473
Views
29
CrossRef citations to date
0
Altmetric
Commentary & View

Metal binding sheds light on mechanisms of amyloid assembly

&
Pages 1-4 | Received 07 Sep 2008, Accepted 28 Jan 2009, Published online: 01 Jan 2009

References

  • York IA, Rock KL. Antigen processing and presentation by the class I major histocompatibility complex. Annu Rev Immunol 1996; 14:369 - 396
  • Floege J, Ehlerding G. Beta-2-microglobulin-associated amyloidosis. Nephron 1996; 72:9 - 26
  • Okon M, Bray P, Vucelic D. 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. Biochemistry 1992; 31:8906 - 8915
  • 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
  • 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
  • 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
  • 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
  • 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
  • Keating MJ. Chronic lymphocytic leukemia. Semin Oncol 1999; 26:107 - 114
  • 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
  • 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
  • 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
  • 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)-microglobulinrelated amyloid fibrils at a neutral pH. Biochemistry 2004; 43:11075 - 11082
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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
  • Eakin CM, Berman AJ, Miranker AD. A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 2006; 13:202 - 208
  • Dobson CM. An accidental breach of a protein's natural defenses. Nat Struct Mol Biol 2006; 13:295 - 297
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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
  • Brown DR, Schmidt B, Kretzschmar HA. Effects of copper on survival of prion protein knockout neurons and glia. J Neurochem 1998; 70:1686 - 1693
  • Millhauser GL. Copper and the prion protein: methods, structures, function, and disease. Annu Rev Phys Chem 2007; 58:299 - 320
  • Viles JH, Klewpatinond M, Nadal RC. Copper and the structural biology of the prion protein. Biochem Soc Trans 2008; 36:1288 - 1292
  • 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
  • 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
  • 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
  • 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
  • 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
  • Bush AI, Tanzi RE. The galvanization of beta-amyloid in Alzheimer's disease. Proc Natl Acad Sci USA 2002; 99:7317 - 7319
  • 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
  • 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
  • Lee JC, Gray HB, Winkler JR. Copper(II) Binding to alpha-Synuclein, the Parkinson's Protein. J Am Chem Soc 2008;
  • 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
  • Sayre LM, Perry G, Smith MA. Redox metals and neurodegenerative disease. Curr Opin Chem Biol 1999; 3:220 - 225
  • 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

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.