2006
DOI: 10.1074/jbc.m606072200
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Real-time and Single Fibril Observation of the Formation of Amyloid β Spherulitic Structures

Abstract: In Alzheimer disease, amyloid ␤, a 39 -43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we … Show more

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Cited by 74 publications
(100 citation statements)
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“…For example, if fibrils become nucleated on the surface of a preexisting fibril (38), it is possible that the seed partially orients the daughter filament. Furthermore, total internal reflection fluorescence microscopy revealed the outgrowth of amyloidlike fibrils in vitro and the formation of fibril bundles due to fibril branching reactions (39) or the formation of star-like spherulites due to a radial extension of fibrils from a seed (40,41).…”
Section: Discussionmentioning
confidence: 99%
“…For example, if fibrils become nucleated on the surface of a preexisting fibril (38), it is possible that the seed partially orients the daughter filament. Furthermore, total internal reflection fluorescence microscopy revealed the outgrowth of amyloidlike fibrils in vitro and the formation of fibril bundles due to fibril branching reactions (39) or the formation of star-like spherulites due to a radial extension of fibrils from a seed (40,41).…”
Section: Discussionmentioning
confidence: 99%
“…We previously reported the amyloid fibrillation of A␤- in real time at a single fibrillar level at pH 7.0 with TIRFM combined with the use of ThT (62). We used the surfaces of various chemically modified substrates.…”
Section: Discussionmentioning
confidence: 99%
“…In previous reports, the Aβ aggregation was induced on the negatively charged surface owing to the repulsion to the net charge of Aβ and the electrostatic interaction to the positive residues in Aβ [23,26,27]. The results corresponded to the Aβ amyloidosis on the cell surfaces.…”
Section: Formation Of Aβ Fibrils On Various Saccharide Surfacesmentioning
confidence: 97%
“…In addition, since Aβ has a negative net charge, the interactions of Aβ with 6-sulfo-GlcNAc and sialic acid were affected by the electrostatic repulsion [23]. Actually, the amyloidosis of Aβ on the cell surfaces is affected not only by saccharide-Aβ interaction, but also by many other interactions such as Aβ-Aβ, Aβ-protein (other proteins) and electrostatic interaction [23,24]. Therefore, the amyloidosis of Aβ on the cell surfaces was not fully understood from the results of our simple experiments.…”
Section: Conformation Analyses Of Aβ On Saccharide Surfacesmentioning
confidence: 99%