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Conference Paper: Fadd (fas-associated death domain-containing protein) as a mediator of cell cycle dysregulation in beta-amyloid peptide-induced apoptosis?

TitleFadd (fas-associated death domain-containing protein) as a mediator of cell cycle dysregulation in beta-amyloid peptide-induced apoptosis?
Authors
Issue Date2008
PublisherSociety for Neuroscience
Citation
Neuroscience 2008, Washington, DC, 15-19 November 2008, Program#/Poster#: 829.11/E29 How to Cite?
AbstractOne of the pathological hallmarks of Alzheimer’s disease (AD) is the senile plaques, which are the extracellular accumulation of beta-amyloid (Aβ) peptides, found in cortex and hippocampus. Neuronal apoptosis has been implicated in AD pathogenesis. In vitro studies have shown that Aβ peptides can induce apoptosis. Owing to the finding of early caspase-8 activation (Suen et al, 2003), as well as our recent publication that extracellular Aβ peptide-triggered apoptosis is independent of the unfolded protein responses (Yu et al, 2006), we proposed the involvement of death receptor signaling in Aβ-induced apoptosis. In the classical death receptor signaling pathway, ligands binding to the death receptor such as Fas-receptor or tumor necrosis factor receptor (TNFR) lead to activation of caspase-8 and caspase-3, which resulted in apoptosis. Fas-Associated Death Domain-containing protein (FADD) is an adaptor molecule that bridges the Fas-receptor to the procaspase-8, thus, forming the death inducing signaling complex (DISC) during apoptosis. To investigate the effects of Aβ toxicity on FADD pathway, we firstly examined the change of both phospho-FADD and FADD proteins during apoptosis. By western blot analysis, the level of phospho-FADD was decreasing when treating with Aβ peptides while FADD protein remained unchanged. To our surprise, immunocytochemical staining showed that both phospho-FADD and FADD reside predominantly in nuclei. Previous studies in cancer research suggest that phospho-FADD plays a role in cell cycle regulation. Together with the recent findings of dysregulation of cell cycle events in postmortem AD brains, we investigate whether phospho-FADD affects the cell cycle regulation which may result in neuronal apoptosis under the Aβ neurotoxicity.
Persistent Identifierhttp://hdl.handle.net/10722/61404

 

DC FieldValueLanguage
dc.contributor.authorYu, MSen_HK
dc.contributor.authorPreisler, Jen_HK
dc.contributor.authorLai, SWen_HK
dc.contributor.authorNg, HKen_HK
dc.contributor.authorHugon, Jen_HK
dc.contributor.authorSo, KFen_HK
dc.contributor.authorChang, RCCen_HK
dc.date.accessioned2010-07-13T03:39:00Z-
dc.date.available2010-07-13T03:39:00Z-
dc.date.issued2008en_HK
dc.identifier.citationNeuroscience 2008, Washington, DC, 15-19 November 2008, Program#/Poster#: 829.11/E29en_HK
dc.identifier.urihttp://hdl.handle.net/10722/61404-
dc.description.abstractOne of the pathological hallmarks of Alzheimer’s disease (AD) is the senile plaques, which are the extracellular accumulation of beta-amyloid (Aβ) peptides, found in cortex and hippocampus. Neuronal apoptosis has been implicated in AD pathogenesis. In vitro studies have shown that Aβ peptides can induce apoptosis. Owing to the finding of early caspase-8 activation (Suen et al, 2003), as well as our recent publication that extracellular Aβ peptide-triggered apoptosis is independent of the unfolded protein responses (Yu et al, 2006), we proposed the involvement of death receptor signaling in Aβ-induced apoptosis. In the classical death receptor signaling pathway, ligands binding to the death receptor such as Fas-receptor or tumor necrosis factor receptor (TNFR) lead to activation of caspase-8 and caspase-3, which resulted in apoptosis. Fas-Associated Death Domain-containing protein (FADD) is an adaptor molecule that bridges the Fas-receptor to the procaspase-8, thus, forming the death inducing signaling complex (DISC) during apoptosis. To investigate the effects of Aβ toxicity on FADD pathway, we firstly examined the change of both phospho-FADD and FADD proteins during apoptosis. By western blot analysis, the level of phospho-FADD was decreasing when treating with Aβ peptides while FADD protein remained unchanged. To our surprise, immunocytochemical staining showed that both phospho-FADD and FADD reside predominantly in nuclei. Previous studies in cancer research suggest that phospho-FADD plays a role in cell cycle regulation. Together with the recent findings of dysregulation of cell cycle events in postmortem AD brains, we investigate whether phospho-FADD affects the cell cycle regulation which may result in neuronal apoptosis under the Aβ neurotoxicity.-
dc.languageengen_HK
dc.publisherSociety for Neuroscience-
dc.relation.ispartofSociety for Neuroscience Annual Meeting-
dc.titleFadd (fas-associated death domain-containing protein) as a mediator of cell cycle dysregulation in beta-amyloid peptide-induced apoptosis?en_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.hkuros154562en_HK

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