Metal binding sheds light on mechanisms of amyloid assembly

Prion

Volumn 3, Issue 1, 2009, Pages 1-4

  Calabrese, Matthew F ^a   Miranker, Andrew D ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

2 microglobulin; Amyloid; Copper; Dialysis related amyloidosis; Prion; Protein folding

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; BETA 2 MICROGLOBULIN; CUPRIC ION; PRION PROTEIN;

AMYLOIDOSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; METAL BINDING; NOTE; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN STRUCTURE; REACTION ANALYSIS;

AMYLOIDOSIS; BETA 2-MICROGLOBULIN; COPPER; HUMANS; MODELS, MOLECULAR; PRIONS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; RENAL DIALYSIS; SENILE PLAQUES;

MAMMALIAN PRION;

EID: 66749133376     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.3.1.8601     Document Type: Note

References (43)

1. York IA, Rock KL. Antigen processing and presentation by the class I major histocompatibility complex. Annu Rev Immunol 1996; 14: 369-396 (Pubitemid 26130189)
2. Floege J, Ehlerding G. Beta-2-microglobulin-associated amyloidosis. Nephron 1996; 72: 9-26. (Pubitemid 26009466)
3. Okon M, Bray P, Vucelic D. 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. Biochemistry 1992; 31: 8906-8915
4. Morgan CJ, Gelfand M, Atreya C, Miranker AD. Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J Mol Biol 2001; 309: 339-345 (Pubitemid 32553492)
5. Kameda A, Hoshino M, Higurashi T, Takahashi S, Naiki H, Goto Y. Nuclear magnetic resonance characterization of the refolding intermediate of beta(2)-microglobulin trapped by non-native prolyl peptide bond. J Mol Biol 2005; 348: 383-397
6. Jahn TR, Parker MJ, Homans SW, Radford SE. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 2006; 13: 195-201. (Pubitemid 43348504)
7. Chiti F, Mangione P, Andreola A, Giorgetti S, Stefani M, Dobson CM, et al. Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin. J Mol Biol 2001; 307: 379-391 (Pubitemid 33029988)
8. Malaguarnera M, Restuccia S, Di Fazio I, Zoccolo AM, Trovato BA, Pistone G. Serum beta2-microglobulin in chronic hepatitis C. Dig Dis Sci 1997; 42: 762-766
9. Keating MJ. Chronic lymphocytic leukemia. Semin Oncol 1999; 26: 107-114 (Pubitemid 29523418)
10. Eakin CM, Attenello FJ, Morgan CJ, Miranker AD. Oligomeric assembly of native-like precursors precedes amyloid formation by beta-2 microglobulin. Biochemistry 2004; 43: 7808-7815 (Pubitemid 38787688)
11. Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, et al. Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci 2000; 9: 831-845 (Pubitemid 30353325)
12. McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, et al. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. Biochemistry 2000; 39: 8735-8746
13. Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, Goto Y, et al. Low concentrations of sodium dodecyl sulfate induce the extension of beta(2)-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 2004; 43: 11075-11082
14. Yamamoto S, Yamaguchi I, Hasegawa K, Tsutsumi S, Goto Y, Gejyo F, et al. Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin- related amyloid fibrils at a neutral pH. J Am Soc Nephrol 2004; 15: 126-133 (Pubitemid 38020704)
15. Vorbeck-Meister I, Sommer R, Vorbeck F, Horl WH. Quality of water used for haemodialysis: bacteriological and chemical parameters. Nephrol Dial Transplant 1999; 14: 666-675 (Pubitemid 29105996)
16. Eakin CM, Knight JD, Morgan CJ, Gelfand MA, Miranker AD. Formation of a copper specific binding site in non-native states of beta-2-microglobulin. Biochemistry 2002; 41: 10646-10656 (Pubitemid 34913324)
17. Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, et al. The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci 2002; 11: 487-499 (Pubitemid 34171254)
18. Villanueva J, Hoshino M, Katou H, Kardos J, Hasegawa K, Naiki H, et al. Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis. Protein Sci 2004; 13: 797-809. (Pubitemid 38252576)
19. Lim J, Vachet RW. Using mass spectrometry to study copper-protein binding under native and non-native conditions: beta-2-microglobulin. Anal Chem 2004; 76: 3498-3504 (Pubitemid 38868807)
20. Eakin CM, Berman AJ, Miranker AD. A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 2006; 13: 202-208 (Pubitemid 43348505)
21. Dobson CM. An accidental breach of a protein's natural defenses. Nat Struct Mol Biol 2006; 13: 295-297 (Pubitemid 43879676)
22. LeVine H, 3rd. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 1993; 2: 404-410
23. Calabrese MF, Miranker AD. Formation of a stable oligomer of beta-2 microglobulin requires only transient encounter with Cu(II). J Mol Biol 2007; 367: 1-7. (Pubitemid 46274708)
24. Antwi K, Mahar M, Srikanth R, Olbris MR, Tyson JF, Vachet RW. Cu(II) organizes {beta}-2-microglobulin oligomers but is released upon amyloid formation. Protein Sci 2008; 17: 748-759
25. Calabrese MF, Eakin CM, Wang JM, Miranker AD. A regulatable switch mediates self-association in an immunoglobulin fold. Nat Struct Mol Biol 2008; 15: 965-971
26. Burns CS, Aronoff-Spencer E, Dunham CM, Lario P, Avdievich NI, Antholine WE, et al. Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry 2002; 41: 3991-4001. (Pubitemid 34251038)
27. McParland VJ, Kalverda AP, Homans SW, Radford SE. Structural properties of an amyloid precursor of beta(2)-microglobulin. Nat Struct Biol 2002; 9: 326-331
28. Brown DR, Qin K, Herms JW, Madlung A, Manson J, Strome R, et al. The cellular prion protein binds copper in vivo. Nature 1997; 390: 684-687 (Pubitemid 28016355)
29. Brown DR, Schmidt B, Kretzschmar HA. Effects of copper on survival of prion protein knockout neurons and glia. J Neurochem 1998; 70: 1686-1693 (Pubitemid 28136985)
30. Millhauser GL. Copper and the prion protein: methods, structures, function, and disease. Annu Rev Phys Chem 2007; 58: 299-320. (Pubitemid 46877592)
31. Viles JH, Klewpatinond M, Nadal RC. Copper and the structural biology of the prion protein. Biochem Soc Trans 2008; 36: 1288-1292
32. Kenward AG, Bartolotti LJ, Burns CS. Copper and zinc promote interactions between membrane-anchored peptides of the metal binding domain of the prion protein. Biochemistry 2007; 46: 4261-4271 (Pubitemid 46559393)
33. Wadsworth JD, Hill AF, Joiner S, Jackson GS, Clarke AR, Collinge J. Strain-specific prion-protein conformation determined by metal ions. Nat Cell Biol 1999; 1: 55-59 (Pubitemid 129495011)
34. Bocharova OV, Breydo L, Salnikov VV, Baskakov IV. Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry 2005; 44: 6776-6787 (Pubitemid 40637231)
35. Davies P, Brown DR. The chemistry of copper binding to PrP: is there sufficient evidence to elucidate a role for copper in protein function? Biochem J 2008; 410: 237-244
36. Cherny RA, Legg JT, McLean CA, Fairlie DP, Huang X, Atwood CS, et al. Aqueous dissolution of Alzheimer's disease Abeta amyloid deposits by biometal depletion. J Biol Chem 1999; 274: 23223-23228 (Pubitemid 129529155)
37. Bush AI, Tanzi RE. The galvanization of beta-amyloid in Alzheimer's disease. Proc Natl Acad Sci USA 2002; 99: 7317-7319
38. Miura T, Suzuki K, Kohata N, Takeuchi H. Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes. Biochemistry 2000; 39: 7024-7031 (Pubitemid 30390396)
39. Uversky VN, Li J, Fink AL. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J Biol Chem 2001; 276: 44284-44296 (Pubitemid 37384003)
40. Lee JC, Gray HB, Winkler JR. Copper(II) Binding to alpha-Synuclein, the Parkinson's Protein. J Am Chem Soc 2008.
41. Davis DP, Gallo G, Vogen SM, Dul JL, Sciarretta KL, Kumar A, et al. Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain. J Mol Biol 2001; 313: 1021-1034 (Pubitemid 33081898)
42. Sayre LM, Perry G, Smith MA. Redox metals and neurodegenerative disease. Curr Opin Chem Biol 1999; 3: 220-225 (Pubitemid 29145789)
43. Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 1987; 329:506-512 (Pubitemid 17131093)