scholarly journals Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro

2004 ◽  
Vol 1690 (3) ◽  
pp. 193-202 ◽  
Author(s):  
Kenjiro Ono ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
Masahito Yamada
Keyword(s):  
Tannic Acid ◽  
Amyloid Fibrils ◽  
Β Amyloid

Inhibitory activity of stilbenes on Alzheimer’s β-amyloid fibrils in vitro

2007 ◽  
Vol 15 (2) ◽  
pp. 1160-1167 ◽  
Author(s):  
Céline Rivière ◽  
Tristan Richard ◽  
Lysiane Quentin ◽  
Stéphanie Krisa ◽  
Jean-Michel Mérillon ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Amyloid Fibrils ◽  
Β Amyloid

Nicotine breaks down preformed Alzheimer’s β-amyloid fibrils in vitro

2002 ◽  
Vol 52 (9) ◽  
pp. 880-886 ◽  
Author(s):  
Kenjiro Ono ◽  
Kazuhiro Hasegawa ◽  
Masahito Yamada ◽  
Hironobu Naiki
Keyword(s):  
Amyloid Fibrils ◽  
Β Amyloid

Estrogen has anti-amyloidogenic effects on Alzheimer’s β-amyloid fibrils in vitro

2007 ◽  
Vol 359 (3) ◽  
pp. 697-702 ◽  
Author(s):  
Akiyoshi Morinaga ◽  
Mie Hirohata ◽  
Kenjiro Ono ◽  
Masahito Yamada
Keyword(s):  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals CD36 Mediates the Innate Host Response to β-Amyloid

2003 ◽  
Vol 197 (12) ◽  
pp. 1657-1666 ◽  
Author(s):  
Joseph B. El Khoury ◽  
Kathryn J. Moore ◽  
Terry K. Means ◽  
Josephine Leung ◽  
Kinya Terada ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Senile Plaques ◽  
Scavenger Receptor ◽  
Intracerebral Injection ◽  
Innate Response ◽  
Macrophage Response ◽  
Class B ◽  
Β Amyloid ◽  
Recognition Receptor

Accumulation of inflammatory microglia in Alzheimer's senile plaques is a hallmark of the innate response to β-amyloid fibrils and can initiate and propagate neurodegeneration characteristic of Alzheimer's disease (AD). The molecular mechanism whereby fibrillar β-amyloid activates the inflammatory response has not been elucidated. CD36, a class B scavenger receptor, is expressed on microglia in normal and AD brains and binds to β-amyloid fibrils in vitro. We report here that microglia and macrophages, isolated from CD36 null mice, had marked reductions in fibrillar β-amyloid–induced secretion of cytokines, chemokines, and reactive oxygen species. Intraperitoneal and stereotaxic intracerebral injection of fibrillar β-amyloid in CD36 null mice induced significantly less macrophage and microglial recruitment into the peritoneum and brain, respectively, than in wild-type mice. Our data reveal that CD36, a major pattern recognition receptor, mediates microglial and macrophage response to β-amyloid, and imply that CD36 plays a key role in the proinflammatory events associated with AD.

scholarly journals Extracellular Hsp90α Detoxifies β-Amyloid Fibrils Through an NRF2 and Autophagy Dependent Pathway

2021 ◽  
Author(s):  
Ayesha Murshid ◽  
Benjamin J Lang ◽  
Thiago J Borges ◽  
Yuka Okusha ◽  
Sachin P Doshi ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Heat Shock Protein 90 ◽  
Microglial Cells ◽  
Related Factor ◽  
Pathological Feature ◽  
Neurotoxic Effects ◽  
Β Amyloid ◽  
Dependent Pathway

We have investigated the role of extracellular Heat shock protein 90 alpha (eHsp90α) in conferring protection of neuronal cells against fibrillary amyloid-beta (f-Aβ1-42) toxicity mediated by microglial cells. The formation of f-Aβ1-42 plaques leads to neurotoxic inflammation, a critical pathological feature of Alzheimer's Disease. We observed increased uptake and clearance of internalized f-Aβ1-42 by microglial cells treated with eHsp90α, an effect associated with activation of NRF2 (NF-E2-related factor 2) - mediated autophagy. eHsp90α thus mitigated the neuronal toxicity of f-Aβ1-42-activated microglia. In addition, eHsp90α facilitated f-Aβ1-42 engulfment by microglial cells in vitro. In summary, eHsp90α triggers NRF2-mediated autophagy in microglia and thus protects against the neurotoxic effects of f-Aβ1-42.

scholarly journals In vitro degradation of β‐amyloid fibrils by microbial keratinase

2019 ◽  
Vol 5 (1) ◽  
pp. 154-163 ◽  
Author(s):  
Debananda S. Ningthoujam ◽  
Saikat Mukherjee ◽  
Laishram Jaya Devi ◽  
Elangbam Shanta Singh ◽  
Keishing Tamreihao ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
In Vitro Degradation ◽  
Β Amyloid

The Anti-Amyloidogenic Effect Is Exerted against Alzheimer's β-Amyloid Fibrils in Vitro by Preferential and Reversible Binding of Flavonoids to the Amyloid Fibril Structure†

Biochemistry ◽  
2007 ◽  
Vol 46 (7) ◽  
pp. 1888-1899 ◽  
Author(s):  
Mie Hirohata ◽  
Kazuhiro Hasegawa ◽  
Shinobu Tsutsumi-Yasuhara ◽  
Yumiko Ohhashi ◽  
Tadakazu Ookoshi ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Reversible Binding ◽  
Fibril Structure ◽  
Β Amyloid

α-Lipoic acid exhibits anti-amyloidogenicity for β-amyloid fibrils in vitro

2006 ◽  
Vol 341 (4) ◽  
pp. 1046-1052 ◽  
Author(s):  
Kenjiro Ono ◽  
Mie Hirohata ◽  
Masahito Yamada
Keyword(s):  
Lipoic Acid ◽  
Amyloid Fibrils ◽  
Β Amyloid

scholarly journals Mechanism of Cellular Formation and In Vivo Seeding Effects of Hexameric β-Amyloid Assemblies

2021 ◽  
Author(s):  
Céline Vrancx ◽  
Devkee M. Vadukul ◽  
Nuria Suelves ◽  
Sabrina Contino ◽  
Ludovic D’Auria ◽  
...  
Keyword(s):  
Cell Lines ◽  
Self Assembly ◽  
Amyloid Fibrils ◽  
Senile Plaques ◽  
Amyloid Peptide ◽  
Cellular Models ◽  
Aβ Aggregation ◽  
Β Amyloid

AbstractThe β-amyloid peptide (Aβ) is found as amyloid fibrils in senile plaques, a typical hallmark of Alzheimer’s disease (AD). However, intermediate soluble oligomers of Aβ are now recognized as initiators of the pathogenic cascade leading to AD. Studies using recombinant Aβ have shown that hexameric Aβ in particular acts as a critical nucleus for Aβ self-assembly. We recently isolated hexameric Aβ assemblies from a cellular model, and demonstrated their ability to enhance Aβ aggregation in vitro. Here, we report the presence of similar hexameric-like Aβ assemblies across several cellular models, including neuronal-like cell lines. In order to better understand how they are produced in a cellular context, we investigated the role of presenilin-1 (PS1) and presenilin-2 (PS2) in their formation. PS1 and PS2 are the catalytic subunits of the γ-secretase complex that generates Aβ. Using CRISPR-Cas9 to knockdown each of the two presenilins in neuronal-like cell lines, we observed a direct link between the PS2-dependent processing pathway and the release of hexameric-like Aβ assemblies in extracellular vesicles. Further, we assessed the contribution of hexameric Aβ to the development of amyloid pathology. We report the early presence of hexameric-like Aβ assemblies in both transgenic mice brains exhibiting human Aβ pathology and in the cerebrospinal fluid of AD patients, suggesting hexameric Aβ as a potential early AD biomarker. Finally, cell-derived hexameric Aβ was found to seed other human Aβ forms, resulting in the aggravation of amyloid deposition in vivo and neuronal toxicity in vitro.

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