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Interaction between Aβ(1−42) and Aβ(1−40) in Alzheimer's β-Amyloid Fibril Formation in Vitro
Abstract
We analyzed the interaction of two kinds of amyloid beta-peptides (A beta), i.e., A beta(1-42) and A beta(1-40), in the kinetics of beta-amyloid fibril (fA beta) formation in vitro, based on a nucleation-dependent polymerization model using fluorescence spectroscopy with thioflavin T. When 25 microM A beta(1-42) was incubated with increasing concentrations of amyloidogenic A beta(1-40), the time to proceed to equilibrium was extended dose-dependently. A similar inhibitory effect was observed when 45 microM A beta(1-40) was incubated with increasing concentrations of A beta(1-42). On the other hand, when 50 microM of nonamyloidogenic A beta(1-40) was incubated with A beta(1-42) at a molar ratio of 10:1 or 5:1, A beta(1-42) initiated fA beta formation from A beta(1-40). The lag time of the reaction shortened in a concentration-dependent manner, with A beta(1-42). We next examined the seeding effect of fA beta formed from A beta(1-42) (fA beta(1-42)) on nonamyloidogenic A beta(1-40). When 50 microM of nonamyloidogenic A beta(1-40) was incubated with 10 or 20 microg/mL (2.2 or 4.4 microM) of fA beta(1-42), the fluorescence showed a sigmoidal increase. The lag time of the reaction was shortened by fA beta(1-42) in a concentration-dependent manner. However, the time to proceed to equilibrium was much longer than when an equal concentration of fA beta formed from A beta(1-40) (fA beta(1-40)) was added to A beta(1-40). The fluorescence increased hyperbolically without a lag phase whe…
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“In vitro biophysical studies of synthetic Aβ demonstrate that Aβ42 aggregates more readily than Aβ40, presumably because Aβ42 nucleates more efficiently.”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Hasegawa et al., 1999
In the citing paper
“Following nucleation, there seems to be little kinetic or thermodynamic differences between elongation of fibrils composed of either Aβ40 or Aβ42 (Hasegawa et al., 1999; Jarrett et al., 1993; Jarrett and Lansbury, 1993).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Hasegawa et al., 1999
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- Abbreviations Aβ, amyloid β-peptides
Cited by
Sorted by citations
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Ono, K., Hasegawa, K., Naiki, H., & Yamada, M. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20025 · Cited by 1,254
Self-citationThe 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Opposing activities protect against age-onset proteotoxicity
Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843
Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565
β-Synuclein Inhibits α-Synuclein Aggregation
Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E. (2001) · Neuron · doi:10.1016/s0896-6273(01)00462-7 · Cited by 398
Metadata
- Authors
- Hasegawa, K., Yamaguchi, I., Omata, S., Gejyo, F., & Naiki, H.
- Affiliations
- Department of Pathology, Fukui Medical University, Fukui 910-1193, Japan, Department of Biosystem Science, Graduate School of Science and Technology, Niigata University, Niigata 950-2181, Japan, and Department of Medicine (II), Niigata University School of Medicine, Niigata 951-8510, Japan
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-11-01
- Volume
- 38
- Issue
- 47
- Pages
- 15514-15521
- ISSN
- 0006-2960
- 1520-4995
- Cited by
- 198
- References
- 1
- Language
- en
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