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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

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
Authors
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
Citation
Neuroreport, 2000, v. 11 n. 14, p. 3227-3230 How to Cite?
Abstract
The 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.
Persistent Identifierhttp://hdl.handle.net/10722/134766
ISSN
2013 Impact Factor: 1.644
2013 SCImago Journal Rankings: 0.909
ISI Accession Number ID
References

 

Author Affiliations
  1. University Health Network University of Toronto
DC FieldValueLanguage
dc.contributor.authorDong Mei Zhangen_HK
dc.contributor.authorLevitan, Den_HK
dc.contributor.authorYu, Gen_HK
dc.contributor.authorNishimura, Men_HK
dc.contributor.authorChen, Fen_HK
dc.contributor.authorTandon, Aen_HK
dc.contributor.authorKawarai, Ten_HK
dc.contributor.authorArawaka, Sen_HK
dc.contributor.authorSupala, Aen_HK
dc.contributor.authorSong, YQen_HK
dc.contributor.authorRogaeva, Een_HK
dc.contributor.authorLiang, Yen_HK
dc.contributor.authorHolmes, Een_HK
dc.contributor.authorMilman, Pen_HK
dc.contributor.authorSato, Cen_HK
dc.contributor.authorZhang, Len_HK
dc.contributor.authorSt GeorgeHyslop, Pen_HK
dc.date.accessioned2011-07-14T07:03:07Z-
dc.date.available2011-07-14T07:03:07Z-
dc.date.issued2000en_HK
dc.identifier.citationNeuroreport, 2000, v. 11 n. 14, p. 3227-3230en_HK
dc.identifier.issn0959-4965en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134766-
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.en_HK
dc.publisherLippincott Williams & Wilkins. The Journal's web site is located at http://www.neuroreport.comen_HK
dc.relation.ispartofNeuroReporten_HK
dc.subjectβ-amyloid precursor proteinen_HK
dc.subjecten_HK
dc.subjectAlzheimer diseaseen_HK
dc.subjectDevelopmenten_HK
dc.subjectlin-12en_HK
dc.subjectNotchen_HK
dc.subjectPresenilinen_HK
dc.subjectSel-12en_HK
dc.subject.meshAmyloid beta-Peptides/*genetics/metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCaenorhabditis elegans/*genetics/metabolismen_US
dc.subject.mesh*Caenorhabditis elegans Proteinsen_US
dc.subject.meshCysteine/*geneticsen_US
dc.subject.meshHelminth Proteins/genetics/*metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMembrane Proteins/*genetics/*metabolismen_US
dc.subject.meshMutation, Missense/physiologyen_US
dc.subject.meshPeptide Fragments/*genetics/metabolismen_US
dc.subject.meshPoint Mutation/geneticsen_US
dc.subject.meshPresenilin-1en_US
dc.subject.meshProtein Structure, Tertiary/geneticsen_US
dc.subject.meshReceptors, Notchen_US
dc.subject.meshSignal Transduction/geneticsen_US
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. elegansen_HK
dc.typeArticleen_HK
dc.identifier.emailSong, YQ:songy@hkucc.hku.hken_HK
dc.identifier.authoritySong, YQ=rp00488en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid11043553en_HK
dc.identifier.scopuseid_2-s2.0-0034727409en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034727409&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume11en_HK
dc.identifier.issue14en_HK
dc.identifier.spage3227en_HK
dc.identifier.epage3230en_HK
dc.identifier.isiWOS:000089833500036-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridDong Mei Zhang=7409524552en_HK
dc.identifier.scopusauthoridLevitan, D=23044813300en_HK
dc.identifier.scopusauthoridYu, G=35370376900en_HK
dc.identifier.scopusauthoridNishimura, M=7403650959en_HK
dc.identifier.scopusauthoridChen, F=7404907428en_HK
dc.identifier.scopusauthoridTandon, A=7103281816en_HK
dc.identifier.scopusauthoridKawarai, T=7003632751en_HK
dc.identifier.scopusauthoridArawaka, S=6602984633en_HK
dc.identifier.scopusauthoridSupala, A=6602797868en_HK
dc.identifier.scopusauthoridSong, YQ=7404921212en_HK
dc.identifier.scopusauthoridRogaeva, E=35372614800en_HK
dc.identifier.scopusauthoridLiang, Y=26642980800en_HK
dc.identifier.scopusauthoridHolmes, E=7201667388en_HK
dc.identifier.scopusauthoridMilman, P=7004252433en_HK
dc.identifier.scopusauthoridSato, C=7201887342en_HK
dc.identifier.scopusauthoridZhang, L=8508954500en_HK
dc.identifier.scopusauthoridSt GeorgeHyslop, P=7005637468en_HK

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