Self-Propagative Replication of Aβ Oligomers Suggests Potential Transmissibility in Alzheimer Disease
Identifieur interne : 001A89 ( Main/Curation ); précédent : 001A88; suivant : 001A90Self-Propagative Replication of Aβ Oligomers Suggests Potential Transmissibility in Alzheimer Disease
Auteurs : Amit Kumar [États-Unis] ; Kayla M. Pate [États-Unis] ; Melissa A. Moss [États-Unis] ; Dexter N. Dean [États-Unis] ; Vijayaraghavan Rangachari [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2014.
Descripteurs français
- KwdFr :
- Activation enzymatique, Agrégation pathologique de protéines, Facteur de transcription NF-kappa B (métabolisme), Humains, Lignée cellulaire, Maladie d'Alzheimer (métabolisme), Multimérisation de protéines, Neuroblastome (métabolisme), Peptides bêta-amyloïdes (), Peptides bêta-amyloïdes (métabolisme), Peptides bêta-amyloïdes (pharmacologie), Température.
- MESH :
- métabolisme : Facteur de transcription NF-kappa B, Maladie d'Alzheimer, Neuroblastome, Peptides bêta-amyloïdes.
- pharmacologie : Peptides bêta-amyloïdes.
- Activation enzymatique, Agrégation pathologique de protéines, Humains, Lignée cellulaire, Multimérisation de protéines, Peptides bêta-amyloïdes, Température.
English descriptors
- KwdEn :
- Alzheimer Disease (metabolism), Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (metabolism), Amyloid beta-Peptides (pharmacology), Cell Line, Enzyme Activation, Humans, NF-kappa B (metabolism), Neuroblastoma (metabolism), Protein Aggregation, Pathological, Protein Multimerization, Temperature.
- MESH :
- chemical , chemistry : Amyloid beta-Peptides.
- metabolism : Alzheimer Disease, Amyloid beta-Peptides, NF-kappa B, Neuroblastoma.
- chemical , pharmacology : Amyloid beta-Peptides.
- Cell Line, Enzyme Activation, Humans, Protein Aggregation, Pathological, Protein Multimerization, Temperature.
Abstract
The aggregation of amyloid-β (Aβ) peptide and its deposition in parts of the brain form the central processes in the etiology of Alzheimer disease (AD). The low-molecular weight oligomers of Aβ aggregates (2 to 30 mers) are known to be the primary neurotoxic agents whose mechanisms of cellular toxicity and synaptic dysfunction have received substantial attention in the recent years. However, how these toxic agents proliferate and induce widespread amyloid deposition throughout the brain, and what mechanism is involved in the amplification and propagation of toxic oligomer species, are far from clear. Emerging evidence based on transgenic mice models indicates a transmissible nature of Aβ aggregates and implicates a prion-like mechanism of oligomer propagation, which manifests as the dissemination and proliferation of Aβ toxicity. Despite accumulating evidence in support of a transmissible nature of Aβ aggregates, a clear, molecular-level understanding of this intriguing mechanism is lacking. Recently, we reported the characterization of unique replicating oligomers of Aβ42 (12–24 mers)
Url:
DOI: 10.1371/journal.pone.0111492
PubMed: 25365422
PubMed Central: 4218758
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PMC:4218758Le document en format XML
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<term>Amyloid beta-Peptides (metabolism)</term>
<term>Amyloid beta-Peptides (pharmacology)</term>
<term>Cell Line</term>
<term>Enzyme Activation</term>
<term>Humans</term>
<term>NF-kappa B (metabolism)</term>
<term>Neuroblastoma (metabolism)</term>
<term>Protein Aggregation, Pathological</term>
<term>Protein Multimerization</term>
<term>Temperature</term>
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<term>Agrégation pathologique de protéines</term>
<term>Facteur de transcription NF-kappa B (métabolisme)</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Maladie d'Alzheimer (métabolisme)</term>
<term>Multimérisation de protéines</term>
<term>Neuroblastome (métabolisme)</term>
<term>Peptides bêta-amyloïdes ()</term>
<term>Peptides bêta-amyloïdes (métabolisme)</term>
<term>Peptides bêta-amyloïdes (pharmacologie)</term>
<term>Température</term>
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<term>Amyloid beta-Peptides</term>
<term>NF-kappa B</term>
<term>Neuroblastoma</term>
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<term>Neuroblastome</term>
<term>Peptides bêta-amyloïdes</term>
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<term>Humans</term>
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<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Multimérisation de protéines</term>
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<front><div type="abstract" xml:lang="en"><p>The aggregation of amyloid-β (Aβ) peptide and its deposition in parts of the brain form the central processes in the etiology of Alzheimer disease (AD). The low-molecular weight oligomers of Aβ aggregates (2 to 30 mers) are known to be the primary neurotoxic agents whose mechanisms of cellular toxicity and synaptic dysfunction have received substantial attention in the recent years. However, how these toxic agents proliferate and induce widespread amyloid deposition throughout the brain, and what mechanism is involved in the amplification and propagation of toxic oligomer species, are far from clear. Emerging evidence based on transgenic mice models indicates a transmissible nature of Aβ aggregates and implicates a prion-like mechanism of oligomer propagation, which manifests as the dissemination and proliferation of Aβ toxicity. Despite accumulating evidence in support of a transmissible nature of Aβ aggregates, a clear, molecular-level understanding of this intriguing mechanism is lacking. Recently, we reported the characterization of unique replicating oligomers of Aβ42 (12–24 mers) <italic>in</italic>
<italic>vitro</italic>
called <underline>L</underline>
arge <underline>F</underline>
atty <underline>A</underline>
cid-derived <underline>O</underline>
ligomers (LFAOs) (Kumar et al., 2012, <italic>J. Biol. Chem</italic>
). In the current report, we establish that LFAOs possess physiological activity by activating NF-κB in human neuroblastoma cells, and determine the experimental parameters that control the efficiency of LFAO replication by self-propagation. These findings constitute the first detailed report on monomer – oligomer lateral propagation reactions that may constitute potential mechanism governing transmissibility among Aβ oligomers. These data support the previous reports on transmissible mechanisms observed in transgenic animal models.</p>
</div>
</front>
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