File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation

TitleGeneration of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
Authors
Issue Date1997
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 1997, v. 94 n. 8, p. 3748-3752 How to Cite?
Abstractβ-amyloid protein (Aβ) formation was reconstituted in permeabilized neuroblastoma cells expressing human Alzheimer β-amyloid precursor protein (βAPP) harboring the Swedish double mutation associated with familial early- onset Alzheimer disease. Permeabilized cells were prepared following metabolic labeling and incubation at 20°C, a temperature that allows βAPP to accumulate in the trans-Golgi network (TGN) without concomitant Aβ formation. Subsequent incubation at 37°C led to the generation of Aβ. Aβ production in the TGN persisted even under conditions in which formation of nascent post-TGN vesicles was inhibited by addition of guanosine 5'-O-(3- thiotriphosphate), a nonhydrolyzable GTP analogue, or by omission of cytosol. These and other results indicate that vesicle budding and trafficking may not be required for proteolytic metabolism of βAPP to Aβ, a process that includes 'γ-secretase' cleavage within the βAPP transmembrane domain.
Persistent Identifierhttp://hdl.handle.net/10722/176348
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXu, Hen_US
dc.contributor.authorSweeney, Den_US
dc.contributor.authorWang, Ren_US
dc.contributor.authorThinakaran, Gen_US
dc.contributor.authorLo, ACYen_US
dc.contributor.authorSisodia, SSen_US
dc.contributor.authorGreengard, Pen_US
dc.contributor.authorGandy, Sen_US
dc.date.accessioned2012-11-26T09:10:45Z-
dc.date.available2012-11-26T09:10:45Z-
dc.date.issued1997en_US
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 1997, v. 94 n. 8, p. 3748-3752en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/176348-
dc.description.abstractβ-amyloid protein (Aβ) formation was reconstituted in permeabilized neuroblastoma cells expressing human Alzheimer β-amyloid precursor protein (βAPP) harboring the Swedish double mutation associated with familial early- onset Alzheimer disease. Permeabilized cells were prepared following metabolic labeling and incubation at 20°C, a temperature that allows βAPP to accumulate in the trans-Golgi network (TGN) without concomitant Aβ formation. Subsequent incubation at 37°C led to the generation of Aβ. Aβ production in the TGN persisted even under conditions in which formation of nascent post-TGN vesicles was inhibited by addition of guanosine 5'-O-(3- thiotriphosphate), a nonhydrolyzable GTP analogue, or by omission of cytosol. These and other results indicate that vesicle budding and trafficking may not be required for proteolytic metabolism of βAPP to Aβ, a process that includes 'γ-secretase' cleavage within the βAPP transmembrane domain.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.subject.meshAmyloid Beta-Peptides - Metabolismen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCell Lineen_US
dc.subject.meshCytoplasmic Granules - Metabolism - Ultrastructureen_US
dc.subject.meshGolgi Apparatus - Metabolism - Ultrastructureen_US
dc.subject.meshHumansen_US
dc.titleGeneration of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formationen_US
dc.typeArticleen_US
dc.identifier.emailLo, ACY: amylo@hkucc.hku.hken_US
dc.identifier.authorityLo, ACY=rp00425en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1073/pnas.94.8.3748en_US
dc.identifier.pmid9108049-
dc.identifier.pmcidPMC20512-
dc.identifier.scopuseid_2-s2.0-0030963605en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030963605&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume94en_US
dc.identifier.issue8en_US
dc.identifier.spage3748en_US
dc.identifier.epage3752en_US
dc.identifier.isiWOS:A1997WW81000050-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridXu, H=7407449104en_US
dc.identifier.scopusauthoridSweeney, D=7101821452en_US
dc.identifier.scopusauthoridWang, R=36071507000en_US
dc.identifier.scopusauthoridThinakaran, G=7003798470en_US
dc.identifier.scopusauthoridLo, ACY=7102780640en_US
dc.identifier.scopusauthoridSisodia, SS=7102763509en_US
dc.identifier.scopusauthoridGreengard, P=36050698100en_US
dc.identifier.scopusauthoridGandy, S=7006803448en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats