Oxidation inhibits amyloid fibril formation of transthyretin

FEBS Journal

Volumn 273, Issue 23, 2006, Pages 5400-5406

  Maleknia, Simin D ^a   Reixach, Natàlia ^b   Buxbaum, Joel N ^b  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Amyloid fibril; Footprinting; Radical probe mass spectometry; Reactive oxygen species; Transthyretin

Indexed keywords

AMYLOID; METHIONINE; PREALBUMIN; VALINE;

AMINO ACID SUBSTITUTION; AMYLOIDOSIS; ARTICLE; CROSS LINKING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; HUMANS; KINETICS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATION-REDUCTION; PREALBUMIN; PROTEIN FOLDING;

EID: 33751112217     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05532.x     Document Type: Article

References (42)

1. Stadtman ER (1992) Protein oxidation and aging. Science 257, 1220-1224.
2. Berlett BS & Stadtman ER (1997) Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272, 20313-20316.
3. Stadtman ER, Van Remmen H, Richardson A, Whr NB & Levine RL (2005) Methionine oxidation and aging. Biochim Biophys Acta 1703, 135.
4. Dean RT, Fu S, Stocker R & Davies MJ (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 324, 1-18.
5. Maleknia SD, Brenowitz M & Chance MR (1999) Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry. Anal Chem 71, 3965-3973.
6. Maleknia SD & Downard KM (2001) Radical approaches to probe protein structure, folding, and interactions by mass spectrometry. Mass Spectrom Rev 20, 388-401.
7. Stadtman ER (1995) The status of oxidatively modified proteins as a marker of aging. In Molecular Aspect of Aging (Esser, K & Martin, GM, eds), pp. 129-143. John Wiley & Sons Ltd., New York, NY.
8. Oliver CN, Starke-Reed Stadtman ER, Liu GJ, Carney JM & Floyd RA (1990) Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia / reperfusion-induced injury to gerbil brain. Proc Natl Acad Sci USA 87, 5144-5147.
9. Hilser VJ, Dowdy D, Oas TG & Freire E (1998) The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc Natl Acad Sci USA 95, 9903-9908.
10. Fleming PJ & Richards FM (2000) Protein packing: dependence on protein size, secondary structure and amino acid composition. J Mol Biol 299, 487-498.
11. Lee KL, Xie D, Freire E & Amzel LM (1994) Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins 20, 68-84.
12. Kay MS & Baldwin RL (1996) Packing interactions in the apomyglobin folding intermediate. Nat Struct Biol 3, 439-445.
13. Thomas PJ, Qu B & Pedersen PL (1995) Defective protein folding as a basis of human disease. Trends Biochem Sci 20, 456-459.
14. Taubes G (1996) Misfolding the way to disease. Science 271, 1493-1495.
15. Kelly JW (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8, 101-106.
16. Dobson CM (2003) Protein folding and misfolding. Nature 426, 884-890.
17. Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426, 900-904.
18. Buxbaum JN & Tagoe CE (2000) The genetics of the amyloidoses. Annu Rev Med 51, 543-569.
19. Hornberg A, Eneqvist T, Olofsson A, Lundgren E & Sauer-Eriksson AE (2000) A comparative analysis of 23 structures of the amyloidogenic protein transthyretin. J Mol Biol 302, 649-669.
20. Westermark P, Sletten K, Johansson B & Cornwell GG (1990) Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci USA 87, 2843-2845.
21. Saraiva MJ (2001) Transthyretin mutations in hyperthyroxinemia and amyloid diseases. Hum Mutat 17, 493-503.
22. Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL & Kelly JW (2005) Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc Chem Res 38, 911-921.
23. Olofsson A, Ippel HJ, Baranov V, Horstedt P, Wijmenga S & Lundgren E (2001) Capture of a dimeric intermediate during transthyretin amyloid formation. J Biol Chem 276, 39592-39599.
24. Reixach N, Deechongki S, Jiang X, Kelly JW & Buxbaum JN (2004) Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci USA 101, 2817-2822.
25. Liu K, Cho HS, Hoy DW, Nguyen TN, Olds P, Kelly JW & Wemmer DE (2000) Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies the stable core of the individual subunits and indicates mobility at the subunit interface. J Mol Biol 303, 555-565.
26. Hammarstrom P, Wiseman RL, Powers ET & Kelly JW (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299, 713-716.
27. Zhang Q & Kelly JW (2003) Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions. Biochemistry 42, 8756-8761.
28. Lashuel HA, Lai Z & Kelly JW (1998) Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37, 17851-17864.
29. McCutchen SL, Colon W & Kelly JW (1993) Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32, 12119-12127.
30. Maleknia SD, Downard KM & Chance MR (1999) Electrospray-assisted modification of proteins: a radical probe of protein structure. Rapid Commun Mass Spectrom 13, 2352-2358.
31. Maleknia SD, Wong JW & Downard KM (2004) Photochemical and electrophysical production of radicals on millisecond timescales to probe the structure, dynamics and interactions of proteins. Photochem Photobiol Sci 3, 741-748.
32. Maleknia SD, Kiselar JG & Downard KM (2002) Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun Mass Spectrom 16, 53-61.
33. Maleknia SD & Downard KM (2001) Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry. Eur J Biochem 268, 5578-5588.
34. Wong JH, Maleknia SD & Downard KM (2003) Study of the ribonuclease-S-protein-peptide complex using a radical probe and electrospray ionization mass spectrometry. Anal Chem 75, 1557-1563.
35. Wong JH, Maleknia SD & Downard KM (2005) Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 16, 225-233.
36. Shum WK, Maleknia SD & Downard KM (2005) Onset of oxidative damage in alpha-crystallin by radical probe mass spectrometry. Anal Biochem 344, 247-256.
37. Teh LC, Murphy LJ, Huq NL, Surus AS, Friesen HG, Lazarus L & Chapman GE (1987) Methionine oxidation in human growth hormone and human chorionic somatomammotropin. Effects on receptor binding and biological activities. J Biol Chem 262, 6472-6477.
38. Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O & Steen L (1993) The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30 fi Met variant to 1.7-Å resolution. J Biol Chem 268, 2416.
39. Willard L, Ranjan A, Zhang H, Monzavil H, Boyko RF, Sykes BD & Wishart DS (2003) VADAR: a web server for quantitative evaluation of protein structure quality. Nucleic Acids Res 31, 3316-3319 (http://redpoll.pharmacy. ualberta.ca/vadar/).
40. Kammerer RA, Kostrewa D, Surdo J, Detken A, Garcia-Echeverria C, Green JD, Muller SA, Meier BH, Winkler FK, Dobson CM, et al. (2004) Exploring amyloid formation by a de novo design. Proc Natl Acad Sci USA 101, 4435-4440.
41. Cervera J & Levine RL (1998) Modulation of the hydrophobicity of glutamine synthetase by mixed-function oxidation. FASEB J 2, 2591-2595.
42. Hammarstrom P, Jiang X, Hurshman AR, Powers ET & Kelly JW (2002) Sequence-dependent denaturation energetics: a major determinant in amyloid disease diversity. Proc Natl Acad Sci USA 99, 16427-16432.