Effect of pH on the aggregate formation of a non-amyloid component (1-13)

Journal of Peptide Science

Volumn 9, Issue 3, 2003, Pages 177-186

  Abe, Hiroshi ^a,b   Nakanishi, Hiroshi ^a,b  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

Author keywords

synuclein; Aggregation; Amyloid fibril; Circular dichroism; Conformational conversion; Electron microscopy; NMR; Non amyloid component

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; CARBOXYL GROUP; GLUTAMIC ACID; PEPTIDE FRAGMENT;

ACIDITY; AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); ELECTRON MICROSCOPY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON TRANSPORT; QUANTITATIVE ANALYSIS; SAMPLING; TITRIMETRY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ELECTRON; NERVE TISSUE PROTEINS; NEUROFIBRILLARY TANGLES; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; SOLUBILITY; SOLUTIONS; SYNUCLEINS;

EID: 0037348552     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.444     Document Type: Article

References (27)

1. Kelly JW, Colon W, Lai Z, Lashuel HA, Mcculloch J, Mccutchen SL, Miroy GJ, Peterson SA. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Protein Chem. 1997; 50: 161-181.
2. Carrell RW, Gooptu B. Conformational changes and disease - serpins, prions and Alzheimer's. Curr. Opin. Struct. Biol. 1998; 8: 799-809.
3. Iwai A, Yoshimoto M, Masliah E, Saitoh T. Non-Aβ component of Alzheimer's disease amyloid (NAC) is amyloidogenic. Biochemistry 1995; 34: 10139-10145.
4. El-Agnaf OMA, Jakes R, Curran MD, Middleton D, Ingenito R, Bianchi E, Pessi A, Neill D, Wallace A. Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments. FEBS Lett. 1998; 440: 71-75.
5. El-Agnaf OMA, Bodles AM, Guthrie DJS, Harriott P, Irvine GB. The N-terminal region of non-Aβ component of Alzheimer's disease amyloid is responsible for its tendency to assume β-sheet and aggregate to form fibrils. Eur. J. Biochem. 1998; 258: 157-163.
6. Bodles AM, Guthrie DJS, Harriott P, Campbell P, Irvine GB. Toxicity of non-Aβ component of Alzheimer's disease amyloid, and N-terminal fragments thereof, correlates to formation of β-sheet structure and fibrils. Eur. J. Biochem. 2000; 267: 2186-2194.
7. Ueda K, Fukushima H, Masliah E, Xia Y, Iwai A, Yoshimoto M, Otero DAC, Kondo J, Ihara Y, Saitoh T. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl Acad. Sci. USA 1993; 90: 11282-11286.
8. Han H, Weinreb PH, Lansbury PT Jr. The core Alzheimer's peptide NAC forms amyloid flbrils which seed and are seeded by β-amyloid: is NAC a common trigger or target in neurodegenerative disease? Chem. Biol. 1995; 2: 163-169.
9. Ueda K, Saitoh T, Mori H. Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-Aβ component of Alzheimer's disease amyloid. Biochem. Biophys. Res. Commun. 1994; 205: 1366-1372.
10. Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M. α-synuclein in Lewy bodies. Nature 1997; 388: 839-840.
11. Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, Pike B, Root H, Rubenstein J, Boyer R, Stenroos ES, Chandrasekharappa S, Athanassiadou A, Papapetropoulos T, Johnson WG, Lazzarini AM, Duvoisin RC, Di Iorio G, Golbe LI, Nussbaum RL. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 1997; 276: 2045-2047.
12. Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S, Przuntek H, Epplen JT, Schols L, Riess O. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat Genet. 1998; 2: 106-108.
13. Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB. On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants. Proc. Natl Acad. Sci. USA 1996; 93: 1125-1129.
14. 2-microglobulin and amyloid formation in vitro. Biochemistry 2000; 39: 8735-8746.
15. Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proc. Natl Acad. Sci. USA 1998; 95: 4224-4228.
16. Wood SJ, Maleeff B, Hart T, Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J. Mol. Biol. 1996; 256: 870-877.
17. Fraser PE, Nguyen JT, Surewicz WK, Kirschner DA. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 1991; 60: 1190-1201.
18. Lashuel HA, LaBrenz SR, Woo L, Serpell LC, Kelly JW. Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science. J. Am. Chem. Soc. 2000; 122: 5262-5277.
19. Wüthrich K. NMR of Proteins and Nucleic Acids. Wiley: New York, 1986.
20. Forman-Kay JD, Clore GM, Gronenborn AM. Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 1992; 31: 3442-3452.
21. Fasman GD (ed.). Circular Dichroism and the Conformational Analysis of Biomolecules. Plenum Press: New York, 1996.
22. Jarrett JT, Lansbury PT Jr. Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-1058.
23. Harper JD, Lansbury PT Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 1997; 66: 385-407.
24. Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CCF, Pepys MB. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 1997; 385: 787-793.
25. Baskakov IV, Legname G, Prusiner SB, Cohen FE. Folding of prion protein to its native α-helical conformation is under kinetic control. J. Biol. Chem. 2001; 276: 19687-19690.
26. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid β-protein. Proc. Natl Acad. Sci. USA 1997; 94: 7942-7947.
27. Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000; 289: 1317-1321.