The molecular basis of amyloidosis

Cellular and Molecular Life Sciences

Volumn 53, Issue 11-12, 1997, Pages 871-887

  Serpell, L C ^a   Sunde, M ^a,b   Blake, C C F ^a,b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Alzheimer's disease; Amyloid; Amyloidosis; Cross conformation; Fibre diffraction; Fibrils; Protofilaments; Spongiform encephalopathies

Indexed keywords

AMYLOID; PRION PROTEIN;

ALZHEIMER DISEASE; AMYLOIDOSIS; BOVINE SPONGIFORM ENCEPHALOPATHY; FIBER; HUMAN; HYDROGEN BOND; KURU; METABOLIC DISORDER; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; PRION DISEASE; PROTEIN METABOLISM; PROTEIN SECONDARY STRUCTURE; REVIEW;

BOVINAE;

EID: 0031435479     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050107     Document Type: Review

References (73)

1. Cohen A. S. and Calkins E. (1959) Electron microscopic observation on a fibrous component in amyloid of diverse origins. Nature 183: 1202-1203
2. Shirahama T. and Cohen A. S. (1967) High resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol. 33: 679-706
3. Cohen A. S., Shirahama T. and Skinner M. (1981) Electron microscopy of amyloid. In: Electron Microscopy of Protein. vol. 3. pp. 165-205, Harriss, I. (ed.), Academic Press, London
4. Kirschner D. A., Abraham C. and Selkoe D. A. (1986) X-ray diffraction from intraneuronal paired helical filaments and extra-neuronal amyloid fibres in Alzheimer's disease indicates cross-β conformation. Proc. Natl. Acad. Sci. USA 83: 503-507
5. Gilchrist P. and Bradshaw J. (1993) Amyloid formation by salmon calcitonin. Biochim. Biophys. Acta 1182: 111-114
6. Nguyen J. T., Inouye H., Baldwin M. A., Fletterick R., Cohen F. E., Prusiner S. B. et al. (1995) X-ray diffraction from scrapie prion rod and PrP peptides. J. Mol. Biol. 252: 412-422
7. Fraser P. E., Nguyen J. T., Surewicz W. K. and Kirschner D. A. (1991) pH dependent structural transitions of Alzheimers amyloid peptides. Biophys. J. 60: 1190-1201
8. Serpell L. C., Sunde M., Fraser P. E., Luther P. K., Morris E., Sandgren O. et al. (1995) The examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254: 113-118
9. Astbury W. T., Dickinson S. and Bailey K. (1935) The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem. J. 29: 2351-2360
10. Pauling L. and Corey R. (1951) Configuration of polypeptide chains with favoured orientation around single bonds: two new pleated sheets. Proc. Natl. Acad. Sci. USA 37: 729-739
11. Geddes A. J., Parker K. D., Atkins E. D. T. and Beighton E. (1968) "Cross β" conformation in protein. J. Mol. Biol. 32: 343-358
12. Blake C. C. F., Kornig D. F., Mair G. A., North A. C. T., Phillips D. C. and Sarma V. R. (1965) Structure of hen egg-white lysozyme. A three dimensional Fourier synthesis at 2 Å resolution. Nature 206: 757-761
13. Reeke G. N., Hartsuck J. A., Ludwig M. L., Quiocho F. A., Steitz T. A. and Lipscomb W. N. (1967) The structure of carboxypeptidase A, VI. Some results at 2.0 Å resolution and the complex with glycyl-tyrosine at 2.8 Å resolution. Proc. Natl. Acad. Sci. USA 58: 2220-2226
14. Chothia C. (1973) Conformations of twisted β-sheets in proteins. J. Mol. Biol. 75: 295-302
15. Burge R. E. (1959) X-ray scattering by bundles of cylinders. Acta Crystallogr. 12: 285-289
16. Burge R. E. (1963) Equatorial X-ray diffraction by fibrous proteins: short range order in collagen, feather keratin and f-actin. J. Mol. Biol. 7: 213-224
17. Eanes E. D. and Glenner G. G. (1968) X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16: 673-677
18. Bonar L., Cohen A. S. and Skinner M. (1967). Characterization of the amyloid fibril as a cross-β protein. Proc. Soc. Exp. Biol. Med. 131: 1373-1375
19. Glenner G. G., Eanes E. D. and Page D. L. (1972) The relation of the properties of congo red-stained amyloid fibrils to the β-conformation. J. Histochem. Cytochem. 20: 821-826
20. Burke M. J. and Rougvie M. A. (1972) Cross-β protein structures I. Insulin Fibrils. Biochemistry 11: 2435-2439
21. Kirschner D. A., Inouye H., Duffy L., Sinclair A., Lind M. and Selkoe D. A. (1987) Synthetic peptide homologous to β-protein from Alzheimer's disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA 84: 6953-6957
22. Blake C. C. F., Serpell L. C., Sunde M. and Lundgren E. (1996). A molecular model of the amyloid fibril. In: CIBA Symposium No. 199, The Nature and Origin of Amyloid Fibrils. pp. 6-21, Bock G. R. and Goode J. A. (eds), John Wiley and Sons Ltd, Chichester
23. Blake C. C. F. and Serpell L. C. (1996) Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4: 989-998
24. Blake C. C. F., Geisow M. J., Oatley S. J., Rerat B. and Rerat C. (1978). Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at I.8 A. J. Mol. Biol. 121: 339-356
25. Richardson J. (1981) The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34: 167-339
26. Saraiva M. J. M. (1995) Transthyretin mutations in health and disease. Hum. Mutation 5: 191-196
27. Vidal R., Garzuly F., Budka H., Lalowski M., Linke R. P., Frangione B. et al. (1996) Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon-18. Am. J. Pathol. 148: 361-366
28. Terry C. J., Damas A. M., Oliviera P., Saraiva M. J. M., Alves A. L., Costa P. P. et al. (1993) Structure of Met30 variant of transthyretin and its amyloidogenic variations. EMBO J. 12: 735-741
29. Hamilton J., Steinrauf L., Braden B., Liepnieks J., Benson M., Holmgren G. et al. (1993) The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7 Å resolution. J. Biol. Chem. 268: 2416-2424
30. Steinrauf L. K., Hamilton J. A., Braden B. C., Murrell J. R. and Benson M. D. (1993) X-ray crystal structure of the Ala109Thr variant of human transthyretin which produces euthyroid hyperthyroxinemia. J. Biol. Chem. 268: 2425-2430
31. Saraiva M. J. M., Almeida M. R., Alves I. L., Bonifacio M. J., Damas A. M., Palha J. A. et al. (1996) Modulating conformational factors in transthyretin amyloid. In: CIBA Symposium No. 199. The Nature and Origin of Amyloid Fibrils, pp. 6-21, Bock G. R. and Goode J. A. (eds), John Wiley and Sons Ltd. Chichester
32. Thylen C., Wahlchrist J., Haetner E., Sandgren O., Holmgren G. and Lundgren E. (1993) Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation. EMBO J. 12: 743-748
33. McCutchen S. and Kelly J. W. (1993) Intermolecular disulphide linkages are not required for transthyretin amyloid fibril formation in vitro Biochem. Biophys. Res. Commun. 197: 415-421
34. Damas A. M. Ribeiro S., Lamzin V. S., Palha J. A. and Saraiva M. J. (1996) Structure of Val1221le variant transthyretin a cardiomyopathic mutant. Acta Crystallogr. D 52: 966-972
35. Serpell L. C. and Blake C. C. F. (1994). In: Amyloid and Amyloidosis, pp. 447-450, Kisilevsky, R., Benson, M. D., Frangione, B., Gauldie, J., Muckle, T. J. and Youngs, I. D. (eds), Parthenon Publishing Group Inc., New York
36. Serpell L. C., Goldsteins G., Dacklin I., Lundgren E. and Blake C. C. F. (1996) The 'edge strand' hypothesis: prediction and test of a mutational 'hot-spot' on the transthyretin molecule associated with FAP amyloidogenesis. Amyloid: Int. J. Exp. Clin. Invest. 3: 75-85
37. Kelly J, W. and Lansbury P. T. (1994) A chemical approach to elucidate the mechanism of transthryretin and β-protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest. 1: 186-205
38. Kelly J. W. (1996) Alternative conformations of amyloidogenic proteins govern their behaviour. Curr. Opin. Struct. Biol. 6: 11-17
39. Rosen H. N., Moses A. C., Murrell J. R., Liepnieks J. J. and Benson M. D. (1993) Thyroxine interactions with transthyretin a comparison of 10 different naturally occurring human transthyretin variants. J. Clin. Endocrinol. Metabol. 77: 370-374
40. Colon W. and Kelly J. W. (1992) Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31: 8654-8660
41. Pepys M. B., Hawkins P. N., Booth D. R., Vigushin D. M., Tennet G. A., Soutar A. K. et al. (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362: 553-557
42. Artymiuk P. J. and Blake C. C. F. (1981) Refinement of human lysozyme at 1.5 Å resolution: analysis of non-bonded and hydrogen-bond interactions. J. Mol. Biol. 152: 737-762
43. 1H NMR Studies of human lysozyme: spectral assignment and comparison with hen lysozyme. Biochemistry 29: 7201-7214
44. Radford S. E., Dobson C. M. and Evans P. A. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358: 302-307
45. Hooke S. D., Radford S. E. and Dobson C. M. (1994) The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme. Biochemistry 33: 5867-5876
46. Booth D. R., Sunde M., Bellotti V., Robinson C. V., Hutchinson, W. L., Fraser P. E. et al. (1997) Instability, unfolding and fibrillogenesis in amyloidogenic lysozyme variants. Nature 385: 787-793
47. Adams M. J., Blundell T. L., Dodson E. J., Dodson G. G., Vijayan M., Baker E. N. et al. (1969) The structure of rhombohedral 2 zinc insulin crystals. Nature 224: 491-495
48. Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A. et al. (1988) The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7: 2593-2599
49. Burtnick L. D., Robinson R. C. and Koepf E. K. (1996) The structure of horse plasma gelsolin to 2.5 Å. Biophys. J. 70: Pt. 2, pSUA12
50. Rick R., Hornemann S., Wider G., Billeter M., Glockshuber R. and Wüthrich K. (1996) NMR structure of the mouse prion protein domain PrP(121-231). Nature 382: 180 182
51. Nolte R. T. and Atkinson D. (1992) Conformational analysis of apolipoprotein A-1 and E-3 based on primary sequence and circular dichroism. Biophys. J. 63: 1221-1239
52. Poljak R. J., Amzel L. M., Avey H. P., Chen B. L., Phizackerlcy R. P. and Saul F. (1973) The three-dimensional structure of a Fab fragment of a human immunoglobulin at 2.8 Å resolution. Proc. Natl. Acad. Sci. USA 70: 3 305-331
53. 2-microglobulin. Proc. Natl. Acad. Sci. USA 82:4225-4229
54. Hilbich C., Kisters-Woike B., Reed J., Masters C. and Beyreuther K. (1991) Aggregation and secondary structure of synthetic amyloid βΛ4 peptides of Alzheimer's disease. J. Mol. Biol. 218: 149-163
55. Sticht H. P., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K. et al. (1995) Structure of amyloid A4(1-40)-pep tide of Alzheimer's disease. Eur. J. Biochem. 233: 293-298
56. Soto C., Castano E., Frangione B. and Inestrosa N. (1995) The α-helical to β-sheet transition in the amino-terminal tragment of the amyloid β-peptide modulates amyloid formation. J. Biol. Chem. 270: 3063-3067
57. Kirshenbaum K. and Daggett V. (1995) pH-Dependent conformations of the amyloid β(1-28) peptide fragment explored using molecular dynamics. Biochemistry 34: 7629-7639
58. Kirshenbaum K. and Daggett V. (1995) Sequence effects on the conformational properties of the amyloid β(1-28) peptide: testing a proposed mechanism for the α→β transition. Biochemistry 34: 7640-7647
59. Barrow C. J., Yasuda A., Kenny P. T. M. and Zagorski M. G. (1992). Solution conformations and aggregational properties of synthetic amyloid β- peptides of Alzheimer's disease. J. Mol. Biol. 225: 1075-1093
60. Terzi E., Holzemann G. and Seelig J. (1994) Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35). Biochemistry 33: 1345-1350
61. Pan K.-M., Baldwin M. A., Nguyen J. T., Gaseet M. Serban A., Groth D. et al. (1993) Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90: 10962-10966
62. Huang Z., Gabriel J.-M., Baldwin M. A., Fletterick R. J., Prusiner S. B. and Cohen F. E. (1994) Proposed 3-dimensional structure for the cellular prion protein. Proc. Natl. Acad. Sci. USA 91: 7139-7143
63. Gasset M., Baldwin M. A., Lloyd D. H., Gabriel J.-M., Hollzman D. M., Cohen F. E. et al. (1992) Predicted α-helieal regions of the prion protein, when synthesized as peptides form amyloid. Proc. Natl. Acad. Sci. USA 89: 10940-10944
64. Gasset M., Baldwin M., Fletterick R. and Prusiner S. (1993) Perturbation of secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. USA 90: 1-5
65. Cohen F. E., Pan K.-M., Huang Z., Baldwin M., Fletterick R. and Prusiner, S. B. (1994) Structural clues to prion replication. Science 264: 530-531
66. Safar J., Roller P., Gajdusek D. and Gibbs C. (1994) Scrapie amyloid (prion) has the conformational characteristics of an aggregated molten globular folding intermediate. Biochemistry 33: 8375-8383
67. McCutchen S., Colon W. and Kelly J. W. (1993) Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32: 12119-12127
68. McCutchen S. L., Lai Z., Miroy G. J., Kelly J. W. and Colon W. (1995) Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34: 13527-13536
69. Prusiner S. B. (1996) Molecular biology and pathogenesis of prion diseases. Trends Biochem. Sci. 21: 482-487
70. Caughey B. and Chesebro B. (1997) Priori protein and the transmissible spongiform encephalopathies. Trends Cell Biol. 7: 56-62
71. Harrison P. M., Bamborough P., Daggett V., Prusiner S. B. and Cohen F. E. (1997) The prion folding problem. Curr. Opin. Struct. Biol. 7: 53-59
72. Telling G. C., Parchi P., DeArmond S. J., Cortelli P., Montagna P., Gabizon R. et al. (1996) Evidence for the conformation of the pathological isoform of the prion protein enciphering and propagating prion diversity. Science 274: 2079-2082
73. Kraulis, P. J. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950