Brilliant Blue G improves cognition in an animal model of Alzheimer’s disease and inhibits amyloid-β-induced loss of filopodia and dendrite spines in hippocampal neurons

Neuroscience ◽  
2014 ◽  
Vol 279 ◽  
pp. 94-101 ◽  
Author(s):  
X. Chen ◽  
J. Hu ◽  
L. Jiang ◽  
S. Xu ◽  
B. Zheng ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Animal Model ◽  
Hippocampal Neurons ◽  
Amyloid Β ◽  
Brilliant Blue ◽  
Brilliant Blue G ◽  
Model Of Alzheimer’S Disease

scholarly journals miRNA-31 Improves Cognition and Abolishes Amyloid-β Pathology by Targeting APP and BACE1 in an Animal Model of Alzheimer’s Disease

2020 ◽  
Vol 19 ◽  
pp. 1219-1236 ◽  
Author(s):  
Ana Teresa Barros-Viegas ◽  
Vítor Carmona ◽  
Elisabete Ferreiro ◽  
Joana Guedes ◽  
Ana Maria Cardoso ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Animal Model ◽  
Amyloid Β ◽  
Model Of Alzheimer’S Disease

scholarly journals Galectin-1 improves cognition and reduces amyloid-β deposits in an animal model of Alzheimer's disease possibly by modulating microglia phenotype and increasing Aβ clearance

IBRO Reports ◽  
2019 ◽  
Vol 6 ◽  
pp. S477
Author(s):  
Jessica Lorena Presa ◽  
Carlos Pomilio ◽  
Angeles Vinuesa ◽  
Melisa Bentivegna ◽  
Agustina Alaimo ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Animal Model ◽  
Amyloid Β ◽  
Model Of Alzheimer’S Disease ◽  
Aβ Clearance

Actions of the Anti-Angiogenic Compound Angiostatin in an Animal Model of Alzheimer’s Disease

2013 ◽  
Vol 10 (3) ◽  
pp. 252-260 ◽  
Author(s):  
Jae K Ryu ◽  
Jonathan P Little ◽  
Andis Klegeris ◽  
Nattinee Jantaratnotai ◽  
James G McLarnon
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Animal Model ◽  
Model Of Alzheimer’S Disease

scholarly journals A Super-Resolved View of the Alzheimer’s Disease-Related Amyloidogenic Pathway in Hippocampal Neurons

2021 ◽  
pp. 1-20
Author(s):  
Yang Yu ◽  
Yang Gao ◽  
Bengt Winblad ◽  
Lars Tjernberg ◽  
Sophia Schedin Weiss
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Hippocampal Neurons ◽  
Three Dimensional ◽  
Amyloid Β ◽  
Stimulated Emission ◽  
Amyloid Β Peptide ◽  
Primary Neurons ◽  
Amyloid Β Protein ◽  
Early Endosomes

Background: Processing of the amyloid-β protein precursor (AβPP) is neurophysiologically important due to the resulting fragments that regulate synapse biology, as well as potentially harmful due to generation of the 42 amino acid long amyloid β-peptide (Aβ 42), which is a key player in Alzheimer’s disease. Objective: Our aim was to clarify the subcellular locations of the amyloidogenic AβPP processing in primary neurons, including the intracellular pools of the immediate substrate, AβPP C-terminal fragment (APP-CTF) and the product (Aβ 42). To overcome the difficulties of resolving these compartments due to their small size, we used super-resolution microscopy. Methods: Mouse primary hippocampal neurons were immunolabelled and imaged by stimulated emission depletion (STED) microscopy, including three-dimensional, three-channel imaging and image analyses. Results: The first (β-secretase) and second (γ-secretase) cleavages of AβPP were localized to functionally and distally distinct compartments. The β-secretase cleavage was observed in early endosomes, where we were able to show that the liberated N- and C-terminal fragments were sorted into distinct vesicles budding from the early endosomes in soma. Lack of colocalization of Aβ 42 and APP-CTF in soma suggested that γ-secretase cleavage occurs in neurites. Indeed, APP-CTF was, in line with Aβ 42 in our previous study, enriched in the presynapse but absent from the postsynapse. In contrast, full-length AβPP was not detected in either the pre- or the postsynaptic side of the synapse. Furthermore, we observed that endogenously produced and endocytosed Aβ 42 were localized in different compartments. Conclusion: These findings provide critical super-resolved insight into amyloidogenic AβPP processing in primary neurons.

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