Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β 2-microglobulin monomer and fibrils

PLoS ONE

Volumn 6, Issue 11, 2011, Pages

  Porter, Morwenna Y ^a   Routledge, Katy E ^a,b   Radford, Sheena E ^a   Hewitt, Eric W ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; MONOMER;

AMYLOIDOSIS; ARTICLE; BONE DESTRUCTION; BONE REMODELING; CARTILAGE CELL; CELL ACTIVITY; CELL INFILTRATION; CELL VIABILITY; COMPLEX FORMATION; CONTROLLED STUDY; CYTOTOXICITY; DISEASE ASSOCIATION; HEMODIALYSIS; HUMAN; HUMAN CELL; HUMAN TISSUE; IN VIVO STUDY; INTERNALIZATION; JOINT; JOINT DESTRUCTION; MACROPHAGE; MONOCYTE; OSTEOBLAST; OSTEOCLAST; OSTEOCLASTOGENESIS; OSTEOLYSIS; PATHOLOGY; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; TARGET CELL; THERAPY EFFECT; CELL CULTURE; CELL SURVIVAL; CHEMISTRY; CYTOLOGY; DRUG EFFECT; IMMUNOBLOTTING; METABOLISM; MONONUCLEAR CELL; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOIDOSIS; BETA 2-MICROGLOBULIN; CELL SURVIVAL; CELLS, CULTURED; CHONDROCYTES; HUMANS; IMMUNOBLOTTING; LEUKOCYTES, MONONUCLEAR; MICROSCOPY, ELECTRON, TRANSMISSION; OSTEOBLASTS;

EID: 80655128596     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027353     Document Type: Article

References (59)

1. Chiti F, Dobson CM, (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
2. Floege J, Ehlerding G, (1996) β2-microglobulin-associated amyloidosis. Nephron 72: 9-26.
3. Floege J, Ketteler M, (2001) β2-microglobulin-derived amyloidosis: an update. Kidney Int Suppl 78: S164-171.
4. Gorevic PD, Casey TT, Stone WJ, DiRaimondo CR, Prelli FC, et al. (1985) β2-microglobulin is an amyloidogenic protein in man. J Clin Invest 76: 2425-2429.
5. Gejyo F, Yamada T, Odani S, Nakagawa Y, Arakawa M, et al. (1985) A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin. Biochem Biophys Res Commun 129: 701-706.
6. Heegaard NH, (2009) β2-microglobulin: from physiology to amyloidosis. Amyloid 16: 151-173.
7. Drueke TB, Massy ZA, (2009) β2-microglobulin. Semin Dial 22: 378-380.
8. Danesh F, Ho LT, (2001) Dialysis-related amyloidosis: history and clinical manifestations. Semin Dial 14: 80-85.
9. Ohashi K, (2001) Pathogenesis of β2-microglobulin amyloidosis. Pathol Int 51: 1-10.
10. Relini A, Canale C, De Stefano S, Rolandi R, Giorgetti S, et al. (2006) Collagen plays an active role in the aggregation of β2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J Biol Chem 281: 16521-16529.
11. Relini A, De Stefano S, Torrassa S, Cavalleri O, Rolandi R, et al. (2008) Heparin strongly enhances the formation of β2-microglobulin amyloid fibrils in the presence of type I collagen. J Biol Chem 283: 4912-4920.
12. Myers SL, Jones S, Jahn TR, Morten IJ, Tennent GA, et al. (2006) A systematic study of the effect of physiological factors on β2-microglobulin amyloid formation at neutral pH. Biochemistry 45: 2311-2321.
13. Borysik AJ, Morten IJ, Radford SE, Hewitt EW, (2007) Specific glycosaminoglycans promote unseeded amyloid formation from β2-microglobulin under physiological conditions. Kidney Int 72: 174-181.
14. Yamamoto S, Yamaguchi I, Hasegawa K, Tsutsumi S, Goto Y, et al. (2004) Glycosaminoglycans enhance the trifluoroethanol-induced extension of β2-microglobulin-related amyloid fibrils at a neutral pH. J Am Soc Nephrol 15: 126-133.
15. Bellotti V, Stoppini M, Mangione P, Sunde M, Robinson C, et al. (1998) β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur J Biochem 258: 61-67.
16. Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, et al. (2000) Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci 9: 831-845.
17. Eichner T, Radford SE, (2009) A generic mechanism of β2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. J Mol Biol 386: 1312-1326.
18. Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE, (2011) Conformational conversion during amyloid formation at atomic resolution. Mol Cell 41: 161-172.
19. Eichner T, Radford SE, (2011) Understanding the complex mechanisms of β2-microglobulin amyloid assembly. FEBS J 278: 3868-83.
20. Inoue H, Saito I, Nakazawa R, Mukaida N, Matsushima K, et al. (1995) Expression of inflammatory cytokines and adhesion molecules in haemodialysis-associated amyloidosis. Nephrol Dial Transplant 10: 2077-2082.
21. Argiles A, Mourad G, Kerr PG, Garcia M, Collins B, et al. (1994) Cells surrounding haemodialysis-associated amyloid deposits are mainly macrophages. Nephrol Dial Transplant 9: 662-667.
22. Garbar C, Jadoul M, Noel H, van Ypersele de Strihou C, (1999) Histological characteristics of sternoclavicular β2-microglobulin amyloidosis and clues for its histogenesis. Kidney Int 55: 1983-1990.
23. Kazama JJ, Maruyama H, Gejyo F, (2001) Osteoclastogenesis and osteoclast activation in dialysis-related amyloid osteopathy. Am Journal Kidney Dis 38: S156-160.
24. Asagiri M, Takayanagi H, (2007) The molecular understanding of osteoclast differentiation. Bone 40: 251-264.
25. Roodman GD, (2006) Regulation of osteoclast differentiation. Ann N Y Acad Sci 1068: 100-109.
26. Raggatt LJ, Partridge NC, (2010) Cellular and molecular mechanisms of bone remodeling. J Biol Chem 285: 25103-25108.
27. Kazama JJ, Yamamoto S, Takahashi N, Ito Y, Maruyama H, et al. (2006) Aβ-2M-amyloidosis and related bone diseases. J Bone Miner Metab 24: 182-184.
28. Menaa C, Esser E, Sprague SM, (2008) β2-microglobulin stimulates osteoclast formation. Kidney Int 73: 1275-1281.
29. Xue WF, Hellewell AL, Gosal WS, Homans SW, Hewitt EW, et al. (2009) Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem 284: 34272-34282.
30. Kad NM, Thomson NH, Smith DP, Smith DA, Radford SE, (2001) β2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J Mol Biol 313: 559-571.
31. Ladner CL, Chen M, Smith DP, Platt GW, Radford SE, et al. (2010) Stacked sets of parallel, in-register β-strands of β2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J Biol Chem 285: 17137-17147.
32. Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
33. O'Nuallain B, Wetzel R, (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A 99: 1485-1490.
34. Nishi S, Ogino S, Maruyama Y, Honma N, Gejyo F, et al. (1990) Electron-microscopic and immunohistochemical study of β2-microglobulin-related amyloidosis. Nephron 56: 357-363.
35. Inoue S, Kuroiwa M, Ohashi K, Hara M, Kisilevsky R, (1997) Ultrastructural organization of hemodialysis-associated β2-microglobulin amyloid fibrils. Kidney Int 52: 1543-1549.
36. Jahn TR, Tennent GA, Radford SE, (2008) A common beta-sheet architecture underlies in vitro and in vivo β2-microglobulin amyloid fibrils. J Biol Chem 283: 17279-17286.
37. Gordon S, Taylor PR, (2005) Monocyte and macrophage heterogeneity. Nat Rev Immunol 5: 953-964.
38. Argiles A, Garcia Garcia M, Mourad G, (2002) Phagocytosis of dialysis-related amyloid deposits by macrophages. Nephrol Dial Transplant 17: 1136-1138.
39. Efstratiadis T, Moss DW, (1985) Tartrate-resistant acid phosphatase in human alveolar macrophages. Enzyme 34: 140-143.
40. Morten IJ, Gosal WS, Radford SE, Hewitt EW, (2007) Investigation into the role of macrophages in the formation and degradation of β2-microglobulin amyloid fibrils. J Biol Chem 282: 29691-29700.
41. Garcia-Garcia M, Argiles Gouin-Charnet A, Durfort M, Garcia-Valero J, et al. (1999) Impaired lysosomal processing of β2-microglobulin by infiltrating macrophages in dialysis amyloidosis. Kidney Int 55: 899-906.
42. Hayman AR, (2008) Tartrate-resistant acid phosphatase (TRAP) and the osteoclast/immune cell dichotomy. Autoimmunity 41: 218-223.
43. Malluche HH, Mawad HW, Monier-Faugere MC, (2011) Renal osteodystrophy in the first decade of the new millennium: analysis of 630 bone biopsies in black and white patients. J Bone Miner Res 26: 1368-1376.
44. Gharibyan AL, Zamotin V, Yanamandra K, Moskaleva OS, Margulis BA, et al. (2007) Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. J Mol Biol 365: 1337-1349.
45. Rigacci S, Bucciantini M, Relini A, Pesce A, Gliozzi A, et al. (2008) The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies. Biophys J 94: 3635-3646.
46. Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV, (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 281: 13828-13836.
47. Giorgetti S, Raimondi S, Cassinelli S, Bucciantini M, Stefani M, et al. (2009) β2-microglobulin is potentially neurotoxic, but the blood brain barrier is likely to protect the brain from its toxicity. Nephrol Dial Transplant 24: 1176-1181.
48. Giorgetti S, Raimondi S, Pagano K, Relini A, Bucciantini M, et al. (2011) Effect of tetracyclines on the dynamics of formation and destructuration of β2-microglobulin amyloid fibrils. J Biol Chem 286: 2121-2131.
49. Corlin DB, Sen JW, Ladefoged S, Lund GB, Nissen MH, et al. (2005) Quantification of cleaved β2-microglobulin in serum from patients undergoing chronic hemodialysis. Clin Chem 51: 1177-1184.
50. Giorgetti S, Rossi A, Mangione P, Raimondi S, Marini S, et al. (2005) β2-microglobulin isoforms display an heterogeneous affinity for type I collagen. Protein Sci 14: 696-702.
51. Dehle FC, Ecroyd H, Musgrave IF, Carver JA, (2010) αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide. Cell stress & chaperones 15: 1013-1026.
52. Lee YJ, Savtchenko R, Ostapchenko VG, Makarava N, Baskakov IV, (2011) Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity. PloS One 6: e20244.
53. Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307: 262-265.
54. Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, et al. (2010) The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. J Mol Biol 402: 783-796.
55. Schonland SO, Hansmann J, Mechtersheimer G, Goldschmidt H, Ho AD, et al. (2008) Bone involvement in patients with systemic AL amyloidosis mimics lytic myeloma bone disease. Haematologica 93: 955-956.
56. Shiraishi M, Ando Y, Mizuta H, Nakamura E, Takagi K, et al. (1997) Charcot knee arthropathy with articular amyloid deposition in familial amyloidotic polyneuropathy. Scand J rheumatol 26: 61-64.
57. Cameron B, Landreth GE, (2010) Inflammation, microglia, and Alzheimer's disease. Neurobiol Dis 37: 503-509.
58. de Koning EJ, van den Brand JJ, Mott VL, Charge SB, Hansen BC, et al. (1998) Macrophages and pancreatic islet amyloidosis. Amyloid 5: 247-254.
59. Gosal WS, Morten IJ, Hewitt EW, Smith DA, Thomson NH, et al. (2005) Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid. J Mol Biol 351: 850-864.