Hemodialysis-Related Amyloidosis

Protein Misfolding Diseases: Current and Emerging Principles and Therapies

Volumn , Issue , 2010, Pages 347-379

  Smith, David P ^a   Ashcroft, Alison E ^a   Radford, Sheena E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Effective therapies against amyloid disease an immense challenge; Hemodialysis related amyloidosis; Hemodialysis related amyloidosis (HDRA), complication of long term hemodialysis and beta 2 microglobulin ( 2m), major components of amyloid fibrils

Indexed keywords

EID: 84878925603     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470572702.ch16     Document Type: Chapter

References (130)

1. Gejyo, F., Yamada, T., Odani, S., Nakagawa, Y., Arakawa, M., Kunitomo, T., Kataoka, H., Suzuki, M., Hirasawa, Y., Shirahama, T., et al. (1985). A new form of amyloid protein associated with chronic-hemodialysis was identified as beta 2-microglobulin. Biochem Biophys Res Commun, 129, 701-706.
2. Floege, J. Ketteler, M. (2001). Beta 2-microglobulin-derived amyloidosis: an update. Kidney Int, 59, 164-171.
3. Khan, A.R., Baker, B.M., Ghosh, P., Biddison, W.E., Wiley, D.C. ( 2000). The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site. J Immunol, 164, 6398-6405.
4. Trinh, C.H., Smith, D.P., Kalverda, A.P., Phillips, S.E., Radford, S.E. (2002). Crystal structure of monomeric human beta 2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci U S A, 99, 9771-9776.
5. Verdone, G., Corazza, A., Viglino, P., Pettirossi, F., Giorgetti, S., Mangione, P., Andreola, A., Stoppini, M., Bellotti, V., Esposito, G. (2002). The solution structure of human beta 2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci, 11, 487-499.
6. Iwata, K., Matsuura, T., Sakurai, K., Nakagawa, A., Goto, Y. (2007). Highresolution crystal structure of beta 2-microglobulin formed at pH 7.0. J Biochem, 142, 413-419.
7. Rosano, C., Zuccotti, S., Mangione, P., Giorgetti, S., Bellotti, V., Pettirossi, F., Corazza, A., Viglino, P., Esposito, G., Bolognesi, M. (2004). Beta 2-microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation. J Mol Biol, 335, 1051-1064.
8. Floege, J., Bartsch, A., Schulze, M., Shaldon, S., Koch, K.M., Smeby, L.C. (1991). Clearance and synthesis rates of beta 2-microglobulin in patients undergoing hemodialysis and in normal subjects. J Lab Clin Med, 118, 153-165.
9. Karlsson, F.A., Groth, T., Sege, K., Wibell, L., Peterson, P.A. (1980). Turnover in humans of beta 2-microglobulin: the constant chain of HLA-antigens. Eur J Clin Invest, 10, 293-300.
10. Vincent, C., Chanard, J., Caudwell, V., Lavaud, S., Wong, T., Revillard, J.P. (1992). Kinetics of I125 beta 2-microglobulin turnover in dialyzed patients. Kidney Int, 42, 1434-1443.
11. Drueke, T.B. (2000). Beta 2-microglobulin and amyloidosis. Nephrol Dial Transplant, 15 (Suppl 1), 17-24.
12. Gejyo, F., Homma, N., Suzuki, Y., Arakawa, M. (1986). Serum levels of beta 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis. N Engl J Med, 314, 585-586.
13. Relini, A., Canale, C., De Stefano, S., Rolandi, R., Giorgetti, S., Stoppini, M., Rossi, A., Fogolari, F., Corazza, A., Esposito, G., et al. (2006). Collagen plays an active role in the aggregation of beta 2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J Biol Chem, 281, 16521-16529.
14. Stoppini, M., Mangione, P., Monti, M., Giorgetti, S., Marchese, L., Arcidiaco, P., Verga, L., Segagni, S., Pucci, P., Merlini, G., Bellotti, V. (2005). Proteomics of beta 2-microglobulin amyloid fibrils. Biochim Biophys Acta, 1753, 23-33.
15. Linke, R.P., Bommer, J., Ritz, E., Waldherr, R., Eulitz, M. (1986). Amyloid kidney stones of uremic patients consist of beta 2-microglobulin fragments. Biochem Biophys Res Commun, 136, 665-671.
16. Bellotti, V., Stoppini, M., Mangione, P., Sunde, M., Robinson, C., Asti, L., Brancaccio, D., Ferri, G. (1998). Beta 2-microglobulin can be refolded into a native state from ex-vivo amyloid fibrils. Eur J Biochem, 258, 61-67.
17. Nissen, M.H., Roepstorff, P., Thim, L., Dunbar, B., Fothergill, J.E. (1990). Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s. Eur J Biochem, 189, 423-429.
18. Giorgetti, S., Stoppini, M., Tennent, G.A., Relini, A., Marchese, L., Raimondi, S., Monti, M., Marini, S., Østergaard, O., Heegaard, N.H., et al. (2007). Lysine 58-cleaved beta2-microglobulin is not detectable by 2D electrophoresis in ex-vivo amyloid fibrils of two patients affected by dialysis-related amyloidosis. Protein Sci, 16, 343-349.
19. Heegaard, N.H., Jørgensen, T.J., Rozlosnik, N., Corlin, D.B., Pedersen, J.S., Tempesta, A.G., Roepstorff, P., Bauer, R., Nissen, M.H. (2005). Unfolding, aggregation, and seeded amyloid formation of lysine-58-cleaved beta 2-microglobulin. Biochemistry, 44, 4397-4407.
20. Kad, N.M., Thomson, N., Smith, D.P., Smith, D.A., Radford, S.E. (2001). Beta 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J Mol Biol, 313, 559-571.
21. Niwa, T., Katsuzaki, T., Miyazaki, S., Momoi, T., Akiba, T., Miyazaki, T., Nokura, K., Hayase, F., Tatemichi, N., Takei, Y. (1997). Amyloid beta 2-microglobulin is modified with imidazolone, a novel advanced glycation end product, in dialysis-related amyloidosis. Kidney Int, 51, 187-194.
22. Jadoul, M., Garbar, C., Noël, H., Sennesael, J., Vanholder, R., Bernaert, P., Rorive, G., Hanique, G., van Ypersele de Strihou, C. (1997). Histological prevalence of beta 2-microglobulin amyloidosis in hemodialysis: a prospective post-mortem study. Kidney Int, 51, 1928-1932.
23. Hou, F.F. Owan, W.F. (2002). Beta 2-microglobulin amyloidosis: role of monocytes / macrophages. Curr Opin Nephrology and Hypertension, 11, 417-421.
24. Pepys, M.B. (2006). Amyloidosis. Annu Rev Med, 57, 223-241.
25. Ono, K., Uchino, F. (1994). Formation of amyloid-like substance from beta 2-microglobulin in vitro. Nephron, 66, 404-407.
26. Yamamoto, S., Hasegawa, K., Yamaguchi, I., Goto, Y., Gejyo, F., Naiki, H. (2005). Kinetic analysis of the polymerization and depolymerization of beta 2-microglobulin-related amyloid fibrils in vitro. Biochim Biophys Acta, 1753, 34-43.
27. Mahley, R.W. (1988). Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science, 240, 622-630.
28. Motomiya, Y., Ando, Y., Haraoka, K., Sun, X., Iwamoto, H., Uchimura, T., Maruyama, I. (2003). Circulating level of alpha2-macroglobulin-beta 2-microglobulin complex in hemodialysis patients. Kidney Int, 64, 2244-2252.
29. McParland, V.J., Kad, N.M., Kalverda, A.P., Brown, A., Kirwin-Jones, P., Hunter, M.G., Sunde, M., Radford, S.E. (2000). Partially unfolded states of beta 2-microglobulin and amyloid formation in vitro. Biochemistry, 39, 8735-8746.
30. Athanasou, N.A., Puddle, B., Sallie, B. (1995). Highly sulphated glycosaminoglycans in articular cartilage and other tissues containing beta 2-microglobulin dialysis amyloid deposits. Nephrol Dial Transplant, 10, 1672-1678.
31. Inoue, S., Kuroiwa, M., Ohashi, K., Hara, M., Kisilevsky, R. (1997). Ultrastructural organization of hemodialysis-associated beta 2-microglobulin amyloid fibrils. Kidney Int, 52, 1543-1549.
32. Hou, F.F., Chertow, G.M., Kay, J., Boyce, J., Lazarus, J.M., Braatz, J.A., Owen, W.F., Jr. (1997). Interaction between beta 2-microglobulin and advanced glycation end products in the development of dialysis related amyloidosis. Kidney Int, 51, 1514-1519.
33. Bardin, T., Kuntz, D. (1987). The arthropathy of chronic haemodialysis. Clin Exp Rheumatol, 5, 379-386.
34. Myers, S.L., Jones, S., Jahn, T.R., Morten, I.J., Tennent, G.A., Hewitt, E.W., Radford, S.E. (2006). A systematic study of the effect of physiological factors on beta 2-microglobulin amyloid formation at neutral pH. Biochemistry, 45, 2311-2321.
35. Yamaguchi, I., Suda, H., Tsuzuike, N., Seto, K., Seki, M., Yamaguchi, Y., Hasegawa, K., Takahashi, N., Yamamoto, S., Gejyo, F., Naiki, H. (2003). Glycosaminoglycan and proteoglycan inhibit the depolymerization of beta 2-microglobulin amyloid fibrils in vitro. Kidney Int, 64, 1080-1088.
36. Borysik, A.J., Morten, I.J., Radford, S.E., Hewitt, E.W. (2007). Specific glycosaminoglycans promote unseeded amyloid formation from beta 2-microglobulin under physiological conditions. Kidney Int, 72, 174-181.
37. Jahn, T.R., Parker, M.J., Homans, S.W., Radford, S.E. (2006). Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol, 13, 195-201.
38. Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, S., Kardos, J., Goto, Y., Gejyo, F., Naiki, H. (2004). Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry, 43, 11075-11082.
39. Giorgetti, S., Rossi, A., Mangione, P., Raimondi, S., Marini, S., Stoppini, M., Corazza, A., Viglino, P., Esposito, G., Cetta, G., et al. (2005). Beta 2-microglobulin isoforms display an heterogeneous affinity for type I collagen. Protein Sci, 14, 696-702.
40. Homma, N., Gejyo, F., Isemura, M., Arakawa, M. (1989). Collagen-binding affinity of beta 2-microglobulin, a preprotein of hemodialysis-associated amyloidosis. Nephron, 53, 37-40.
41. Coggi, G., Dell'Orto, P., Braidotti, P., Coggi, A., Viale, G. (1989). Coexpression of intermediate filaments in normal and neoplastic human tissues: a reappraisal. Ultrastruct Pathol, 13, 501-514.
42. Yamaguchi, I., Hasegawa, K., Takahashi, N., Gejyo, F., Naiki, H. (2001). Apolipoprotein E inhibits the depolymerization of beta 2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry, 40, 8499-8507.
43. Naiki, H., Yamamoto, S., Hasegawa, K., Yamaguchi, I., Goto, Y., Gejyo, F. (2005). Molecular interactions in the formation and deposition of beta 2-microglobulinrelated amyloid fibrils. Amyloid, 12, 15-25.
44. Linke, R.P., Schäeffer, J., Gielow, P., Lindner, P., Lottspeich, F., Plückthun, A., Weiss, E.H. (2000). Production of recombinant human beta 2-microglobulin for scintigraphic diagnosis of amyloidosis in uremia and hemodialysis. Eur J Biochem, 267, 627-633.
45. Bellotti, V., Gallieni, M., Giorgetti, S., Brancaccio, D. (2001). Dynamic of beta 2-microglobulin fibril formation and reabsorption: the role of proteolysis. Semin Dial, 14, 117-122.
46. Ayers, D.C., Athanasou, N.A., Woods, C.G., Duthie, R.B. (1993). Dialysis arthropathy of the hip. Clin Orthop Relat Res, 216-224.
47. Ohashi, K., Hara, M., Kawai, R., Ogura, Y., Honda, K., Nihei, H., Mimura, N. (1992). Cervical disks are most susceptible to beta 2-microglobulin amyloid deposition in the vertebral column. Kidney Int, 41, 1646-1652.
48. Hou, F.F., Miyata, T., Boyce, J., Yuan, Q., Chertow, G.M., Kay, J., Schmidt, A.M., Owen, W.F. (2001). Beta 2-microglobulin modified with advanced glycation end products delays monocyte apoptosis. Kidney Int, 59, 990-1002.
49. Miyata, T., Hori, O., Zhang, J., Yan, S.D., Ferran, L., Iida, Y., Schmidt, A.M. (1996). The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-beta 2-microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway. Implications for the pathogenesis of dialysis-related amyloidosis. J Clin Invest, 98, 1088-1094.
50. Matsuo, K., Ikizler, T.A., Hoover, R.L., Nakamoto, M., Yasunaga, C., Pupim, L.B., Hakim, R.M. (2000). Transforming growth factor-beta is involved in the pathogenesis of dialysis-related amyloidosis. Kidney Int, 57, 697-708.
51. Miyata, T., Inagi, R., Iida, Y., Sato, M., Yamada, N., Oda, O., Maeda, K., Seo, H. (1994). Involvement of beta 2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis. Induction of human monocyte chemotaxis and macrophage secretion of tumor necrosis factoralpha and interleukin-1. J Clin Invest, 93, 521-528.
52. Ramadori, G., Rieder, H., Sipe, J., Shirahama, T., Meyerzum Büschenfelde, K.H. (1989). Murine tissue macrophages synthesize and secrete amyloid proteins different to amyloid-A (AA). Eur J Clin Invest, 19, 316-322.
53. Van Ypersele, C., Drucke, T.B.(1996). Dialysis Amyloid, Oxford University Press, New York, pp. 34-68.
54. Gosal, W.S., Morten, I.J., Hewitt, E.W., Smith, D.A., Thomson, N.H., Radford, S.E. (2005). Competing pathways determine fibril morphology in the self-assembly of beta 2-microglobulin into amyloid. J Mol Biol, 351, 850-864.
55. Morten, I.J., Gosal, W.S., Radford, S.E., Hewitt, E.W. (2007). Investigation into the role of macrophages in the formation and degradation of beta 2-microglobulin amyloid fibrils. J Biol Chem, 282, 29691-29700.
56. Gorevic, P.D., Casey, T.T., Stone, W.J., DiRaimondo, C.R., Prelli, F.C., Frangione, B. (1985). Beta 2-microglobulin is an amyloidogenic protein in man. J Clin Invest, 76, 2425-2429.
57. Naiki, H., Hashimoto, N., Suzuki, S., Kimura, H., Nakakuki, K., Gejyo, F. (1997). Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid:Int J Exp Clin Invest, 4, 223-232.
58. Ban, T., Hamada, D., Hasegawa, K., Naiki, H., Goto, Y. (2003). Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem, 278, 16462-16465.
59. Chiti, F., De Lorenzi, E., Grossi, S., Mangione, P., Giorgetti, S., Caccialanza, G., Dobson, C.M., Merlini, G., Ramponi, G., Bellotti, V. (2001). A partially structured species of beta 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J Biol Chem, 276, 46714-46721.
60. Ohhashi, Y., Kihara, M., Naiki, H., Goto, Y. (2005). Ultrasonication-induced amyloid fibril formation of beta 2-microglobulin. J Biol Chem, 280, 32843-32848.
61. Kihara, M., Chatani, E., Sakai, M., Hasegawa, K., Naiki, H., Goto, Y. (2005). Seeding-dependent maturation of beta 2-microglobulin amyloid fibrils at neutral pH. J Biol Chem, 280, 12012-12018.
62. Morgan, C.J., Gelfand, M., Atreya, C., Miranker, A.D. (2001). Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J Mol Biol, 309, 339-345.
63. Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., Naiki, H. (2004). Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. J Am Soc Nephrol, 15, 126-133.
64. Sasahara, K., Yagi, H., Naiki, H., Goto, Y. (2007). Heat-induced conversion of beta 2-microglobulin and hen egg-white lysozyme into amyloid fibrils. J Mol Biol, 372, 981-991.
65. Eakin, C.M., Berman, A.J., Miranker, A.D. (2006). A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol, 13, 202-208.
66. Esposito, G., Michelutti, R., Verdone, G., Viglino, P., Hernández, H., Robinson, C.V., Amoresano, A., Dal Piaz, F., Monti, M., Pucci, P., et al. (2000). Removal of the N-terminal hexapeptide from human beta 2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci, 9, 831-845.
67. Jones, S., Smith, D.P., Radford, S.E. (2003). Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH. J Mol Biol, 330, 935-941.
68. Gosal, W.S., Myers, S.L., Radford, S.E., Thomson, N.H. (2006). Amyloid under the atomic force microscope. Protein Pept Lett, 13, 261-270.
69. Kad, N.M., Myers, S.L., Smith, D.P., Smith, D.A., Radford, S.E., Thomson, N.H. (2003). Hierarchical assembly of beta 2-microglobulin amyloid in vitro revealed by atomic force microscopy. J Mol Biol, 330, 785-797.
70. Smith, D.P., Jones, S., Serpell, L.C., Sunde, M., Radford, S.E. (2003). A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J Mol Biol, 330, 943-954.
71. Fabian, H., Gast, K., Laue, M., Misselwitz, R., Uchanska-Ziegler, B., Ziegler, A., Naumann, D. (2008). Early stages of misfolding and association of beta 2-microglobulin: insights from infrared spectroscopy and dynamic light scattering. Biochemistry, 47, 6895-6906.
72. Naiki, H., Hashimoto, N., Suzuki, S., Kimura, H., Nakakuki, K., Gejyo, F. (1997). Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid Int J Exp Clin Invest, 4, 223-232.
73. Chatani, E., Kato, M., Kawai, T., Naiki, H., Goto, Y. (2005). Main-chain dominated amyloid structures demonstrated by the effect of high pressure. J Mol Biol, 352, 941-951.
74. Chatani, E., Naiki, H., Goto, Y. (2006). Seeding-dependent propagation and maturation of beta 2-microglobulin amyloid fibrils under high pressure. J Mol Biol, 359, 1086-1096.
75. Myers, S.L., Thomson, N.H., Radford, S.E., Ashcroft, A.E. (2006). Investigating the structural properties of amyloid-like fibrils formed in vitro from beta 2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry. Rapid Commun Mass Spectrom, 20, 1628-1636.
76. Monti, M., Principe, S., Giorgetti, S., Mangione, P., Merlini, G., Clark, A., Bellotti, V., Amoresano, A., Pucci, P. (2002). Topological investigation of amyloid fibrils obtained from beta 2-microglobulin. Protein Sci, 11, 2362-2369.
77. Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H., Goto, Y. (2002). Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange. Nat Struct Biol, 9, 332-336.
78. Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H., Goto, Y. (2004). Core and heterogeneity of beta 2-microglobulin amyloid fibrils as revealed by H/D exchange. J Mol Biol, 338, 559-571.
79. O'Nuallain, B., Wetzel, R. (2002). Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A, 99, 1485-1490.
80. Kayed, R., Head, E., Thompson, J.L., McIntire, T.M., Milton, S.C., Cotman, C.W., Glabe, C.G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 300, 486-489.
81. Bunka, D.H., Mantle, B.J., Morten, I.J., Tennent, G.A., Radford, S.E., Stockley, P.G. (2007). Production and characterization of RNA aptamers specific for amyloid fibril epitopes. J Biol Chem, 282, 34500-34509.
82. Jahn, T.R., Tennent, G.A., Radford, S.E. (2008). A common beta-sheet architecture underlies in vitro and in vivo beta 2-microglobulin amyloid fibrils. J Biol Chem, 283, 17279-17286.
83. Gozu, M., Lee, Y.H., Ohhashi, Y., Hoshino, M., Naiki, H., Goto, Y. (2003). Conformational dynamics of beta 2-microglobulin analyzed by reduction and reoxidation of the disulfide bond. J Biochem, 133, 731-736.
84. Smith, D.P., Radford, S.E. (2001). Role of the single disulphide bond of beta 2-microglobulin in amyloidosis in vitro. Protein Sci, 10, 1775-1784.
85. Ohhashi, Y., Hagihara, Y., Kozhukh, G., Hoshino, M., Hasegawa, K., Yamaguchi, I., Naiki, H., Goto, Y. (2002). The intrachain disulfide bond of beta 2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. J Biochem, 131, 45-52.
86. Yamamoto, K., Yagi, H., Ozawa, D., Sasahara, K., Naiki, H., Goto, Y. (2008). Thiol compounds inhibit the formation of amyloid fibrils by beta 2-microglobulin at neutral pH. J Mol Biol, 376, 258-268.
87. Kihara, M., Chatani, E., Iwata, K., Yamamoto, K., Matsuura, T., Nakagawa, A., Naiki, H., Goto, Y. (2006). Conformation of amyloid fibrils of beta 2-microglobulin probed by tryptophan mutagenesis. J Biol Chem, 281, 31061-31069.
88. Chiba, T., Hagihara, Y., Higurashi, T., Hasegawa, K., Naiki, H., Goto, Y. (2003). Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of beta 2-microglobulin. J Biol Chem, 278, 47016-47024.
89. Fandrich, M. (2007). On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell Mol Life Sci, 64, 2066-2078.
90. Kozhukh, G.V., Hagihara, Y., Kawakami, T., Hasegawa, K., Naiki, H., Goto, Y. (2002). Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by Achromobacter protease I. J Biol Chem, 277, 1310-1315.
91. Hasegawa, K., Ohhashi, Y., Yamaguchi, I., Takahashi, N., Tsutsumi, S., Goto, Y., Gejyo, F., Naiki, H. (2003). Amyloidogenic synthetic peptides of beta 2-microglobulin: a role of the disulfide bond. Biochem Biophys Res Commun, 304, 101-106.
92. Jones, S., Manning, J., Kad, N.M., Radford, S.E. (2003). Amyloid-forming peptides from beta 2-microglobulin:insights into the mechanism of fibril formation in vitro. J Mol Biol, 325, 249-257.
93. Ivanova, M.I., Gingery, M., Whitson, L.J., Eisenberg, D. (2003). Role of the Cterminal 28 residues of beta 2-microglobulin in amyloid fibril formation. Biochemistry, 42, 13536-13540.
94. Ivanova, M.I., Sawaya, M.R., Gingery, M., Attinger, A., Eisenberg, D. (2004). An amyloid-forming segment of beta 2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci U S A, 101, 10584-10589.
95. Ivanova, M.I., Thompson, M.J., Eisenberg, D. (2006). A systematic screen of beta 2-microglobulin and insulin for amyloid-like segments. Proc Natl Acad Sci U S A, 103, 4079-4082.
96. Platt, G.W., McParland, V.J., Kalverda, A.P., Homans, S.W., Radford, S.E. (2005). Dynamics in the unfolded state of beta 2-microglobulin studied by NMR. J Mol Biol, 346, 279-294.
97. Gazit, E. (2002). A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J, 16, 77-83.
98. McParland, V.J., Kalverda, A.P., Homans, S.W., Radford, S.E. (2002). Structural properties of an amyloid precursor of beta 2-microglobulin. Nat Struct Biol, 9, 326-331.
99. Platt, G.W., Routledge, K.E., Homans, S.W., Radford, S.E. (2008). Fibril growth kinetics reveal a region of beta 2-microglobulin important for nucleation and elongation of aggregation. J Mol Biol, 378, 251-263.
100. Lopez de la Paz, M., Serrano, L. (2004). Sequence determinants of amyloid fibril formation. Proc Natl Acad Sci U S A, 101, 87-92.
101. Conchillo-Solé , O., de Groot, N.S., Avilés, F.X., Vendrell, J., Daura, X., Ventura, S. (2007). AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics, 8, 65.
102. Richardson, J.S.,. Richardson, D.C. (2002). Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A, 99, 2754-2759.
103. Esposito, G., Ricagno, S., Corazza, A., Rennella, E., Gümral, D., Mimmi, M.C., Betto, E., Pucillo, C.E., Fogolari, F., Viglino, P., et al. (2008). The controlling roles of Trp60 and Trp95 in beta 2-microglobulin function, folding and amyloid aggregation properties. J Mol Biol, 378, 885-895.
104. Kameda, A., Hoshino, M., Higurashi, T., Takahashi, S., Naiki, H., Goto, Y. (2005). Nuclear magnetic resonance characterization of the refolding intermediate of beta 2-microglobulin trapped by non-native prolyl peptide bond. J Mol Biol, 348, 383-397.
105. Borysik, A.J., Radford, S.E., Ashcroft, A.E. (2004). Co-populated conformational ensembles of beta 2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J Biol Chem, 279, 27069-27077.
106. Smith, D.P., Giles, K., Bateman, R.H., Radford, S.E., Ashcroft, A.E. (2007). Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry. J Am Soc Mass Spectrom, 18, 2180-2190.
107. Jørgensen, T.J.D., Chenga, L., Heegaard, N.H.H. (2007). Mass spectrometric characterization of conformational preludes to beta 2-microglobulin aggregation. Int J Mass Spectrom, 268, 207-216.
108. Smith, A.M., Jahn, T.R., Ashcroft, A.E., Radford, S.E. (2006). Direct observation of oligomeric species formed in the early stages of amyloid fibril formation using electrospray ionisation mass spectrometry. J Mol Biol, 364, 9-19.
109. Xue, W.F., Homans, S.W., Radford, S.E. (2008). Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci U S A, 105, 8926-8931.
110. Calabrese, M.F., Miranker, A.D. (2007). Formation of a stable oligomer of beta 2-microglobulin requires only transient encounter with Cu(II). J Mol Biol, 367, 1-7.
111. Adlard, P.A., Bush, A.I. (2006). Metals and Alzheimer's disease. J Alzheimer's Dis, 10, 145-163.
112. Eakin, C.M., Miranker, A.D. (2005). From chance to frequent encounters: origins of beta 2-microglobulin fibrillogenesis. Biochim Biophys Acta, 1753, 92-99.
113. Thomson, N.M., Stevens, B.J., Humphery, T.J., Atkins, R.C. (1983). Comparison of trace elements in peritoneal dialysis, hemodialysis, and uremia. Kidney Int, 23, 9-14.
114. Vorbeck-Meister, I., Sommer, R., Vorbeck, F., Hörl, W.H. (1999). Quality of water used for haemodialysis: bacteriological and chemical parameters. Nephrol Dial Transplant, 14, 666-675.
115. Eakin, C.M., Knight, J.D., Morgan, C.J., Gelfand, M.A., Miranker, A.D. (2002). Formation of a copper specific binding site in non-native states of beta 2-microglobulin. Biochemistry, 41, 10646-10656.
116. De Lorenzi, E., Grossi, S., Massolini, G., Giorgetti, S., Mangione, P., Andreola, A., Chiti, F., Bellotti, V., Caccialanza, G. (2002). Capillary electrophoresis investigation of a partially unfolded conformation of beta 2-microglobulin. Electrophoresis, 23, 918-925.
117. Eakin, C.M., Attenello, F.J., Morgan, C.J., Miranker, A.D. (2004). Oligomeric assembly of native-like precursors precedes amyloid formation by beta 2-microglobulin. Biochemistry, 43, 7808-7815.
118. Villanueva, J., Hoshino, M., Katou, H., Kardos, J., Hasegawa, K., Naiki, H., Goto, Y. (2004). Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis. Protein Sci, 13, 797-809.
119. Deng, N.J., Yan, L., Singh, D., Cieplak, P. (2006). Molecular basis for the Cu2+ binding-induced destabilization of beta 2-microglobulin revealed by molecular dynamics simulation. Biophys J, 90, 3865-3879.
120. Antwi, K., Mahar, M., Srikanth, R., Olbris, M.R., Tyson, J.F., Vachet, R.W. (2008). Cu(II) organizes beta 2-microglobulin oligomers but is released upon amyloid formation. Protein Sci, 17, 748-759.
121. Yamamoto, S., Gejyo, F. (2005). Historical background and clinical treatment of dialysis-related amyloidosis. Biochim Biophys Acta, 1753, 4-10.
122. Jaradat, M.I., Moe, S.M. (2001). Effect of hemodialysis membranes on beta 2-microglobulin amyloidosis. Semin Dial, 14, 107-112.
123. Kutsuki, H. (2005). Beta 2-microglobulin-selective direct hemoperfusion column for the treatment of dialysis-related amyloidosis. Biochim Biophys Acta, 1753, 141-145.
124. Lornoy, W., Because, I., Billiouw, J.M., Sierens, L., Van Malderen, P., D'Haenens, P. (2000). On-line haemodiafiltration: remarkable removal of beta 2-microglobulin. Long-term clinical observations. Nephrol Dial Transplant, 15(Suppl 1), 49-54.
125. Gejyo, F., Kawaguchi, Y., Hara, S., Nakazawa, R., Azuma, N., Ogawa, H., Koda, Y., Suzuki, M., Kaneda, H., Kishimoto, H., et al. (2004). Arresting dialysis-related amyloidosis: a prospective multicenter controlled trial of direct hemoperfusion with a beta 2-microglobulin adsorption column. Artif Organs, 28, 371-380.
126. Winchester, J.F., Salsberg, J.A., Levin, N.W. (2003). Beta 2-microglobulin in ESRD: an in-depth review. Adv Ren Replace Ther, 10, 279-309.
127. Bunka, D.H., Stockley, P.G. (2006). Aptamers come of age-at last. Nat Rev Microbiol, 4, 588-596.
128. Gillmore, J.D., Hawkins, P.N. (2006). Drug insight: emerging therapies for amyloidosis. Nat Clin Pract Nephrol, 2, 263-270.
129. Corazza, A., Pettirossi, F., Viglino, P., Verdone, G., Garcia, J., Dumy, P., Giorgetti, S., Mangione, P., Raimondi, S., Stoppini, M., et al. (2004). Properties of some variants of human beta 2-microglobulin and amyloidogenesis. J Biol Chem, 279, 9176-9189.
130. Linke, R.P., Hampl, H., Lobeck, H., Ritz, E., Bommer, J., Waldherr, R., Eulitz, M. (1989). Lysine-specific cleavage of beta 2-microglobulin in amyloid deposits associated with hemodialysis. Kidney Int, 36, 675-681.