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 Novel hybrids of oxoisoaporphine-tryptamine as acetylcholinesterase-induced β-amyloid aggregation inhibitors with improved antioxidant properties

2015 ◽  
Vol 80 (2) ◽  
pp. 127-136 ◽  
Author(s):  
Hai-Tao Zhao ◽  
Shu-Ming Zhong ◽  
Jiang-Ke Qin ◽  
Huang Tang
Keyword(s):  
Inhibitory Activity ◽  
Antioxidant Properties ◽  
Drug Candidates ◽  
Ache Inhibitors ◽  
Ache Inhibitory Activity ◽  
Ic50 Values ◽  
Aggregation Inhibitors ◽  
Β Amyloid ◽  
Micromolar Range

A series of dual binding site acetylcholinesterase (AChE) inhibitors have been designed, synthesized, and tested for their antioxidant ability and inhibitory potency on AChE and AChE-induced b-amyloid (Ab) aggregation. The new hybrids consist of a unit of 1-azabenzanthrone and a tryptamine or its derivative, connected through a a,w - alkyldiamide bridge. These hybrids exhibit moderate AChE inhibitory activity with IC50 values in the micromolar range and significant in vitro inhibitory activity toward the AChE-induced Ab aggregation. Moreover, six out of the nine hybrids of this series exhibit a higher oxygen radical absorbance capacity than trolox, which makes them promising anti-Alzheimer drug candidates.

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