Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters
Author
Source
International Journal of Alzheimer's Disease
Issue
Vol. 2011, Issue 2011 (31 Dec. 2011), pp.1-7, 7 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2011-01-13
Country of Publication
Egypt
No. of Pages
7
Main Subjects
Abstract EN
It is widely accepted that the conversion of the soluble, nontoxic amyloid β-protein (Aβ) monomer to aggregated toxic Aβ rich in β-sheet structures is central to the development of Alzheimer’s disease.
However, the mechanism of the abnormal aggregation of Aβ in vivo is not well understood.
Accumulating evidence suggests that lipid rafts (microdomains) in membranes mainly composed of sphingolipids (gangliosides and sphingomyelin) and cholesterol play a pivotal role in this process.
This paper summarizes the molecular mechanisms by which Aβ aggregates on membranes containing ganglioside clusters, forming amyloid fibrils.
Notably, the toxicity and physicochemical properties of the fibrils are different from those of Aβ amyloids formed in solution.
Furthermore, differences between Aβ-(1–40) and Aβ-(1–42) in membrane interaction and amyloidogenesis are also emphasized.
American Psychological Association (APA)
Matsuzaki, Katsumi. 2011. Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters. International Journal of Alzheimer's Disease،Vol. 2011, no. 2011, pp.1-7.
https://search.emarefa.net/detail/BIM-511211
Modern Language Association (MLA)
Matsuzaki, Katsumi. Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters. International Journal of Alzheimer's Disease No. 2011 (2011), pp.1-7.
https://search.emarefa.net/detail/BIM-511211
American Medical Association (AMA)
Matsuzaki, Katsumi. Formation of Toxic Amyloid Fibrils by Amyloid β-Protein on Ganglioside Clusters. International Journal of Alzheimer's Disease. 2011. Vol. 2011, no. 2011, pp.1-7.
https://search.emarefa.net/detail/BIM-511211
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-511211