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Article: Low molecular weight Aβ induces collapse of endoplasmic reticulum

TitleLow molecular weight Aβ induces collapse of endoplasmic reticulum
Authors
KeywordsAlzheimer's disease
Autophagy
Cytoskeleton
Endoplasmic reticulum
β-amyloid
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ymcne
Citation
Molecular And Cellular Neuroscience, 2009, v. 41 n. 1, p. 32-43 How to Cite?
AbstractThe endoplasmic reticulum (ER) is a dynamic multifunction organelle that is responsible for Ca2+ homeostasis, protein folding, post-translational modification, protein degradation, and transportation of nascent proteins. Disruption of ER architecture might affect the normal physiology of the cell. In yeast, expansion of the ER is observed under unfolded protein response (UPR) and subsequently induces autophagy initiated from the ER. Here, we found that soluble low molecular weight of Aβ disrupted the anchoring between ER and microtubules (MT) and induced collapse of ER. In addition, it decreased the stability of MT. Subsequently, low molecular weight Aβ triggered autophagy and enhanced lysosomal degradation, as shown by electron microscopy and live-cell imaging. Dysfunction of ER can be further proved in postmortem AD brain and transgenic mice bearing APP Swedish mutation by immunohistochemical analysis of calreticulin. Treatment with Taxol, a MT-stabilizing agent, could partially inhibit collapse of the ER and induction of autophagy. The results show that Aβ-induced disruption of MT can affect the architecture of the ER. Collapse/aggregation of the ER may play an important role in Aβ peptide-triggered neurodegenerative processes. © 2009 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149714
ISSN
2023 Impact Factor: 2.6
2023 SCImago Journal Rankings: 1.042
ISI Accession Number ID
Funding AgencyGrant Number
GRF7552/06M
N_HKU707/07M
Procore France-Hong Kong Joint Research Scheme
HKU Alzheimer's Disease Research Network
HKU Seed Funding for Basic Research200711159028
Funding Information:

We are grateful to Dr. D.R. Klopfenstein for CLIMP63-GFP, Dr. N.S. Wong for LC3-DsRed and Dr. S.K. Kong for KDEL-DsRed. The study is Supported by GRF (7552/06M), N_HKU (707/07M), Procore France-Hong Kong Joint Research Scheme, HKU Alzheimer's Disease Research Network and HKU Seed Funding for Basic Research (200711159028).

References
Grants

 

DC FieldValueLanguage
dc.contributor.authorLai, CSWen_US
dc.contributor.authorPreisler, Jen_US
dc.contributor.authorBaum, Len_US
dc.contributor.authorLee, DHSen_US
dc.contributor.authorNg, HKen_US
dc.contributor.authorHugon, Jen_US
dc.contributor.authorSo, KFen_US
dc.contributor.authorChang, RCCen_US
dc.date.accessioned2012-06-26T05:57:30Z-
dc.date.available2012-06-26T05:57:30Z-
dc.date.issued2009en_US
dc.identifier.citationMolecular And Cellular Neuroscience, 2009, v. 41 n. 1, p. 32-43en_US
dc.identifier.issn1044-7431en_US
dc.identifier.urihttp://hdl.handle.net/10722/149714-
dc.description.abstractThe endoplasmic reticulum (ER) is a dynamic multifunction organelle that is responsible for Ca2+ homeostasis, protein folding, post-translational modification, protein degradation, and transportation of nascent proteins. Disruption of ER architecture might affect the normal physiology of the cell. In yeast, expansion of the ER is observed under unfolded protein response (UPR) and subsequently induces autophagy initiated from the ER. Here, we found that soluble low molecular weight of Aβ disrupted the anchoring between ER and microtubules (MT) and induced collapse of ER. In addition, it decreased the stability of MT. Subsequently, low molecular weight Aβ triggered autophagy and enhanced lysosomal degradation, as shown by electron microscopy and live-cell imaging. Dysfunction of ER can be further proved in postmortem AD brain and transgenic mice bearing APP Swedish mutation by immunohistochemical analysis of calreticulin. Treatment with Taxol, a MT-stabilizing agent, could partially inhibit collapse of the ER and induction of autophagy. The results show that Aβ-induced disruption of MT can affect the architecture of the ER. Collapse/aggregation of the ER may play an important role in Aβ peptide-triggered neurodegenerative processes. © 2009 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ymcneen_US
dc.relation.ispartofMolecular and Cellular Neuroscienceen_US
dc.subjectAlzheimer's disease-
dc.subjectAutophagy-
dc.subjectCytoskeleton-
dc.subjectEndoplasmic reticulum-
dc.subjectβ-amyloid-
dc.subject.meshAmyloid Beta-Peptides - Chemistry - Genetics - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshEndoplasmic Reticulum - Metabolism - Ultrastructureen_US
dc.subject.meshHippocampus - Cytologyen_US
dc.subject.meshHumansen_US
dc.subject.meshLysosomes - Metabolism - Ultrastructureen_US
dc.subject.meshMiceen_US
dc.subject.meshMice, Transgenicen_US
dc.subject.meshMicrotubules - Metabolismen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshNeurons - Cytology - Metabolismen_US
dc.subject.meshNocodazole - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshRecombinant Fusion Proteins - Genetics - Metabolismen_US
dc.subject.meshTubulin - Metabolismen_US
dc.subject.meshTubulin Modulators - Metabolismen_US
dc.subject.meshVacuoles - Metabolismen_US
dc.titleLow molecular weight Aβ induces collapse of endoplasmic reticulumen_US
dc.typeArticleen_US
dc.identifier.emailSo, KF:hrmaskf@hkucc.hku.hken_US
dc.identifier.emailChang, RCC:rccchang@hkucc.hku.hken_US
dc.identifier.authoritySo, KF=rp00329en_US
dc.identifier.authorityChang, RCC=rp00470en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.mcn.2009.01.006en_US
dc.identifier.pmid19386229-
dc.identifier.scopuseid_2-s2.0-67349098681en_US
dc.identifier.hkuros155385-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-67349098681&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume41en_US
dc.identifier.issue1en_US
dc.identifier.spage32en_US
dc.identifier.epage43en_US
dc.identifier.isiWOS:000265715700004-
dc.publisher.placeUnited Statesen_US
dc.relation.projectInvestigating the impact of oligomeric β-amyloid peptide on RNA-trifficking in neurons. Implication on local protein translation control in neurons.-
dc.identifier.scopusauthoridLai, CSW=26022547000en_US
dc.identifier.scopusauthoridPreisler, J=35201486700en_US
dc.identifier.scopusauthoridBaum, L=7103310839en_US
dc.identifier.scopusauthoridLee, DHS=7406670050en_US
dc.identifier.scopusauthoridNg, HK=7401619354en_US
dc.identifier.scopusauthoridHugon, J=7103202992en_US
dc.identifier.scopusauthoridSo, KF=34668391300en_US
dc.identifier.scopusauthoridChang, RCC=7403713410en_US
dc.identifier.issnl1044-7431-

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