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Conference Paper: Aggregation of the endoplasmic reticulum may play a major role in initiating autophagic flux in oligomeric β-amyloid peptide-treated neurons

TitleAggregation of the endoplasmic reticulum may play a major role in initiating autophagic flux in oligomeric β-amyloid peptide-treated neurons
Authors
KeywordsEndoplasmic reticulum
Autophagy
Amyloid
Issue Date2011
PublisherSociety for Neuroscience.
Citation
The 41st Annual Meeting of the Society for Neuroscience (SfN 2011), Washington, D.C., 12-16 November 2011. How to Cite?
AbstractIncreasing lines of evidence have shown that autophagy can be an adaptive process for neurons to struggle for survives. Our previous studies have demonstrated the presence of autophagosomes in concomitance with the aggregation of the endoplasmic reticulum (ER) in cultured neurons upon exposure to oligomeric β-amyloid (Aβ) peptide. However, the precise mechanisms of how aggregation of the ER leads to formation of autophagosomes are largely unclear. We hypothesize that the damaged ER serves as a seed for nucleation proteins to form autophagosomes. The aim of this study is to elucidate the biological mechanisms of the nucleation step. Primary cultures of hippocampal neurons were employed for this study. Different DNA constructs conjugated with fluorescent proteins were used to monitor the change of autophagic flux in live neurons. By using multiphoton live cell imaging system, we observed that Aβ-induced autophagosomes were accompanied by omegasomes which were precursors for autophagosomes. Aggregation of the ER could facilitate the formation of the omegasomes. Meanwhile, Atg14L, a key mediator for forming omegasomes, was also found to be clustered at the ER aggregation site. The clustered Atg14L would further recruit Beclin 1-Vps34 to form a nucleation complex that would contribute to formation of omegasomes. Our results are among the first to demonstrate how aggregated ER trigger autophagy in neurons stressed by oligomeric Aβ peptide.
DescriptionNanosymposium - 637. Alzheimer's Disease and Other Dementias: Abeta Oligomerization and Toxicity: Poster no. 637.10
Persistent Identifierhttp://hdl.handle.net/10722/146946

 

DC FieldValueLanguage
dc.contributor.authorChang, RCCen_US
dc.contributor.authorZhang, NQen_US
dc.contributor.authorHung, CHLen_US
dc.contributor.authorHo, YSen_US
dc.contributor.authorWuwongse, Sen_US
dc.date.accessioned2012-05-23T05:51:09Z-
dc.date.available2012-05-23T05:51:09Z-
dc.date.issued2011en_US
dc.identifier.citationThe 41st Annual Meeting of the Society for Neuroscience (SfN 2011), Washington, D.C., 12-16 November 2011.en_US
dc.identifier.urihttp://hdl.handle.net/10722/146946-
dc.descriptionNanosymposium - 637. Alzheimer's Disease and Other Dementias: Abeta Oligomerization and Toxicity: Poster no. 637.10-
dc.description.abstractIncreasing lines of evidence have shown that autophagy can be an adaptive process for neurons to struggle for survives. Our previous studies have demonstrated the presence of autophagosomes in concomitance with the aggregation of the endoplasmic reticulum (ER) in cultured neurons upon exposure to oligomeric β-amyloid (Aβ) peptide. However, the precise mechanisms of how aggregation of the ER leads to formation of autophagosomes are largely unclear. We hypothesize that the damaged ER serves as a seed for nucleation proteins to form autophagosomes. The aim of this study is to elucidate the biological mechanisms of the nucleation step. Primary cultures of hippocampal neurons were employed for this study. Different DNA constructs conjugated with fluorescent proteins were used to monitor the change of autophagic flux in live neurons. By using multiphoton live cell imaging system, we observed that Aβ-induced autophagosomes were accompanied by omegasomes which were precursors for autophagosomes. Aggregation of the ER could facilitate the formation of the omegasomes. Meanwhile, Atg14L, a key mediator for forming omegasomes, was also found to be clustered at the ER aggregation site. The clustered Atg14L would further recruit Beclin 1-Vps34 to form a nucleation complex that would contribute to formation of omegasomes. Our results are among the first to demonstrate how aggregated ER trigger autophagy in neurons stressed by oligomeric Aβ peptide.-
dc.languageengen_US
dc.publisherSociety for Neuroscience.-
dc.relation.ispartofNeuroscience 2011en_US
dc.rightsNeuroscience 2011. Copyright © Society for Neuroscience.-
dc.subjectEndoplasmic reticulum-
dc.subjectAutophagy-
dc.subjectAmyloid-
dc.titleAggregation of the endoplasmic reticulum may play a major role in initiating autophagic flux in oligomeric β-amyloid peptide-treated neuronsen_US
dc.typeConference_Paperen_US
dc.identifier.emailChang, RCC: rccchang@hku.hken_US
dc.identifier.emailHung, CHL: chlhung@hku.hken_US
dc.identifier.emailHo, YS: janiceys@hku.hk-
dc.identifier.emailWuwongse, S: suthicha@hku.hk-
dc.identifier.authorityChang, RCC=rp00470en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros199441en_US
dc.publisher.placeUnited States-
dc.description.otherThe 41st Annual Meeting of the Society for Neuroscience (SfN 2011), Washington, D.C., 12-16 November 2011.-

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