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ABeta is formed from sequential cleavage of the Amyloid precursor protein. This protein is expressed as an integral membrane protein but its role is unknown. The most plausible current explanation is that it is used in synaptic formation and anterograde neuronal transport.
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We observed that once a small but critical concentration of Aβ42 aggregates has been generated through primary nucleation of monomers, surface-catalyzed secondary nucleation becomes the dominant process, whereby the surfaces of the fibrils once formed serve as catalytic sites for the generation of toxic oligomeric species .
beta-amyloid — were the cause of nerve cell toxicity in Alzheimer's, researchers now believe that small, soluble aggregates of beta-amyloid may be more toxic. What is beta-amyloid? Beta-amyloid is a small piece of a larger protein called "amyloid precursor protein" (APP).
Oligomer-specific Aβ toxicity in cell models is mediated by selective uptake. ... Oligomeric Aβ 1–42 is internalized by an endocytic process and is transported to the lysosomes. Inhibition of uptake specifically inhibits oligomer but not fibril toxicity. ... Materials and methods2.1. Antibodies and reagents
These studies have not only demonstrated a critical role of LRP1 in abeta clearance but have also highlighted the importance of various brain cell types, including neurons, glia, smooth muscle cells and pericytes, in the process of brain abeta clearance.
The team at IRB Barcelona has studied the aggregation of two of the most common variants of Abeta, namely Abeta 40 and Abeta 42, with 40 and 42 amino acids, respectively, the latter being the variant most closely associated with Alzheimer's disease.
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A dilution of the sample would help, but of course you would also dilute the concentration and effectiveness of IDE and the concentration of Abeta, which would slow down the aggregation process ...
The fast aggregation process, rapid conformational changes as well as solvent effects provide challenges in measuring monomeric and oligomeric amyloid peptide structures in solution. Theoretical and computational studies complement experiments and provide insights that are otherwise difficult to obtain using conventional experimental tools.
As observed by DLS, SEC and SAXS, the composition of the soluble material is different between the two pre-treatments (HFIP Aβ 42 has higher molecular weight aggregates compared with the NH 4 OH material). The HFIP pretreated Aβ 42 had a faster propensity to aggregate in the ThT assay .
Amyloid beta peptide (Aβ) is the main component of extraneuronal senile plaques typical of Alzheimer's disease (AD) brains. ... (early and late endosomes, lysosomes and autolysosomes) as well as to cellular structures associated with related process of protein secretion (such as Golgi-derived secretory vesicles and synaptic vesicles) using ...
The study showed for the first time that in this clustered form, beta-amyloid can bind strongly to a receptor on nerve cells, setting in motion an intercellular process that erodes their synapses with other nerve cells. Synapses are the connections between nerve cells.
In addition, interactions between the Abeta peptide and GM1 enhanced the conversion of the peptide to its more toxic beta-strand form. Our observations suggest a mechanism by which Abeta is released from membranes, a process in the Abeta aggregation pathway that has previously been uncharacterized.
BACKGROUND: How beta-amyloid (Abeta) and tau exert toxicity in Alzheimer's disease is only partly understood. Major questions include (1) which aggregation state of Abeta confers toxicity, (2) do ...
The beta amyloid (Abeta) protein is a key molecule in the pathogenesis of Alzheimer's disease (AD). The tendency of the Abeta peptide to aggregate, its reported neurotoxicity, and genetic linkage studies, have led to a hypothesis of AD pathogenesis that many …
Proteolytic processing of the amyloid precursor protein (APP) generates amyloid beta (Abeta) peptide, which is thought to be causal for the pathology and subsequent cognitive decline in Alzheimer's disease.
RO4929097 is a γ secretase inhibitor with IC50 of 4 nM in a cell-free assay, inhibiting cellular processing of Aβ40 and Notch with EC50 of 14 nM and 5 nM, respectively. Phase 2. Hepatology, 2015, 10.1002/hep.28367 Nat Commun, 2016, 7:13616 ... and cell viability was assessed by CellTiter-Blue assay as described in Materials and Methods. The ...
Read "Structural basis for amyloid beta binding to neuronal cells, Alzheimer's and Dementia" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips. ... There are studies suggesting that cellular membranes play a major role in Abeta oligomerization process and ...
Erythropoietin prevents PC12 cells from beta-amyloid-induced apoptosis via PI3K⁄Akt pathway
You can vary your experiments, for instance by having Abeta aggregate WITH your interesting protein for 24 hours and adding the entire mixture to the cells, or letting your Abeta aggregate, add it ...
Abeta aggregates into fibrils, but rather than these end-products of the aggregation process, intermediate species, referred to as oligomers, have been identified as the most neurotoxic Abeta aggregates.
The rest of the disease process, including formation of neurofibrillary tangles containing tau protein, is proposed to result from an imbalance between Abeta production and Abeta clearance." ... Why Amyloid beta aggregates: "The salt bridge between Asp23 and Lys28" ... "Amyloid-beta(Aβ or Abeta) denotes peptidesof 36–43 amino ...
Alzheimer's disease (AD) pathogenesis is widely believed to be driven by the production and deposition of the β-amyloid peptide (Aβ). For many years, investigators have been puzzled by the weak to nonexistent correlation between the amount of neuritic plaque pathology in the human brain and the degree of clinical dementia.
In the nucleation phase, monomers undergo conformational changes and self-associate to form oligomeric nuclei that are rich in β-sheets. Once the nucleus is formed, assembly of larger aggregates and fibril elongation, a much more favourable process and proceeds rapidly.
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Amyloid beta is commonly thought to be intrinsically unstructured, meaning that in solution it does not acquire a unique tertiary fold but rather populates a set of structures. As such, it cannot be crystallized and most structural knowledge on amyloid beta comes from NMR and molecular dynamics.
how to process abeta agrregates - Abeta immunotherapy leads to clearance of early, but not . The present results show that in a transgenic model of Alzheimer's disease (AD), clearance of Abeta early ...