Retraction: Glycation accelerates fibrillization of the amyloidogenic W7fW14F apomyoglobin (PLoS One (2013) 8:12 (e80768) DOI: 10.1371/journal.pone.0080768);Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobin

PLoS ONE

Volumn 8, Issue 12, 2013, Pages

  Iannuzzi, Clara ^a   Maritato, Rosa ^a   Irace, Gaetano ^a   Sirangelo, Ivana ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; AMYLOID; APOMYOGLOBIN; GLUCOSE; LYSINE; RIBOSE; UNCLASSIFIED DRUG; W7FW14F APOMYOGLOBIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL VIABILITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOTOXICITY; FIBRILLIZATION; MOUSE; NONHUMAN; PROTEIN AGGREGATION; PROTEIN CROSS LINKING; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; TOXICITY TESTING;

AMYLOIDOGENIC PROTEINS; ANIMALS; APOPROTEINS; CELL SURVIVAL; ESCHERICHIA COLI; FLOCCULATION; GENE EXPRESSION; GLUCOSE; GLYCOSYLATION; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; MICE; MODELS, MOLECULAR; MYOGLOBIN; NIH 3T3 CELLS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RIBOSE;

EID: 84891875678     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0218284     Document Type: Erratum

References (57)

1. Dobson CM (2003) Protein folding and misfolding. Nature 426: 884-890.
2. Luheshi LM, Dobson CM (2009) Bridging the gap: from protein misfolding to protein mis-folding diseases. FEBS Letters 583: 2581-2586.
3. Serpell LC, Sunde M, Benson MD, Tennent GA, Pepys MB, et al. (2000)) The protofilament substructure of amyloid fibrils. J Mol Biol 300: 1033-1039.
4. Kodali R, Wetzel R (2007) Polymorphism in the intermediates and products of amyloid assembly. Current Opinion in Structural Biology 17: 48-57.
5. Invernizzi G, Papaleo E, Sabate R, Ventura S (2012) Protein aggregation: mechanisms and functional consequences. Int J Biochem Cell Biol. 44: 1541-1554.
6. Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511.
7. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human diseases. Annual Review of Biochemistry 75: 333-366.
8. Uversky VN (2010) Mysterious oligomerization of the amyloidogenic proteins. FEBS J 277: 2940-2953.
9. Stefani M (2012) Structural features and cytotoxicity of amyloid oligomers: Implication in Alzheimer's disease and other diseases with amyloid deposits. Progress in Neurobiology 99: 226-245.
10. Aggeli A, Nyrkova IA, Bell M, Harding R, Carrick L, et al. (2001) Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils and fibers. PNAS USA 98: 11857-11862.
11. Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM (1998) Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 95: 4224-4228.
12. Litvinovich SV, Brew SA, Aota S, Akiyama SK, Haudenschild C, et al. (1998) Formation of amyloid like fibrils by self association of a partially unfolded fibronectin type III module. J Mol Biol 280: 245-258.
13. Chiti F, Webster P, Taddei N, Clark A, Stefani M, et al. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 96: 3590-3594.
14. Vilasi S, Iannuzzi C, Portaccio M, Irace G, Sirangelo I (2008) Effect of trehalose on W7FW14F apomyoglobin and insulin fibrillization: new insight into inhibition activity. Biochemistry 47: 1789-1796.
15. Fandrich M, Forge V, Buder K, Kittler M, Dobson CM, et al. (2003) Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc Natl.Acad.Sci USA 100: 15463-15468.
16. Sirangelo I, Malmo C, Casillo M, Mezzogiorno A, Papa M, et al. (2002) Tryptophanyl substitution in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH. J Biol Chem 277: 45887-45891.
17. Sirangelo I, Malmo C, Iannuzzi C, Mezzogiorno A, Bianco MR, et al. (2004) Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F. J Biol Chem 279: 13183-13189.
18. Iannuzzi C, Vilasi S, Portaccio M, Irace G, Sirangelo I (2007) Heme binding inhibits the fibrillization of amyloidogenic apomyoglobin and determines lack of aggregate cytotoxicity. Protein Sci 16: 507-516.
19. Iannuzzi C, Maritato R, Irace G, Sirangelo I (2013) Misfolding and amyloid aggregation of apomyoglobin. Int J Mol Sci 14: 14287-14300.
20. Malmo C, Vilasi S, Iannuzzi C, Tacchi S, Cametti C, et al. (2006) Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a pre-fibrillar, highly cytotoxic state. FASEB J 20: 346-347.
21. Ortore MG, Spinozzi F, Vilasi S, Sirangelo I, Irace G, et al. (2011) Time-resolved small-angle x-ray scattering study of the early stage of amyloid formation of an apomyoglobin mutant. Phys Rev E Stat Nonlin Soft Matter Phys 84: 061904.
22. Vilasi A, Vilasi S, Romano R, Acernese F, Barone F, et al. (2013) Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and 1 H-NMR metabonomic approach. J Cell Physiol 228: 1359-1367.
23. Miyata T, Oda O, Inagi R, Iida Y, Araki N, et al. (1993) b2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis. J Clin Invest 92: 1243-1252.
24. Kikuchi S, Ogata A, Shinpo K, Moriwaka F, Fujii F, et al. (2000) Detection of an Amadori product, 1-hexitol-lysine, in the anterior horn of the amyotrophic lateral sclerosis and spinobulbar muscular atrophy spinal cord: evidence for early involvement of glycation in motoneuron diseases. Acta Neuropathol 99: 63-66.
25. Munch G, Luth HJ, Wong A, Arendt T, Hirsch E, et al. (2000) Crosslinking of alpha-synuclein by advanced glycation endproducts-an early pathophysiological step in Lewy body formation? J Chem Neuroanat 20: 253-257.
26. Dukic-Stefanovic S, Schinzel R, Riederer P, Munch G (2001) AGES in brainageing: AGE-inhibitors as neuroprotective and anti-dementia drugs? Biogerontology 2: 19-34.
27. Shults CW (2006) Lewy bodies. Proc Natl Acad Sci USA 103: 1661-1668.
28. Lyons TJ, Silvestri G, Dunn JA, Dyer DG, Baynes JW (1991) Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes 40: 1010-1015.
29. McCance DR, Dyer DG, Dunn JA, Bailie KE, Thorpe SR, et al. (1993) Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J Clin Invest 91: 2470-2478.
30. Miyata T, van Ypersele de Strihou C, Kurokawa K, Baynes JW (1999) Alterations in nonenzymatic biochemistry in uremia: origin and significance of "carbonyl stress" in long-term uremic complications. Kidney Int 55: 389-399.
31. Day JF, Thorpe SR, Baynes JW (1979) Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum. J Biol Chem 254: 595-597.
32. Monnier VM, Nagaraj RH, Portero-Otin M, Glomb M, Elgawish AH, et al. (1996) Structure of advanced Maillard reaction products and their pathological role. Nephrol Dial Transplant 11: 20-26.
33. Necula M, Kuret J (2004) Pseudophosphorylation and glycation of Tau protein enhance but do not trigger fibrillization in vitro. J Biol Chem 279: 49694-49703.
34. Obrenovich ME, Monnier VM (2004) Glycation stimulates amyloid formation. Sci. Aging Knowledge Environ 2004: pe3.
35. Vitek MP, Bhattacharya K, Glendening JM, Stopa E, Vlassara H, et al. (1994) Advanced glycation end products contribute to amyloidosis in Alzheimer disease. Proc Natl Acad Sci USA 91: 4766-4770.
36. Shaikh S, Nicholson LF (2008) Advanced glycation end products induce in vitro cross-linking of alpha-synuclein and accelerate the process of intracellular inclusion body formation. J Neurosci Res 86: 2071-2082.
37. Woltjer RL, Maezawa I, Ou JJ, Montine KS, Montine TJ (2003) Advanced glycation endproduct precursor alters intracellular amyloid-beta/A beta PP carboxy-terminal fragment aggregation and cytotoxicity. J Alzheimers Dis 5: 467-476.
38. Oliveira LM, Lages A, Gomes RA, Neves H, Família C, et al. (2011) Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formation. BMC Biochemistry 12: 41.
39. Kong FL, Cheng W, Chen J, Liang Y (2011) d-Ribose glycates β(2)-microglobulin to form aggregates with high cytotoxicity through a ROS-mediated pathway. Chem Biol Interact 194: 69-78.
40. Wei Y, Chen L, Chen J, Ge L, He R (2009) Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells. BMC Cell Biol 10: 10.
41. Chen L, Wei Y, Wang X, He R (2009) D-Ribosylated Tau forms globular aggregates with high cytotoxicity. Cell Mol Life Sci 66: 2559-2571.
42. Chen L, Wei Y, Wang X, He R (2010) Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products. PLoS One 5: e9052.
43. Nelson DL, Cox MM (2004) Lehninger Principle of Biochemistry 3rd ed., Worth Publishers, New York, America. 297-324.
44. Wei Y, Han CS, Zhou J, Liu Y, Chen L, et al. (2012) D-ribose in glycation and protein aggregation. BBA 1820: 488-494.
45. Johansen MB, Kiemer L, Brunak S (2006) Analysis and prediction of mammalian protein glycation. Glycobiology 16: 844-853.
46. Munanairi A, O'Banion SK, Gamble R, Breuer E, Harris AW, et al. (2007) The multiple Maillard reactions of ribose and deoxyribose sugars and sugar phosphates. Carbohydr Res 342: 2575-2592.
47. Levine H, III (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2: 404-410.
48. Naiki H, Higuchi K, Hosokawa M, Takeda T (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177: 244-249.
49. Cussimanio BL, Booth AA, Todd P, Hudson BG, Khalifah RG (2003) Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophysical Chemistry 105: 743-755.
50. Bokiej M, Livermore AT, Harris AW, Onishi AC, Sandwick RK (2011) Ribose Sugars Generate Interrnal Glycation Cross-links in Horse Heart Myoglobin. Biochem Biophys Res Commun. 407: 191-196.
51. Infusini G, Iannuzzi C, Vilasi S, Birolo L, Pagnozzi D, et al. (2012). Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F. Eur Biophys J 41: 615-627.
52. Infusini G, Iannuzzi C, Vilasi S, Maritato R, Birolo L, et al. (2013) W-F Substitutions in Apomyoglobin Increase the Local Flexibility of the N-terminal Region Causing Amyloid Aggregation: A H/D Exchange Study. Protein Pept Lett 20: 898-904.
53. Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81: 678-699.
54. Li J, Liu D, Sun L, Lu Y, Zhang Z (2012) Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective. Journal of the Neurological Sciences 317: 1-15.
55. Prischi F, Pastore C, Carroni M, Iannuzzi C, Adinolfi S, et al. (2010) Of the vulnerability of orphan complex proteins: the case study of the E. coli IscU and IscS proteins. Protein Expr Purif 73: 161-166.
56. Yan R, Konarev PV, Iannuzzi C, Adinolfi S, Roche B, et al. (2013) Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS. J Biol Chem 288: 24777-24787.
57. Hansen MB, Nielsen SE, Berg K (1989) Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill. J Immunol Methods 119: 203-210.