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Conference Paper: Low molecular weight Aβ peptide leads to endoplasmic reticulum aggregation by interfering the microtubule stability

TitleLow molecular weight Aβ peptide leads to endoplasmic reticulum aggregation by interfering the microtubule stability
Authors
Issue Date2008
PublisherThe Society for Neuroscience
Citation
Neuroscience 2008, Washington, DC, 15-19 November 2008, Program#/Poster#: 829.1/E19 How to Cite?
AbstractDifferent modes of neurodegeneration contribute to the neuronal cell death in Alzheimer’s disease (AD). Increasing lines of evidence have demonstrated that synaptic degeneration and dysfunction of axonal transport may be the initial degenerative processes in AD. Endoplasmic reticulum (ER) is an important organelle that responsible for Ca2+ homeostasis, protein folding, post-translational modification, protein degradation, and transportation of nascent protein. Here we aim to examine the impact of sublethal dose of low molecular weight Aβ on the ER morphology. Low molecular weight of Aβ induces collapse of ER and affects anchoring the ER to microtubule (MT). In addition, the acetylation level of tubulin that related to the stability of microtubule is also decreased. Furthermore, prolonged treatment of low molecular weight Aβ triggers autophagy and enhances lysosome degradation. Loss of ER-retention protein, calreticulin, is also found in postmortem AD brain tissue. Treatment of MT-stabilizing agent, Taxol and histone deactylase inhibitor, trichostatin A can inhibit collapse of the ER. The results provide evidence to show that Aβ-induced disruption of MT can affect not only axonal transport but also intracellular organelles architecture such as the ER. Taken together, we provide evidence here to propose a new mechanism showing that collapse/aggregation of the ER plays a role in Aβ peptide-triggered neurodegenerative process.
Persistent Identifierhttp://hdl.handle.net/10722/61458

 

DC FieldValueLanguage
dc.contributor.authorLai, SWen_HK
dc.contributor.authorPreisler, Jen_HK
dc.contributor.authorBaum, Len_HK
dc.contributor.authorNg, HKen_HK
dc.contributor.authorHugon, Jen_HK
dc.contributor.authorSo, KFen_HK
dc.contributor.authorChang, RCCen_HK
dc.date.accessioned2010-07-13T03:40:05Z-
dc.date.available2010-07-13T03:40:05Z-
dc.date.issued2008en_HK
dc.identifier.citationNeuroscience 2008, Washington, DC, 15-19 November 2008, Program#/Poster#: 829.1/E19en_HK
dc.identifier.urihttp://hdl.handle.net/10722/61458-
dc.description.abstractDifferent modes of neurodegeneration contribute to the neuronal cell death in Alzheimer’s disease (AD). Increasing lines of evidence have demonstrated that synaptic degeneration and dysfunction of axonal transport may be the initial degenerative processes in AD. Endoplasmic reticulum (ER) is an important organelle that responsible for Ca2+ homeostasis, protein folding, post-translational modification, protein degradation, and transportation of nascent protein. Here we aim to examine the impact of sublethal dose of low molecular weight Aβ on the ER morphology. Low molecular weight of Aβ induces collapse of ER and affects anchoring the ER to microtubule (MT). In addition, the acetylation level of tubulin that related to the stability of microtubule is also decreased. Furthermore, prolonged treatment of low molecular weight Aβ triggers autophagy and enhances lysosome degradation. Loss of ER-retention protein, calreticulin, is also found in postmortem AD brain tissue. Treatment of MT-stabilizing agent, Taxol and histone deactylase inhibitor, trichostatin A can inhibit collapse of the ER. The results provide evidence to show that Aβ-induced disruption of MT can affect not only axonal transport but also intracellular organelles architecture such as the ER. Taken together, we provide evidence here to propose a new mechanism showing that collapse/aggregation of the ER plays a role in Aβ peptide-triggered neurodegenerative process.-
dc.languageengen_HK
dc.publisherThe Society for Neuroscience-
dc.relation.ispartofNeuroscience 2008-
dc.titleLow molecular weight Aβ peptide leads to endoplasmic reticulum aggregation by interfering the microtubule stabilityen_HK
dc.typeConference_Paperen_HK
dc.identifier.emailSo, KF: hrmaskf@hkucc.hku.hken_HK
dc.identifier.emailChang, RCC: rccchang@hkucc.hku.hken_HK
dc.identifier.authoritySo, KF=rp00329en_HK
dc.identifier.authorityChang, RCC=rp00470en_HK
dc.identifier.hkuros154561en_HK

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