Cooperative binding of dominant-negative prion protein to kringle domains

Journal of Molecular Biology

Volumn 329, Issue 2, 2003, Pages 323-333

  Ryou, Chongsuk ^a   Prusiner, Stanley B ^a,b   Legname, Giuseppe ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Cooperative binding; Dominant negative; Kringle domain; Phage display library; Prion protein

Indexed keywords

COMPLEMENTARY DNA; LYSINE; MUTANT PROTEIN; PRION PROTEIN; PROTEIN ANTIBODY; RECOMBINANT PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BETA SHEET; CODON; COMPARATIVE STUDY; CONTROLLED STUDY; DATA ANALYSIS; DNA LIBRARY; DOSE RESPONSE; ENZYME LINKED IMMUNOSORBENT ASSAY; IN VITRO STUDY; KRINGLE DOMAIN; MOLECULE; MOUSE; MUTATION; NEUROBLASTOMA CELL; NONHUMAN; PHAGE DISPLAY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; RADIOASSAY;

EID: 0038399786     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00342-5     Document Type: Article

References (59)

1. Prusiner S.B. An introduction to prion biology and diseases. Prusiner S.B. Prion Biology and Diseases. 1999;1-66 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
2. Prusiner S.B. Prions. Proc. Natl Acad. Sci. USA. 95:1998;13363-13383.
3. Prusiner S.B., Groth D., Serban A., Koehler R., Foster D., Torchia M., et al. 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. Büeler H., Aguzzi A., Sailer A., Greiner R.-A., Autenried P., Aguet M., Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell. 73:1993;1339-1347.
5. Prusiner S.B., Peters P., Kaneko K., Taraboulos A., Lingappa V., Cohen F.E., DeArmond S.J. Cell biology of prions. Prusiner S.B. Prion Biology and Diseases. 1999;349-391 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
6. Stahl N., Borchelt D.R., Hsiao K., Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell. 51:1987;229-240.
7. Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S.B. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibits formation of the scrapie isoform. J. Cell Biol. 129:1995;121-132.
8. Gorodinsky A., Harris D.A. Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J. Cell Biol. 129:1995;619-627.
9. Vey M., Pilkuhn S., Wille H., Nixon R., DeArmond S.J., Smart E.J., et al. Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc. Natl Acad. Sci. USA. 93:1996;14945-14949.
10. Kaneko K., Vey M., Scott M., Pilkuhn S., Cohen F.E., Prusiner S.B. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl Acad. Sci. USA. 94:1997;2333-2338.
11. Prusiner S.B., Kaneko K., Cohen F.E., Safar J., Riesner D. Some strategies and methods for the study of prions. Prusiner S.B. Prion Biology and Diseases. 1999;653-715 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
12. Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell. 83:1995;79-90.
13. Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., James T.L., 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. 94:1997;10069-10074.
14. Rogers M., Yehiely F., Scott M., Prusiner S.B. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl Acad. Sci. USA. 90:1993;3182-3186.
15. Zulianello L., Kaneko K., Scott M., Erpel S., Han D., Cohen F.E., Prusiner S.B. Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74:(9):2000;4351-4360.
16. Oesch B., Teplow D.B., Stahl N., Serban D., Hood L.E., Prusiner S.B. Identification of cellular proteins binding to the scrapie prion protein. Biochemistry. 29:1990;5848-5855.
17. Kurschner C., Morgan J.I. Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Mol. Brain Res. 37:1996;249-258.
18. C interacts with molecular chaperones of the Hsp60 family. J. Virol. 70:1996;4724-4728.
19. Rieger R., Edenhofer F., Lasmézas C.I., Weiss S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nature Med. 3:1997;1383-1388.
20. Martins V.R., Graner E., Garcia-Abreu J., de Souza S.J., Mercadante A.F., Veiga S.S., et al. Complementary hydropathy identifies a cellular prion protein receptor. Nature Med. 3:1997;1376-1382.
21. Yehiely F., Bamborough P., Costa M.D., Perry B.J., Thinakaran G., Cohen F.E., et al. Identification of candidate proteins binding to prion protein. Neurobiol. Dis. 3:1997;339-355.
22. Keshet G.I., Bar-Peled O., Yaffe D., Nudel U., Gabizon R. The cellular prion protein colocalizes with the dystroglycan complex in the brain. J. Neurochem. 75:2000;1889-1897.
23. Mouillet-Richard S., Ermonval M., Chebassier C., Laplanche J.L., Lehmann S., Launay J.M., Kellermann O. Signal transduction through prion protein. Science. 289:2000;1925-1928.
24. 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.
25. Graner E., Mercadante A.F., Zanata S.M., Forlenza O.V., Cabral A.L.B., Veiga S.S., et al. Cellular prion protein binds laminin and mediates neuritogenesis. Mol. Brain Res. 76:2000;85-92.
26. Gauczynski S., Peyrin J.M., Haik S., Leucht C., Hundt C., Rieger R., et al. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 20:2001;5863-5875.
27. Hundt C., Peyrin J.M., Haik S., Gauczynski S., Leucht C., Rieger R., et al. Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO J. 20:2001;5876-5886.
28. Schmitt-Ulms G., Legname G., Baldwin M.A., Ball H.L., Bradon N., Bosque P.J., et al. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J. Mol. Biol. 314:2001;1209-1225.
29. Gherardi E., Gonzalez Manzano R., Cottage A., Hawker K., Aparicio S. Evolution of plasminogen-related growth factors (HGF/SF and HGF1/MSP). Ciba Found. Symp. 212:1997;24-35.
30. Castellino F.J., McCance S.G. The kringle domains of human plasminogen. Ciba Found. Symp. 212:1997;46-60.
31. Gherardi E., Hartmann G., Hepple J., Chirgadze D., Srinivasan N., Blundell T. Domain structure of hepatocyte growth factor/scatter factor (HGF/SF). Ciba Found. Symp. 212:1997;84-93.
32. Soff G.A. Angiostatin and angiostatin-related proteins. Cancer Metastasis Rev. 19:2000;97-107.
33. 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.
34. 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.
35. Cohen F.E., Prusiner S.B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67:1998;793-819.
36. McKinley M.P., Bolton D.C., Prusiner S.B. A protease-resistant protein is a structural component of the scrapie prion. Cell. 35:1983;57-62.
37. Freifelder D. Physical Biochemistry: Applications to Biochemistry and Molecular Biology. 2nd edit. 1982;W.H. Freeman, San Francisco, CA.
38. Tsirka S.E., Rogove A.D., Bugge T.H., Degen J.L., Strickland S. An extracellular proteolytic cascade promotes neuronal degeneration in the mouse hippocampus. J. Neurosci. 17:1997;543-552.
39. Davies B.J., Pickard B.S., Steel M., Morris R.G., Lathe R. Serine proteases in rodent hippocampus. J. Biol. Chem. 273:1998;23004-23011.
40. Matsumoto K., Nakamura T. Emerging multipotent aspects of hepatocyte growth factor. J. Biochem. (Tokyo). 119:1996;591-600.
41. Moriyama T., Kataoka H., Koono M., Wakisaka S. Expression of hepatocyte growth factor/scatter factor and its receptor c-Met in brain tumors: evidence for a role in progression of astrocytic tumors (Review). Int. J. Mol. Med. 3:1999;531-536.
42. Harr S.D., Uint L., Hollister R., Hyman B.T., Mendez A.J. Brain expression of apolipoproteins E, J, and A-I in Alzheimer's disease. J. Neurochem. 66:1996;2429-2435.
43. Mockel B., Zinke H., Flach R., Weiss B., Weiler-Guttler H., Gassen H.G. Expression of apolipoprotein A-I in porcine brain endothelium in vitro. J. Neurochem. 62:1994;788-798.
44. Weinstein J.R., Gold S.J., Cunningham D.D., Gall C.M. Cellular localization of thrombin receptor mRNA in rat brain: expression by mesencephalic dopaminergic neurons and codistribution with prothrombin mRNA. J. Neurosci. 15:1995;2906-2919.
45. Dihanich M., Kaser M., Reinhard E., Cunningham D., Monard D. Prothrombin mRNA is expressed by cells of the nervous system. Neuron. 6:1991;575-581.
46. Yasuhara O., Walker D.G., McGeer P.L. Hageman factor and its binding sites are present in senile plaques of Alzheimer's disease. Brain Res. 654:1994;234-240.
47. Plow E.F., Herren T., Redlitz A., Miles L.A., Hoover-Plow J.L. The cell biology of the plasminogen system. FASEB J. 9:1995;939-945.
48. Lijnen H.R. Elements of the fibrinolytic system. Ann. N.Y. Acad. Sci. 936:2001;226-236.
49. Schwab W., Gavlik J.M., Beichler T., Funk R.H., Albrecht S., Magdolen V., et al. Expression of the urokinase-type plasminogen activator receptor in human articular chondrocytes: association with caveolin and beta 1-integrin. HIstochem. Cell. Biol. 115:2001;317-323.
50. Stahl A., Mueller B.M. The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J. Cell Biol. 129:1995;335-344.
51. Liu J., Razani B., Tang S., Terman B.I., Ware J.A., Lisanti M.P. Angiogenesis activators and inhibitors differentially regulate caveolin-1 expression and caveolae formation in vascular endothelial cells. Angiogenesis inhibitors block vascular endothelial growth factor-induced down-regulation of caveolin-1. J. Biol. Chem. 274:1999;15781-15785.
52. Ledesma M.D., Da Silva J.S., Crassaerts K., Delacourte A., De Strooper B., Dotti C.G. Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains. EMBO Rep. 1:2000;530-535.
53. Westaway D., Cooper C., Turner S., Da Costa M., Carlson G.A., Prusiner S.B. Structure and polymorphism of the mouse prion protein gene. Proc. Natl Acad. Sci. USA. 91:1994;6418-6422.
54. Baskakov I.V., Aagaard C., Mehlhorn I., Wille H., Groth D., Baldwin M.A., et al. Self-assembly of recombinant prion protein of 106 residues. Biochemistry. 39:2000;2792-2804.
55. Mehlhorn I., Groth D., Stöckel J., Moffat B., Reilly D., Yansura D., et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry. 35:1996;5528-5537.
56. Baskakov I.V., Legname G., Prusiner S.B., Cohen F.E. Folding of prion protein to its native α-helical conformation is under kinetic control. J. Biol. Chem. 276:2001;19687-19690.
57. Harlow E., Lane D. Antibodies: A Laboratory Manual. 1988;Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
58. Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Schmitt-Ulms G., et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature. 412:2001;739-743.
59. Dahlquist F.W. The meaning of Scatchard and Hill plots. Methods Enzymol. 48:1978;270-299.