031-1299845     Document Type: Article

References (54)

1. Baldwin, A., Cohen, F., E., Prusiner, S. B., Prion protein isoforms, a convergence of biological and structural investigations. J. Biol. Chem. 270, 19197 (1995)
2. Béranger, F., Mangé, A., Solassol, J. et al., Cell culture models of Transmissible Spongiform Encephalopathies. Biochem. Biophys. Res. Commun. 289, 311 (2001)
3. Bos, R. P., Koopman, J. P. Theuws, J., L. et al., The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: internal exposure of rats to benzidine after intestinal azo reduction. Mutat. Res. 181, 327 (1987)
4. Bosque, P. J., Prusiner, S. B., Cultured cell sublines highly susceptible to prion infection. J. Virol. 74, 4377 (2000)
5. Butler, D., A., Scott, M., R., D., Bockman, J. M. et al., Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J. Virol, 62, 1558 (1988)
6. Caspi, S., Halimi, M., Yanai, A. et al., The antiprion activity of Congo Red. Putative mechanism. J. Biol. Chem. 273, 3484 (1998)
7. Caughey, B., Race, R. E., Potent inhibition of scrapie-associated PrP accumulation by Congo Red. J. Neurochem. 59, 768 (1992)
8. Caughey, B., Raymond, G., J., Sulfated Polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J. Virol. 67, 643 (1993)
9. Caughey, B., Race, R. E., Scrapie-associated PrP accumulation and its inhibition: revisiting the amyloid glycosaminoglycan connection. Ann. NY Acad. Sci. 724, 290 (1994)
10. Caughey, B., Kocisko, D., A., Priola, S., A. et al., in: Methods in Molecular Medicine: Prion Disease, H. Baker, R. M. Ridley (eds.), pp. 285-300. Humana Press, Totowa (1997)
11. Caughey, W., S., Raymond, L., D., Horiuchi, M., et al., Inhibition of protease-resistant prion protein formation by porphyrins and phtalocyanines. Proc. Natl. Acad. Sci. USA 95, 12117 (1998)
12. Chaugey, B., Chesebro, B., Transmissible Spongiform encephalopathies and prion protein interconversion. Adv. Virus Res. 56, 277 (2001)
13. Clarke, M, Haig, D., A., Multiplication of scrapie agent in cell culture. Res. Vet. Sci. 11, 500 (1970)
14. De Gioia, L., Selavaggini, C., Ghibaudi, E. et al., Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J. Biol. Chem. 269, 7859 (1994)
15. Demaimay, R., Harper, J., Gordon, H. et al., Structural aspects of Congo Red as an inhibitor of protease-resistant prion protein formation. J. Neurochem. 71, 2534 (1998)
16. Demaimay, R., Chesebro, B., Caughey B., Inhibition of formation of protease-resistant prion protein by trypan blue, sirius red and other Congo red analogues. Arch. Virol. Suppl. 16, 277 (2000)
17. Ehlers, B., Diringer, H., Dextran sulfate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J. Gen. Virol. 65, 1325 (1984)
18. Forloni, G., Angeretti, N., Chiesa R. et al., Neurotoxicity of a prion protein fragment. Nature 362, 543 (1993)
19. Gabizon, R., Meiner, Z., Halimi, M. et al., Heparin-like molecules bind differentially to prion-proteins and change their intacellular metabolic fate. J. Cell Physiol. 157, 319 (1993)
20. Gasset, M., Baldwin, M., A., Lloyd, D. H. et al., Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid. Proc. Natl. Acad. Sci. USA 89, 10940 (1992)
21. Giaccone, G., Canciani, B., Puoti, G. et al., Creutzfeldt-Jakob disease: carnoy's fixative improves the immunohistochemistry of the proteinase K-resistant prion protein. Brain Pathol. 10, 31 (2000)
22. Hansen, M., B., Nielsen, S. E., Berg, K., Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell killing. J. Immunol. Methods 119, 203 (1989)
23. Harris, D. A., Cellular Biology of Prion Diseases. Clin. Microbiol. Rev. 12, 429 (1999)
24. Hirakura, Y., Yiu, W. W., Yamamoto, A. et al., Amiloyd Peptide channels: blockade by zinc and hinibition by Congo red (amyloid channel block). Amyloid 7, 194 (2000)
25. Jobling, M., F., Stewart, L. R., White, A. R. et al., The hydrophobic core sequence modulates the neurotoxic and secondary structure properties of the prion peptide 106-126. J. Neurochem. 73, 1557 (1999)
26. Kaneko, K., Zulianello, L., Scott, M. et al., Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94, 10069 (1997)
27. Kimberlin, R. H., Walker, C. A., Suppression of scrapie infection in mice by Heteropolyanion 23, Dextran Sulfate, and some other Polyanions. Antimicrob. Agents Chemother. 30, 409 (1986)
28. Korth, C., May B. C. H., Cohen, F. E. et al., Acridine and phenotiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. USA 98, 9836 (2001)
29. Lehmann, S., Harris, D. A., Blockade of glycosilation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479 (1997)
30. Merlini, G., Ascari, E., Amboldi, N. et al., Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis. Proc. Natl. Acad. Sci. USA 92, 2959 (1995)
31. Milhavet, O., Mangé, A., Casanova, D. et al., Effect of Congo Red on wild-type and mutated Prion Proteins in cultured cells. J. Neurochem. 74, 222 (2000)
32. Nishida, N., Harris, D. A., Vilette, D. et al., Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J. Virol. 74, 320 (2000)
33. Pan, K., M., Baldwin, M., Nguyen J. et al., Conversion of alpha helices into beta sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90, 10962 (1993)
34. Perrier, D., Wallace, A. C., Kaneko, K. et al., Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc. Natl. Acad. Sci. USA 97, 6073 (2000)
35. Priola, S. A., Caughey, B., Raymond, G., J. et al., Prion Protein and the scrapie agent: in vitro studies in infected neuroblastoma cells. Infect. Agents Dis. 3, 54 (1994)
36. Priola, S. A., Raines, A., Caughey, W. B., Porphyrins and phthalocyanine anti-scrapie compounds. Science 287, 1503 (2000)
37. Prusiner, S. B., Prions. Proc. Natl. Acad. Sci USA 95, 13363 (1998)
38. Race, R. E., Fadness, L. H, Chesebro, B., Characterization of scrapie infection in mouse neuroblastoma cells. J. Gen. Virol. 68, 1391 (1987)
39. Race, R. E., Caughey, B., Graham, K. et al., Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cells clones. J. Virol. 62, 2845 (1988)
40. 1H NMR and restrained molecular dynamics. Eur. J. Biochem. 266, 1192 (1999)
41. res in scrapie-infected cells. J. Gen. Virol. 81, 1155 (2000)
42. Rymer, D. L., Good, T. G., The role of prion peptide structure and aggregation in toxicity and membrane binding. J. Neurochem. 75, 2536 (2000)
43. Safar, J., Roller, P., Gajdusek, D. C. et al., Thermal stability and conformational transition of scrapie amyloid (prion) protein correlate with infectivity. J. Biol. Chem. 268, 20276 (1993)
44. Selvaggini, C., De Gioia, L., Cant-, L. et al., Molecular characteristics of a protease resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Biophys. Res. Commun. 194, 1380 (1993)
45. Seman, M., Adjou K. T., Perspective thérapeutiques des encéphalopathies subaigues spongiformes transmissibles. Rev. Prat. 49, 971 (1999)
46. Shearman, M. S., Toxicity of protein aggregates in PC12 cells: 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay. Methods Enzymol. 309, 716 (1999)
47. c, in cultured cells. J. Biol. Chem. 270, 30221 (1995)
48. Tagliavini, F., Prelli, F., Ghiso, J. et al., Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10, 513 (1991)
49. Tagliavini, F., Prelli, F., Verga, L. et al., Synthetic peptides homologous to prion protein residues 106-147 form amyloid like-fibrils in vitro. Proc. Natl. Acad. Sci. USA 90, 9678 (1993)
50. Tagliavini, F., McArthur, R. A., Canciani, B. et al., Effectiveness of anthracycline against experimental prion disease in Syrian hamsters. Science 276, 1119 (1997)
51. sc in vitro. J. Mol. Biol. 300, 1309 (2000)
52. Tagliavini, F., Forloni, G., D'Ursi, P., et al., Studies on peptide fragments of prion proteins. Adv. Protein Chem. 57, 171 (2001)
53. sc in scrapie-infected mouse neuroblastoma cells. Biol. Chem. 381, 463 (2000)
54. Wuthrich, K., Riek, R., Three-dimensional structures of prion proteins. Adv. Protein Chem. 57, 55 (2001)