The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides

FEBS Letters

Volumn 581, Issue 6, 2007, Pages 1161-1165

  Liao, M Q ^a   Tzeng, Y J ^a   Chang, Lea Y X ^a   Huang, H B ^b   Lin, T H ^c   Chyan, C L ^d   Chen, Y C ^a  

^a TZU CHI UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

^c TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

^d NATIONAL DONG HWA UNIVERSITY   (Taiwan)

Author keywords

A ; Aggregation; Neurotoxicity; Secondary structure

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[25-35];

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HYDROPHOBICITY; NERVE CELL NECROSIS; NEUROTOXICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; RAT; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; ANIMALS; CELL SURVIVAL; DIMERIZATION; HUMANS; NEUROTOXICITY SYNDROMES; PC12 CELLS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; RATS; SEQUENCE DELETION;

EID: 33947182575     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.026     Document Type: Article

References (25)

1. Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron 6 (1991) 487-498
2. Tanzi R.E., Bird E.D., Latt S.A., and Neve R.L. The amyloid beta protein gene is not duplicated in brains from patients with Alzheimer's disease. Science 238 (1987) 666-669
3. Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A., Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y., Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A., Biere A.L., Curran E., Burgess T., Louis J.C., Collins F., Treanor J., Rogers G., and Citron M. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286 (1999) 735-741
4. Li Y.M., Xu M., Lai M.T., Huang Q., Castro J.L., DiMuzio-Mower J., Harrison T., Lellis C., Nadin A., Neduvelil J.G., Register R.B., Sardana M.K., Shearman M.S., Smith A.L., Shi X.P., Yin K.C., Shafer J.A., and Gardell S.J. Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405 (2000) 689-694
5. Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., and Teplow D.B. The role of APP processing and trafficking pathways in the formation of amyloid beta-protein. Proc. Natl. Acad. Sci. USA 93 (1996) 1125-1129
6. Dahlgren K.N., Manelli A.M., Stine W., Baine J., Baker L.K., Krafft G.A., and LaDu M.J. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 277 (2002) 32046-32053
7. Gowing E., Roher A.E., Woods A.S., Cotter R.J., Chaney M., Little S.P., and Ball M.J. Chemical characterization of Aβ 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. J. Biol. Chem. 269 (1994) 10987-10990
8. Kubo T., Nishimura S., Kumagae Y., and Kaneko I. In vivo conversion of racemized beta-amyloid ([d-Ser26]Aβ1-40) to truncated and toxic fragments ([d-Ser26]Aβ25-35/40) and fragment presence in the brains of Alzheimer's patients. J. Neurosci. Res. 70 (2002) 474-483
9. Jarrett J.T., Berger E.P., and Lansbury Jr. P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
10. Casoli T., Di Stefano G., Delfino A., Solazzi M., Fattoretti P., Bertoni-Freddari C., Guidi M., Scarpino O., Giunta S., and Galeazzi L. Beta-amyloid fragment 25-35 selectively damages platelets from patients with Alzheimer's disease. Ann. NY Acad. Sci. 977 (2002) 296-302
11. Monji A., Utsumi H., Ueda T., Imoto T., Yoshida I., Hashioka S., Tashiro K., and Tashiro N. Amyloid-beta-protein (Aβ) (25-35)-associated free radical generation is strongly influenced by the aggregational state of the peptides. Life Sci. 70 (2002) 833-841
12. Liu R., McAllister C., Lyubchenko Y., and Sierks M.R. Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation. J. Neurosci. Res. 75 (2004) 162-171
13. Hansen M.B., Nielsen S.E., and Berg K. Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill. J. Immunol. Meth. 1119 (1989) 203-212
14. LeVine III H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
15. Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) 668-673
16. Lobley A., Whitmore L., and Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18 (2002) 211-212
17. Compton L.A., and Johnson Jr. W.C. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155 (1986) 155-167
18. Mao D., Wachter T.A., and Wallace B.A. Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. Biochemistry 21 (1982) 4960-4968
19. Hensley K., Carney J.M., Mattson M.P., Aksenova M., Harris M., Wu J.F., Floyd R.A., and Butterfield D.A. A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Natl. Acad. Sci. USA 91 (1994) 3270-3274
20. Yan S.D., Chen X., Fu J., Chen M., Zhu H., Roher A., Slattery T., Zhao L., Nagashima M., Morser J., Migheli A., Nawroth P., Stern D., and Schmidt A.M. RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature 382 (1996) 685-691
21. Miklossy J., Taddei K., Martins R., Escher G., Kraftsik R., Pillevuit O., Lepori D., and Campiche M. Alzheimer disease: curly fibers and tangles in organs other than brain. J. Neuropathol. Exp. Neurol. 58 (1999) 803-814
22. Chen Y.R., Huang H.B., Chyan C.L., Shiao M.S., Lin T.H., and Chen Y.C. The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy. J. Biochem. 139 (2006) 733-740
23. Davis J., and van Nostrand W.E. Enhanced pathologic properties of Dutch-type mutant amyloid β-protein. Proc. Natl. Acad. Sci. USA 93 (1996) 2996-3000
24. Serpell L.C., and Smith J.M. Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid. J. Mol. Biol. 299 (2000) 225-231
25. Selkoe D.J. Cell biology of the amyloid β-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10 (1994) 373-403