The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural Transitions Associated with the Interaction of Alzheimer β-Amyloid Peptides with Gangliosides
Open accessAbstract
Alzheimer's disease is characterized pathologically by the presence of neurofibrillary tangles and amyloid plaques. The principal component of the plaque is the beta-amyloid peptide (Abeta), a 39-43-residue peptide. The conformational change required for the conversion of soluble peptide into amyloid fibrils is modulated by pH, Abeta concentration, addition of kinetic and thermodynamic enhancers, and alterations in the primary sequence of Abeta. We report here the ability of gangliosides to induce an alpha-helical structure in Abeta and thereby diminish fibrillogenesis. Circular dichroism and a fluorescence dye release assay data indicate that gangliosides interact with and induce alpha-helix formation in Abeta. We find that the sialic acid moiety of gangliosides is necessary for the induction of alpha-helical structure. Differences in the amount and the position of the sialic acid on the carbohydrate backbone also affect the conformational switch. The Abeta-ganglioside interaction at pH 7.0, monitored by CD, is stable over time and resistant to high concentrations of NaCl. The induction of alpha-helical structure is greater with Abeta1-40 than Abeta1-42. The ability of gangliosides to sequester Abeta from fibril formation was also evaluated by electron microscopy.
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Cites
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Evans, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., & Lansbury, P. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.763 · Cited by 333
Cited by
Kakio, A., Nishimoto, S.-I., Yanagisawa, K., Kozutsumi, Y., & Matsuzaki, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100252200 · Cited by 406
GM1 Specifically Interacts with α-Synuclein and Inhibits Fibrillation
Martinez, Z., Zhu, M., Han, S., & Fink, A. L. (2007) · Biochemistry · doi:10.1021/bi061749a · Cited by 260
McLaurin, J., Franklin, T., Zhang, X., Deng, J., & Fraser, P. E. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00957.x · Cited by 258
Self-citationElimination of GD3 synthase improves memory and reduces amyloid-β plaque load in transgenic mice
Bernardo, A., Harrison, F. E., McCord, M., Zhao, J., Bruchey, A., Davies, S. S., Jackson Roberts, L., Mathews, P. M., Matsuoka, Y., Ariga, T., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.12.022 · Cited by 127
Insulin resistance: a connecting link between Alzheimer's disease and metabolic disorder
Kshirsagar, V., Thingore, C., & Juvekar, A. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-020-00622-2 · Cited by 66
Metadata
- Authors
- McLaurin, J., Franklin, T., Fraser, P. E., & Chakrabartty, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-02
- Volume
- 273
- Issue
- 8
- Pages
- 4506-4515
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2121890455
- Cited by
- 188
- References
- 2
- FWCI
- 5.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- McLaurin, J., Franklin, T., Fraser, P. E., & Chakrabartty, A. (1998). Structural Transitions Associated with the Interaction of Alzheimer β-Amyloid Peptides with Gangliosides. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.8.4506
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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