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Article: Mutation of the conserved N-terminal cysteine (Cys92) of human presenilin 1 causes increased Aβ42 secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans
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TitleMutation of the conserved N-terminal cysteine (Cys92) of human presenilin 1 causes increased Aβ42 secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans
 
AuthorsDong Mei Zhang1
Levitan, D1
Yu, G1
Nishimura, M1
Chen, F1
Tandon, A1
Kawarai, T1
Arawaka, S1
Supala, A1
Song, YQ1
Rogaeva, E1
Liang, Y1
Holmes, E1
Milman, P1
Sato, C1
Zhang, L1
St GeorgeHyslop, P1
 
Keywordsβ-amyloid precursor protein

Alzheimer disease
Development
lin-12
Notch
Presenilin
Sel-12
 
Issue Date2000
 
PublisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.neuroreport.com
 
CitationNeuroreport, 2000, v. 11 n. 14, p. 3227-3230 [How to Cite?]
 
AbstractThe presenilin proteins are involved in the proteolytic processing of transmembrane proteins such as Notch/lin-12 and the β-amyloid precursor protein (βAPP). Mutation of a conserved cysteine (Cys60Ser) in the C. elegans presenilin sel-12 has a loss-of-function effect on Notch/lin-12 processing similar to that of null mutations in sel-12. In contrast, in mammalian cells, most missense mutations increase γ-secretase cleavage of βAPP. We report here that mutation of this conserved cysteine (Cys92Ser) in human presenilin 1 confers a loss-of-function effect in C. elegans, but causes increased Aβ42 secretion in mammalian cells. These data suggest that the role of presenilins in Notch/lin-12 signalling and βAPP processing are either separately regulated activities or independent activities of the presenilins. (C) 2000 Lippincott Williams and Wilkins.
 
ISSN0959-4965
2013 Impact Factor: 1.644
2013 SCImago Journal Rankings: 0.909
 
ISI Accession Number IDWOS:000089833500036
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorDong Mei Zhang
 
dc.contributor.authorLevitan, D
 
dc.contributor.authorYu, G
 
dc.contributor.authorNishimura, M
 
dc.contributor.authorChen, F
 
dc.contributor.authorTandon, A
 
dc.contributor.authorKawarai, T
 
dc.contributor.authorArawaka, S
 
dc.contributor.authorSupala, A
 
dc.contributor.authorSong, YQ
 
dc.contributor.authorRogaeva, E
 
dc.contributor.authorLiang, Y
 
dc.contributor.authorHolmes, E
 
dc.contributor.authorMilman, P
 
dc.contributor.authorSato, C
 
dc.contributor.authorZhang, L
 
dc.contributor.authorSt GeorgeHyslop, P
 
dc.date.accessioned2011-07-14T07:03:07Z
 
dc.date.available2011-07-14T07:03:07Z
 
dc.date.issued2000
 
dc.description.abstractThe presenilin proteins are involved in the proteolytic processing of transmembrane proteins such as Notch/lin-12 and the β-amyloid precursor protein (βAPP). Mutation of a conserved cysteine (Cys60Ser) in the C. elegans presenilin sel-12 has a loss-of-function effect on Notch/lin-12 processing similar to that of null mutations in sel-12. In contrast, in mammalian cells, most missense mutations increase γ-secretase cleavage of βAPP. We report here that mutation of this conserved cysteine (Cys92Ser) in human presenilin 1 confers a loss-of-function effect in C. elegans, but causes increased Aβ42 secretion in mammalian cells. These data suggest that the role of presenilins in Notch/lin-12 signalling and βAPP processing are either separately regulated activities or independent activities of the presenilins. (C) 2000 Lippincott Williams and Wilkins.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationNeuroreport, 2000, v. 11 n. 14, p. 3227-3230 [How to Cite?]
 
dc.identifier.epage3230
 
dc.identifier.isiWOS:000089833500036
 
dc.identifier.issn0959-4965
2013 Impact Factor: 1.644
2013 SCImago Journal Rankings: 0.909
 
dc.identifier.issue14
 
dc.identifier.pmid11043553
 
dc.identifier.scopuseid_2-s2.0-0034727409
 
dc.identifier.spage3227
 
dc.identifier.urihttp://hdl.handle.net/10722/134766
 
dc.identifier.volume11
 
dc.publisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.neuroreport.com
 
dc.publisher.placeUnited States
 
dc.relation.ispartofNeuroReport
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmyloid beta-Peptides/*genetics/metabolism
 
dc.subject.meshAnimals
 
dc.subject.meshCaenorhabditis elegans/*genetics/metabolism
 
dc.subject.mesh*Caenorhabditis elegans Proteins
 
dc.subject.meshCysteine/*genetics
 
dc.subject.meshHelminth Proteins/genetics/*metabolism
 
dc.subject.meshHumans
 
dc.subject.meshMembrane Proteins/*genetics/*metabolism
 
dc.subject.meshMutation, Missense/physiology
 
dc.subject.meshPeptide Fragments/*genetics/metabolism
 
dc.subject.meshPoint Mutation/genetics
 
dc.subject.meshPresenilin-1
 
dc.subject.meshProtein Structure, Tertiary/genetics
 
dc.subject.meshReceptors, Notch
 
dc.subject.meshSignal Transduction/genetics
 
dc.subjectβ-amyloid precursor protein
 
dc.subject
 
dc.subjectAlzheimer disease
 
dc.subjectDevelopment
 
dc.subjectlin-12
 
dc.subjectNotch
 
dc.subjectPresenilin
 
dc.subjectSel-12
 
dc.titleMutation of the conserved N-terminal cysteine (Cys92) of human presenilin 1 causes increased Aβ42 secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans
 
dc.typeArticle
 
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<contributor.author>Chen, F</contributor.author>
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<contributor.author>Arawaka, S</contributor.author>
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Author Affiliations
  1. University Health Network University of Toronto