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- Publisher Website: 10.1073/pnas.94.8.3748
- Scopus: eid_2-s2.0-0030963605
- PMID: 9108049
- WOS: WOS:A1997WW81000050
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Article: Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
Title | Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation |
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Authors | |
Issue Date | 1997 |
Publisher | National 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? |
Abstract | β-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 Identifier | http://hdl.handle.net/10722/176348 |
ISSN | 2023 Impact Factor: 9.4 2023 SCImago Journal Rankings: 3.737 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Xu, H | en_US |
dc.contributor.author | Sweeney, D | en_US |
dc.contributor.author | Wang, R | en_US |
dc.contributor.author | Thinakaran, G | en_US |
dc.contributor.author | Lo, ACY | en_US |
dc.contributor.author | Sisodia, SS | en_US |
dc.contributor.author | Greengard, P | en_US |
dc.contributor.author | Gandy, S | en_US |
dc.date.accessioned | 2012-11-26T09:10:45Z | - |
dc.date.available | 2012-11-26T09:10:45Z | - |
dc.date.issued | 1997 | en_US |
dc.identifier.citation | Proceedings Of The National Academy Of Sciences Of The United States Of America, 1997, v. 94 n. 8, p. 3748-3752 | en_US |
dc.identifier.issn | 0027-8424 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/176348 | - |
dc.description.abstract | β-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.language | eng | en_US |
dc.publisher | National Academy of Sciences. The Journal's web site is located at http://www.pnas.org | en_US |
dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America | en_US |
dc.subject.mesh | Amyloid Beta-Peptides - Metabolism | en_US |
dc.subject.mesh | Biological Transport | en_US |
dc.subject.mesh | Cell Line | en_US |
dc.subject.mesh | Cytoplasmic Granules - Metabolism - Ultrastructure | en_US |
dc.subject.mesh | Golgi Apparatus - Metabolism - Ultrastructure | en_US |
dc.subject.mesh | Humans | en_US |
dc.title | Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lo, ACY: amylo@hkucc.hku.hk | en_US |
dc.identifier.authority | Lo, ACY=rp00425 | en_US |
dc.description.nature | link_to_OA_fulltext | en_US |
dc.identifier.doi | 10.1073/pnas.94.8.3748 | en_US |
dc.identifier.pmid | 9108049 | - |
dc.identifier.pmcid | PMC20512 | - |
dc.identifier.scopus | eid_2-s2.0-0030963605 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0030963605&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 94 | en_US |
dc.identifier.issue | 8 | en_US |
dc.identifier.spage | 3748 | en_US |
dc.identifier.epage | 3752 | en_US |
dc.identifier.isi | WOS:A1997WW81000050 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Xu, H=7407449104 | en_US |
dc.identifier.scopusauthorid | Sweeney, D=7101821452 | en_US |
dc.identifier.scopusauthorid | Wang, R=36071507000 | en_US |
dc.identifier.scopusauthorid | Thinakaran, G=7003798470 | en_US |
dc.identifier.scopusauthorid | Lo, ACY=7102780640 | en_US |
dc.identifier.scopusauthorid | Sisodia, SS=7102763509 | en_US |
dc.identifier.scopusauthorid | Greengard, P=36050698100 | en_US |
dc.identifier.scopusauthorid | Gandy, S=7006803448 | en_US |
dc.identifier.issnl | 0027-8424 | - |