AIP-1 ameliorates β-amyloid peptide toxicity in a Caenorhabditis elegans Alzheimer's disease model

AbstractAlzheimer’s disease (AD) is a neurological disease caused by the accumulation of extracellular senile plaques consisting of β-amyloid peptide (Aβ) in the brain. A transgenic Caenorhabditis elegans which demonstrated paralysis due to the expression of human beta amyloid Aβ42 gene was used to study the anti-paralysis effect of mixed tocotrienols. The content of the mixed tocotrienols were 12.1% α-, 2.7% β-, 18.6% γ-, and 8.1% δ-tocotrienols. Mixed tocotrienols significantly delayed the Aβ-induced paralysis in the transgenic nematode and exhibited anti-oxidant properties towards Aβ-generated oxidative stress. The mixture also presented potent inhibitory activities against Aβ aggregation with an IC50 value of 600 ng/ml. It is concluded that mixed tocotrienols could potentially serve as a new therapeutic candidate for AD.

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Strength training and running elicit different neuroprotective outcomes in a β-amyloid peptide-mediated Alzheimer's disease model

Physiology & Behavior ◽

10.1016/j.physbeh.2019.04.012 ◽

2019 ◽

Vol 206 ◽

pp. 206-212 ◽

Cited By ~ 5

Author(s):

Helen L. Schimidt ◽

Alexandre Garcia ◽

Ivan Izquierdo ◽

Pâmela B. Mello-Carpes ◽

Felipe P. Carpes

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Strength Training ◽

Disease Model ◽

Amyloid Peptide ◽

Β Amyloid ◽

Β Amyloid Peptide

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Alzheimer's disease drug discovery: in vivo screening using Caenorhabditis elegans as a model for β-amyloid peptide-induced toxicity

Drug Discovery Today Technologies ◽

10.1016/j.ddtec.2012.02.002 ◽

2013 ◽

Vol 10 (1) ◽

pp. e115-e119 ◽

Cited By ~ 53

Author(s):

A.L. Lublin ◽

C.D. Link

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Drug Discovery ◽

Caenorhabditis Elegans ◽

Amyloid Peptide ◽

In Vivo Screening ◽

Β Amyloid ◽

Β Amyloid Peptide

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Peptide multifunctionalized gold nanorods decrease toxicity of β-amyloid peptide in a Caenorhabditis elegans model of Alzheimer's disease

Nanomedicine Nanotechnology Biology and Medicine ◽

10.1016/j.nano.2017.06.013 ◽

2017 ◽

Vol 13 (7) ◽

pp. 2341-2350 ◽

Cited By ~ 22

Author(s):

Francisco Morales-Zavala ◽

Hector Arriagada ◽

Natalia Hassan ◽

Carolina Velasco ◽

Ana Riveros ◽

...

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Caenorhabditis Elegans ◽

Gold Nanorods ◽

Amyloid Peptide ◽

Model Of Alzheimer’S Disease ◽

Β Amyloid ◽

Β Amyloid Peptide

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Pentapeptide Amides Interfere with the Aggregation of β-Amyloid Peptide of Alzheimer's Disease

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.2002.6745 ◽

2002 ◽

Vol 292 (4) ◽

pp. 931-936 ◽

Cited By ~ 39

Author(s):

Csaba Hetényi ◽

Zoltán Szabó ◽

Éva Klement ◽

Zsolt Datki ◽

Tamás Körtvélyesi ◽

...

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Amyloid Peptide ◽

Β Amyloid ◽

Β Amyloid Peptide

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Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease

The Journal of Cell Biology ◽

10.1083/jcb.200505082 ◽

2005 ◽

Vol 171 (1) ◽

pp. 87-98 ◽

Cited By ~ 590

Author(s):

W. Haung Yu ◽

Ana Maria Cuervo ◽

Asok Kumar ◽

Corrinne M. Peterhoff ◽

Stephen D. Schmidt ◽

...

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Cell Survival ◽

Mammalian Target Of Rapamycin ◽

Amyloid Peptide ◽

Survival Pathways ◽

Secretase Activity ◽

Amyloid Aβ ◽

Β Amyloid ◽

Β Amyloid Peptide

Macroautophagy, which is a lysosomal pathway for the turnover of organelles and long-lived proteins, is a key determinant of cell survival and longevity. In this study, we show that neuronal macroautophagy is induced early in Alzheimer's disease (AD) and before β-amyloid (Aβ) deposits extracellularly in the presenilin (PS) 1/Aβ precursor protein (APP) mouse model of β-amyloidosis. Subsequently, autophagosomes and late autophagic vacuoles (AVs) accumulate markedly in dystrophic dendrites, implying an impaired maturation of AVs to lysosomes. Immunolabeling identifies AVs in the brain as a major reservoir of intracellular Aβ. Purified AVs contain APP and β-cleaved APP and are highly enriched in PS1, nicastrin, and PS-dependent γ-secretase activity. Inducing or inhibiting macroautophagy in neuronal and nonneuronal cells by modulating mammalian target of rapamycin kinase elicits parallel changes in AV proliferation and Aβ production. Our results, therefore, link β-amyloidogenic and cell survival pathways through macroautophagy, which is activated and is abnormal in AD.

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