The structure function relationship for the Prion protein

Journal of Alzheimer's Disease

Volumn 6, Issue 3, 2004, Pages 283-289

  Deignan, Marguerite E ^a   Prior, Marguerite ^a   Stuart, Lorraine E ^a   Comerford, Emma J ^a   McMahon, Hilary E M ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Amino terminus; Carboxyl terminus; Copper; Glycosylation; Prion

Indexed keywords

BINDING PROTEIN; PRION PROTEIN; PROLYLHISTIDYLGLYCYLGLYCYLGLYCYLTRYPTOPHYLGLYCYLGLUTAMATE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; METAL BINDING; PRION DISEASE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 3042629535     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2004-6309     Document Type: Review

References (68)

1. B.S. Berlett and E.R. Stadtman, Protein oxidation in aging, disease, and oxidative stress, J. Biol. Chem. 272 (1997), 20313-20316.
2. C.J. Bosques and B. Imperiali, The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment, Proc. Natl. Acad. Sci. USA 100 (2003), 7593-7598.
3. D.R. Brown, C. Clive and S.J. Haswell, Antioxidant activity related to copper binding of native prion protein, J. Neurochem. 76 (2001), 69-76.
4. D.R. Brown, F. Hafiz, L.L. Glasssmith, B.S. Wong, I.M. Jones, C. Clive and S.J. Haswell, Consequences of manganese replacement of copper for prion protein function and proteinase resistance, EMBO J 19 (2000), 1180-1186.
5. D.R. Brown, K. Qin, J.W. Herms, A. Madlung, J. Manson, R. Strome, P.E. Fraser, T. Kruck, A. von Bohlen, W. Schulz-Schaeffer, A. Giese, D. Westaway and H. Kretzschmar, The cellular prion protein binds copper in vivo, Nature 390 (1997), 684-687.
6. H. Bueler, A. Aguzzi, A. Sailer, R.A. Greiner, P. Autenried, M. Aguet and C. Weissmann, Mice devoid of PrP are resistant to scrapie, Cell 73 (1993), 1339-1347.
7. P.Y. Chen, C.C. Lin, Y.T. Chang, S.C. Lin and S.I. Chan, One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide, Proc. Natl. Acad. Sci. USA 99 (2002), 12633-12638.
8. S.G. Chen, D.B. Teplow, P. Parchi, J.K. Teller, P. Gambetti and L. Autilio-Gambetti, Truncated forms of the human prion protein in normal brain and in prion diseases, J. Biol. Chem. 270 (1995), 19173-19180.
9. J. Collinge, K.C. Sidle, J. Meads, J. Ironside and A.F. Hill, Molecular analysis of prion strain variation and the aetiology of new variant CJD, Nature 383 (1996), 685-690.
10. N.R. Deleault, R.W. Lucassen and S. Supattapone, RNA molecules stimulate prion protein conversion, Nature 425 (2003), 717-720.
11. V. Ellis, M. Daniels, R. Misra and D.R. Brown, Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner, Biochemistry 41 (2002), 6891-6896.
12. A.P. Garnett and J.H. Viles, Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism, J. Biol. Chem. 278 (2003), 6795-6802.
13. S. Gauczynski, J.M. Peyrin, S. Haik, C. Leucht, C. Hundt, R. Rieger, S. Krasemann, J.P. Deslys, D. Dormont, C.I. Lasmezas and S. Weiss, The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein, EMBO J 20 (2001), 5863-5875.
14. E. Graner, A.F. Mercadante, S.M. Zanata, O.V. Forlenza, A.L. Cabral, S.S. Veiga, M.A. Juliano, R. Roesler, R. Walz, A. Minetti, I. Izquierdo, V.R. Martins and R.R. Brentani, Cellular prion protein binds laminin and mediates neuritogenesis, Brain Res. Mol. Brain Res. 76 (2000), 85-92.
15. R.S. Hegde, J.A. Mastrianni, M.R. Scott, K.A. DeFea, P. Tremblay, M. Torchia, S.J. DeArmond, S.B. Prusiner and V.R. Lingappa, A transmembrane form of the prion protein in neurodegenerative disease, Science 279 (1998), 827-834.
16. A.F. Hill, M. Antoniou and J. Collinge, Protease-resistant prion protein produced in vitro lacks detectable infectivity, J. Gen. Virol. 80(Pt 1) (1999), 11-14.
17. G. Hutter, F.L. Heppner and A. Aguzzi, No superoxide dismutase activity of cellular prion protein in vivo, Biol. Chem. 384 (2003), 1279-1285.
18. G.S. Jackson, L.L. Hosszu, A. Power, A.F. Hill, J. Kenney, H. Saibil, C.J. Craven, J.P. Waltho, A.R. Clarke and J. Collinge, Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations, Science 283 (1999), 1935-1937.
19. G.S. Jackson, I. Murray, L.L. Hosszu, N. Gibbs, J.P. Waltho, A.R. Clarke and J. Collinge, Location and properties of metal-binding sites on the human prion protein, Proc. Natl. Acad. Sci. USA 98 (2001), 8531-8535.
20. M.F. Jobling, X. Huang, L.R. Stewart, K.J. Barnham, C. Curtain, I. Volitakis, M. Perugini, A.R. White, R.A. Cherny, C.L. Masters, C.J. Barrow, S.J. Collins, A.I. Bush and R. Cappai, Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126, Biochemistry 40 (2001), 8073-8084.
21. K. Kaneko, M. Vey, M. Scott, S. Pilkuhn, F.E. Cohen and S.B. Prusiner, 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.
22. K. Kaneko, L. Zulianello, M. Scott, C.M. Cooper, A.C. Wallace, T.L. James, F.E. Cohen and S.B. Prusiner, 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.
23. D.A. Kocisko, J.H. Come, S.A. Priola, B. Chesebro, G.J. Raymond, P.T. Lansbury and B. Caughey, Cell-free formation of protease-resistant prion protein, Nature 370 (1994), 471-474.
24. M.L. Kramer, H.D. Kratzin, B. Schmidt, A. Romer, O. Windl, S. Liemann, S. Hornemann and H. Kretzschmar, Prion protein binds copper within the physiological concentration range, J. Biol. Chem. 276 (2001), 16711-16719.
25. C.I. Lasmezas, J.P. Deslys, O. Robain, A. Jaegly, V. Beringue, J.M. Peyrin, J.G. Fournier, J.J. Hauw, J. Rossier and D. Dormont, Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein, Science 275 (1997), 402-405.
26. S. Lee and D. Eisenberg, Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process, Nat. Struct. Biol. 10 (2003), 725-730.
27. S. Lee and D. Eisenberg, Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process, Nat. Struct. Biol. 10 (2003), 25-730.
28. S. Lehmann and D.A. Harris, Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells, J. Biol. Chem. 272 (1997), 21479-21487.
29. T. Liu, R. Li, T. Pan, D. Liu, R.B. Petersen, B.S. Wong, P. Gambetti and M.S. Sy, Intercellular transfer of the cellular prion protein, J. Biol. Chem. 277 (2002), 47671-47678.
30. Sc-like conformation in living cells, Nat. Cell Biol. 1 (1999), 358-361.
31. Sc-like conformation in the cytosol, Science 298 (2002), 1785-1788.
32. N. Madore, K.L. Smith, C.H. Graham, A. Jen, K. Brady, S. Hall and R. Morris, Functionally different GPI proteins are organized in different domains on the neuronal surface, EMBO J 18 (1999), 6917-6926.
33. M.J. McConville and M.A. Ferguson, The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes, Biochem. J. 294(Pt 2) (1993), 305-324.
34. D. McKenzie, J. Bartz, J. Mirwald, D. Olander, R. Marsh and J. Aiken, Reversibility of scrapie inactivation is enhanced by copper, J. Biol. Chem. 273 (1998), 25545-25547.
35. H.E. McMahon, A. Mange, N. Nishida, C. Creminon, D. Casanova and S. Lehmann, Cleavage of the amino terminus of the prion protein by reactive oxygen species, J. Biol. Chem. 276 (2001), 2286-2291.
36. O. Milhavet, H.E. McMahon, W. Rachidi, N. Nishida, S. Katamine, A. Mange, M. Arlotto, D. Casanova, J. Riondel, A. Favier and S. Lehmann, Prion infection impairs the cellular response to oxidative stress, Proc. Natl. Acad. Sci. USA 97 (2000), 13937-13942.
37. T. Miura, A. Hori-i, H. Mototani and H. Takeuchi, Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence, Biochemistry 38 (1999), 11560-11569.
38. S. Mouillet-Richard, M. Ermonval, C. Chebassier, J.L. Laplanche, S. Lehmann, J.M. Launay and O. Kellermann, Signal transduction through prion protein, Science 289 (2000), 1925-1928.
39. M. Nunziante, S. Gilch and H.M. Schatzl, Essential role of the prion protein N terminus in subcellular trafficking and half-life of cellular prion protein, J. Biol. Chem. 278 (2003), 3726-3734.
40. B. Oesch, D. Westaway, M. Walchli, M.P. McKinley, S.B. Kent, R. Aebersold, R.A. Barry, P. Tempst, D.B. Teplow and L.E. Hood, A cellular gene encodes scrapie PrP 27-30 protein, Cell 40 (1985), 735-746.
41. T. Pan, R. Li, B.S. Wong, T. Liu, P. Gambetti and M.S. Sy, Heterogeneity of normal prion protein in two-dimensional immunoblot: presence of various glycosylated and truncated forms, J. Neurochem. 81 (2002), 1092-1101.
42. P.C. Pauly and D.A. Harris, Copper stimulates endocytosis of the prion protein, J. Biol. Chem. 273 (1998), 33107-33110.
43. V. Perrier, A.C. Wallace, K. Kaneko, J. Safar, S.B. Prusiner and F.E. Cohen, Mimicking dominant negative inhibition of prion replication through structure-based drug design, Proc. Natl. Acad. Sci. USA 97 (2000), 6073-6078.
44. M. Pocchiari, Prions and related neurological diseases, Mol. Aspects Med. 15 (1994), 195-291.
45. S.B. Prusiner, Prions, Proc. Natl. Acad. Sci. USA 95 (1998), 13363-13383.
46. S.B. Prusiner, M.R. Scott, S.J. DeArmond and F.E. Cohen, Prion protein biology, Cell 93 (1998), 337-348.
47. E. Quaglio, R. Chiesa and D.A. Harris, Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform, J. Biol. Chem. 276 (2001), 11432-11438.
48. W. Rachidi, D. Vilette, P. Guiraud, M. Arlotto, J. Riondel, H. Laude, S. Lehmann and A. Favier, Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery, J. Biol. Chem. 278 (2003), 9064-9072.
49. J.R. Requena, D. Groth, G. Legname, E.R. Stadtman, S.B. Prusiner and R.L. Levine, Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein, Proc. Natl. Acad. Sci. USA 98 (2001), 7170-7175.
50. H. Sauer, K. Wefer, V. Vetrugno, M. Pocchiari, C. Gissel, A. Sachinidis, J. Hescheler and M. Wartenberg, Regulation of intrinsic prion protein by growth factors and TNF-alpha: the role of intracellular reactive oxygen species, Free Radic. Biol. Med. 35 (2003), 586-594.
51. Y. Shaked, H. Rosenmann, N. Hijazi, M. Halimi and R. Gabizon, Copper binding to the PrP isoforms: a putative marker of their conformation and function, J. Virol. 75 (2001), 7872-7874.
52. D. Shmerling, I. Hegyi, M. Fischer, T. Blattler, S. Brandner, J. Gotz, T. Rulicke, E. Flechsig, A. Cozzio, C. von Mering, C. Hangartner, A. Aguzzi and C. Weissmann, Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions, Cell 93 (1998), 203-214.
53. S.L. Shyng, M.T. Huber and D.A. Harris, A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells, J. Biol. Chem. 268 (1993), 15922-15928.
54. E.M. Sigurdsson, D.R. Brown, M.A. Alim, H. Scholtzova, R. Carp, H.C. Meeker, F. Prelli, B. Frangione and T. Wisniewski, Copper chelation delays the onset of prion disease, J. Biol. Chem. 278 (2003), 46199-46202.
55. N. Stahl, M.A. Baldwin, R. Hecker, K.M. Pan, A.L. Burlingame and S.B. Prusiner, Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid, Biochemistry 31 (1992), 5043-5053.
56. R.S. Stewart and D.A. Harris, Mutational analysis of topological determinants in PrP, and measurement of transmembrane and cytosolic PrP during prion infection, J. Biol. Chem. 278 (2003), 45960-45968.
57. J. Stockel, J. Safar, A.C. Wallace, F.E. Cohen and S.B. Prusiner, Prion protein selectively binds copper(II) ions, Biochemistry 37 (1998), 7185-7193.
58. B. Vincent, E. Paitel, P. Saftig, Y. Frobert, D. Hartmann, B. De Strooper, J. Grassi, E. Lopez-Perez and F. Checler, The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein, J. Biol. Chem. 276 (2001), 37743-37746.
59. J.D. Wadsworth, A.F. Hill, S. Joiner, G.S. Jackson, A.R. Clarke and J. Collinge, Strain-specific prion-protein conformation determined by metal ions, Nat. Cell Biol. 1 (1999), 55-59.
60. D.J. Waggoner, B. Drisaldi, T.B. Bartnikas, R.L. Casareno, J.R. Prohaska, J.D. Gitlin and D.A. Harris, Brain copper content and cuproenzyme activity do not vary with prion protein expression level, J. Biol. Chem. 275 (2000), 7455-7458.
61. A.R. Walmsley, F. Zeng and N.M. Hooper, Membrane topology influences N-glycosylation of the prion protein, EMBO J 20 (2001), 703-712.
62. A.R. Walmsley, F. Zeng and N.M. Hooper, The N-terminal region of the prion protein ectodomain contains a lipid raft targeting determinant, J. Biol. Chem. 278 (2003), 37241-37248.
63. E. Welker, L.D. Raymond, H.A. Scheraga and B. Caughey, Intramolecular versus intermolecular disulfide bonds in prion proteins, J. Biol. Chem. 277 (2002), 33477-33481.
64. D. Westaway, S.J. DeArmond, J. Cayetano-Canlas, D. Groth, D. Foster, S.L. Yang, M. Torchia, G.A. Carlson and S.B. Prusiner, Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins, Cell 76 (1994), 117-129.
65. B.S. Wong, R. Li, J. Sassoon, S.C. Kang, T. Liu, T. Pan, N.S. Greenspan, T. Wisniewski, D.R. Brown and M.S. Sy, Mapping the antigenicity of copper-treated cellular prion protein with the scrapie isoform, Cell Mol. Life Sci. 60 (2003), 1224-1234.
66. C. Wong, L.W. Xiong, M. Horiuchi, L. Raymond, K. Wehrly, B. Chesebro and B. Caughey, Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein, EMBO J 20 (2001), 377-386.
67. R. Zahn, A. Liu, T. Luhrs, R. Riek, C. von Schroetter, G.F. Lopez, M. Billeter, L. Calzolai, G. Wider and K. Wuthrich, NMR solution structure of the human prion protein, Proc. Natl. Acad. Sci. USA 97 (2000), 145-150.
68. S.M. Zanata, M.H. Lopes, A.F. Mercadante, G.N. Hajj, L.B. Chiarini, R. Nomizo, A.R. Freitas, A.L. Cabral, K.S. Lee, M.A. Juliano, E. de Oliveira, S.G. Jachieri, A. Burlingame, L. Huang, R. Linden, R.R. Brentani and V.R. Martins, Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection, EMBO J 21 (2002), 3307-3316.