scholarly journals Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Cell ◽  
2013 ◽  
Vol 154 (6) ◽  
pp. 1257-1268 ◽  
Author(s):  
Jun-Xia Lu ◽  
Wei Qiang ◽  
Wai-Ming Yau ◽  
Charles D. Schwieters ◽  
Stephen C. Meredith ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Brain Tissue ◽  
Amyloid Fibrils ◽  
Β Amyloid

Structure of β-amyloid fibrils and its relevance to their neurotoxicity: Implications for the pathogenesis of Alzheimer’s disease

2005 ◽  
Vol 99 (5) ◽  
pp. 437-447 ◽  
Author(s):  
Kazuhiro Irie ◽  
Kazuma Murakami ◽  
Yuichi Masuda ◽  
Akira Morimoto ◽  
Hajime Ohigashi ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals Rescue of cognitive deficits in APP/PS1 mice by accelerating the aggregation of β-amyloid peptide

2019 ◽  
Vol 11 (1) ◽  
Author(s):  
Jian-Xiang Zhang ◽  
Yi-Hui Lai ◽  
Pan-Ying Mi ◽  
Xue-Ling Dai ◽  
Ran Zhang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Brain Tissue ◽  
Amyloid Peptide ◽  
Flavonoid Compound ◽  
Protective Effects ◽  
Behavioral Experiments ◽  
Aβ Oligomers ◽  
Amyloid Aβ ◽  
Β Amyloid

Abstract Background Brain amyloid deposition is one of the main pathological characteristics of Alzheimer’s disease (AD). Soluble oligomers formed during the process that causes β-amyloid (Aβ) to aggregate into plaques are considered to have major neurotoxicity. Currently, drug development for the treatment of Alzheimer’s disease has encountered serious difficulties. Our newly proposed solution is to accelerate the aggregation of Aβ to reduce the amount of cytotoxic Aβ oligomers in brain tissue. This strategy differs from the existing strategy of reducing the total Aβ content and the number of amyloid plaques. Method In this study, we screened a small library and found that a flavonoid compound (ZGM1) promoted the aggregation of β-amyloid (Aβ). We further verified the binding of ZGM1 to Aβ42 using a microscale thermophoresis (MST) assay. Subsequently, we used dot blotting (DB), transmission electron microscopy (TEM), and thioflavin T fluorescence (ThT) measurements to study the aggregation of Aβ under the influence of ZGM1. By using cell experiments, we determined whether ZGM1 can inhibit the cytotoxicity of Aβ. Finally, we studied the protective effects of ZGM1 on cognitive function in APPswe/PS1 mice via behavioral experiments and measured the number of plaques in the mouse brain by thioflavin staining. Results ZGM1 can bind with Aβ directly and mediate a new Aβ assembly process to form reticular aggregates and reduce the amount of Aβ oligomers. Animal experiments showed that ZGM1 can significantly improve cognitive dysfunction and that Aβ plaque deposition in the brain tissue of mice in the drug-administered group was significantly increased. Conclusion Our research suggests that promoting Aβ aggregation is a promising treatment method for AD and deserves further investigation.

β-Amyloid Peptide and Amyloid Precursor Proteins in Olfactory Mucosa of Patients with Alzheimer's Disease, Parkinson's Disease, and down Syndrome

1995 ◽  
Vol 104 (8) ◽  
pp. 655-661 ◽  
Author(s):  
Peter B. Crino ◽  
Barry Greenberg ◽  
John A. Martin ◽  
Virginia M.-Y. Lee ◽  
William D. Hill ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Alzheimer’S Disease ◽  
Parkinson’S Disease ◽  
Alzheimer's Disease ◽  
Parkinson's Disease ◽  
Down Syndrome ◽  
Amyloid Fibrils ◽  
Olfactory Mucosa ◽  
Amyloid Peptide ◽  
Β Amyloid

Dystrophic neurites are present in olfactory epithelium (OE) of patients with Alzheimer's disease (AD), Parkinson's disease (PD), and Down syndrome (DS) and occasionally in normal individuals. Cultured olfactory neuroblasts from AD patients generate carboxy terminal amyloid precursor protein (APP) fragments that contain β-amyloid (Aβ), but it is not known if deposits of Aβ and/or APP fragments occur in the OE of individuals with or without AD, PD, or DS. To determine if Aβ accumulates in the OE in situ, we probed postmortem samples of olfactory mucosa from patients with AD, PD and AD (PD/AD), and DS and AD (DS/AD), as well as from controls, using polyclonal and monoclonal antibodies to Aβ and flanking sequences in APPs. Samples of OE also were examined by thioflavin-S and electron microscopy. Labeling of Aβ was observed in 10 of 12 AD cases, 2 of 3 PD/AD cases, 3 of 4 DS/AD cases, 3 of 10 adult controls, and 4 of 6 fetal cases. The Aβ staining was seen in the basal third of the OE, in axons projecting through the lamina propria, and in metaplastic respiratory epithelium within the OE. Antibodies to other APP domains stained the OE of patients and controls. Thioflavin-S staining was present in the basal third of the OE of 8 of 9 AD patients and several PD/AD and DS/AD patients, but only in rare cells of 3 controls. Electron microscopy did not reveal amyloid fibrils in the OE. These data suggest that deposition of Aβ occurs in a variety of circumstances and is not restricted to patients with AD, PD, or DS.

The load and distribution of β-amyloid in brain tissue of patients with Alzheimer's disease

2001 ◽  
Vol 103 (2) ◽  
pp. 88-92 ◽  
Author(s):  
M. Kraszpulski ◽  
H. Soininen ◽  
S. Helisalmi ◽  
I. Alafuzoff
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Brain Tissue ◽  
Β Amyloid

Imaging β-amyloid fibrils in Alzheimer's disease: a critical analysis through simulation of amyloid fibril polymerization

2005 ◽  
Vol 32 (4) ◽  
pp. 337-351 ◽  
Author(s):  
Kooresh Shoghi-Jadid ◽  
Jorge R. Barrio ◽  
Vladimir Kepe ◽  
Hsiao-Ming Wu ◽  
Gary W. Small ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Critical Analysis ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Β Amyloid
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