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Titolo:
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation
Autore:
Nilsberth, C; Westlind-Danielsson, A; Eckman, CB; Condron, MM; Axelman, K; Forsell, C; Stenh, C; Luthman, J; Teplow, DB; Younkin, SG; Naslund, J; Lannfelt, L;
Indirizzi:
AstraZeneca, Discovery Res Area CNS & Pain Control, S-15185 Sodertalje, Sweden AstraZeneca Sodertalje Sweden S-15185 ontrol, S-15185 Sodertalje, Sweden Mayo Clin Jacksonville, Jacksonville, FL 32224 USA Mayo Clin JacksonvilleJacksonville FL USA 32224 cksonville, FL 32224 USA Brigham & Womens Hosp, Ctr Neurol Dis, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 eurol Dis, Boston, MA 02115 USA
Titolo Testata:
NATURE NEUROSCIENCE
fascicolo: 9, volume: 4, anno: 2001,
pagine: 887 - 893
SICI:
1097-6256(200109)4:9<887:T'AM(C>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYLOID PRECURSOR PROTEIN; FIBRIL FORMATION; IN-VITRO; CEREBRAL-HEMORRHAGE; GENE; FIBRILLOGENESIS; A-BETA(1-42); PRESENILINS; PEPTIDES; PLASMA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Lannfelt, L Karolinska Inst, Novum KFC, Dept Neurotec, S-14186 Huddinge, Sweden Karolinska Inst Huddinge Sweden S-14186 186 Huddinge, Sweden
Citazione:
C. Nilsberth et al., "The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation", NAT NEUROSC, 4(9), 2001, pp. 887-893

Abstract

Several pathogenic Alzheimer's disease (AD) mutations have been described,all of which cause increased amyloid beta -protein (A beta) levels. Here we present studies of a pathogenic amyloid precursor protein (APP) mutation,located within the A beta sequence at codon 693 (E693G), that causes AD ina Swedish family. Carriers of this 'Arctic' mutation showed decreased A beta 42 and A beta 40 levels in plasma. Additionally, low levels of A beta 42were detected in conditioned media from cells transfected with APP(E693G). Fibrillization studies demonstrated no difference in fibrillization rate, but A beta with the Arctic mutation formed protofibrils at a much higher rate and in larger quantities than wild-type (wt) A beta. The finding of increased protofibril formation and decreased A beta plasma levels in the Arctic AD may reflect an alternative pathogenic mechanism for AD involving rapidA beta protofibril formation leading to accelerated buildup of insoluble Abeta intra- and/or extracellularly.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:39:04