Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

Chemistry and Biology

Volumn 4, Issue 2, 1997, Pages 119-125

  Harper, James D ^a,b   Wong, Stanislaus S ^c   Lieber, Charles M ^c   Lansbury Jr , Peter T ^b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c HARVARD UNIVERSITY   (United States)

Author keywords

amyloid; atomic force microscopy; protofibril

Indexed keywords

AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; ARTICLE; ATOMIC FORCE MICROSCOPY; BRAIN LEVEL; CHEMISTRY; HUMAN; METHODOLOGY; PATHOLOGY;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; BRAIN CHEMISTRY; HUMANS; MICROSCOPY, ATOMIC FORCE;

EID: 0030614627     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90255-6     Document Type: Article

References (32)

1. Selkoe, D. (1995). Deciphering Alzheimer's disease: molecular genetics and cell biology yield major clues. J. NIH Research 7, 57-64.
2. Lorenzo, A. & Yankner, B.A. (1994). β amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91 12243-12247.
3. El Khoury, J., Hickman, S.E., Thomas, C.A., Cao, L., Silverstein, S.C. & Lokie, J.D.-(1996). Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils. Nature 382, 716-719.
4. Hsiao, K., et al., & Cole, G. (1996). Correlative memory defects, Aβ elevation, and amyloid plaques in transgenic mice. Science 274, 99-102.
5. Lansbury, P.T., Jr (1996). A reductionist view of Alzheimer's disease. Acc. Chem. Res. 29, 317-321.
6. Jarrett, J.T. & Lansbury P.T., Jr (1993). Seeding the 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
7. Jarrett, J.T., Berger, E.P. & Lansbury P.T., Jr (1993). The carboxy terminus of β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697.
8. Schneuner, D., et al., & Younkin, S.G. (1996). Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat. Med. 2, 864-870.
9. Suzuki, N., et al., & Younkin, S.G. (1994). An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (bAPP717) mutants. Science 264, 1336-1340.
10. Borchelt, D.R. et al., & Sisodia, S.S. (1996). Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/Aβ1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013.
11. Citron, M., et al., & Selkoe, D.J. (1997). Mutant presenilins of Alzhcimer's disease increase production of 42-residue amyloid âprotein in both transfected cells and transgenic mice. Nat. Med 3, 1-6.
12. Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nulina, N. & Ihara, Y. (1994). Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 13, 45-53.
13. Lemere, C., et al., & Arango, J.C. (1996). The E280A presenilin 1 mutation leads to a distinct Alzheimer's disease phenotype: increased Aβ42 deposition and severe cerebellar pathology. Nat. Med. 2, 1146-1150.
14. Duff, K., et al., & Younkin, S.G. (1996). Increased amyloid β42(43) in brains of mice expressing mutant presenifin 1. Nature 383, 710-713.
15. Snyder, S.W., et al., & Holzman, T.F. (1994). amyloid β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J. 67, 1216-1228.
16. Soreghan, B., Kosmoski, J. & Glabe, C. (1994). Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation. J. Biol. Chem. 269, 28551-28554.
17. Lomakin, A., Chung, D.S., Benedek, G.B., Kirschner, D.A. & Teplow, D.B. (1996). On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl Acad. Sci. USA 93, 1125-1129.
18. Drake, B., et al., & Hansma, P.K. (1989). Imaging crystals, polymers, and processes in water with the atomic force microscope. Science 243, 1586-1589.
19. Busiamante, C. & Kelier, D. (1995). Scanning force microscopy in biology. Physics Today 48, 32-38.
20. Stine, W.B., et al., & Krafft, G.A. (1996). The nanometer-scale structure of amyloid β visualized by atomic force microscopy. J. Prof. Chem. 15, 193-203.
21. Evans, K.C., Berger, E.P., Cho, C.-G., Weisgraber, K.H. & Lansbury, P.T., Jr (1995), Apolipoprotein E is a kinetic, but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer'a disease. Proc. Natl Acad. Sci. USA 92, 763-767.
22. Fraser, P.E., Duffy, L.K., Nguyen, J., Inouye, H. & Kirschner, D.A. (1991). Morphology and antibody recognition of synthetic β-amyloid peptides. J. Neurosci. Res. 28, 474-485.
23. Lansbury, P.T., Jr, et al., & Griffin, R.G. (1995). Structural model of the β amyloid fibril: interstrand alignment of an antiparallel β sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2, 990-998.
24. Halverson, K., Fraser, P.E., Kirschner, D. A. & Lansbury, P.T., Jr (1990). Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry 29, 2639-2644.
25. Blake, C.C.F. & Serpell, L (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4, 989-998.
26. Serpell, L.C., et al., & Blake, C.C.F. (1995), Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254, 113-118.
27. Fraser, P.E., Nguyen, J.T., Surewicz, W.K. & Kirschner, D.A. (1991). pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys. J. 60, 1190-1201.
28. Selkoe, D.J. (1994). Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17, 489-517.
29. Chan, W., Fornwald, M., Brawner, M. & Wetzel, R. (1996). Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ. Biochemistry 35, 7123-7130.
30. Corder, E.H., et al., & Perciak-Vance, M.A. (1993). Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261, 921-923.
31. Maggio, J.E., et al., & Mantyh, P.W. (1992). Reversible in vitro growth of Alzheimer disease β-amyloid plaques by deposition of labeled amyloid peptide. Prod. Nat. Acad. Sci. USA 89, 5462-5466.
32. Naiki, H. & K. Nakakuki. (1996). First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab. Invest. 74, 374-383.