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Titolo:
Endosomal sorting of amyloid precursor protein-P-selectin chimeras influences secretase processing
Autore:
Daugherty, BL; Green, SA;
Indirizzi:
Univ Virginia, Sch Med, Dept Cell Biol, Charlottesville, VA 22908 USA UnivVirginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
TRAFFIC
fascicolo: 12, volume: 2, anno: 2001,
pagine: 908 - 916
SICI:
1398-9219(200112)2:12<908:ESOAPP>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANS-GOLGI NETWORK; MANNOSE 6-PHOSPHATE RECEPTOR; BETA-SECRETASE; CELL-SURFACE; CYTOPLASMIC DOMAIN; CLEAVAGE; PEPTIDE; MEMBRANE; EXPRESSION; GENERATION;
Keywords:
Alzheimer's disease; amyloid precursor protein; endosome; recycling; secretase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Green, SA Univ Virginia, Sch Med, Dept Cell Biol, POB 800732, Charlottesville, VA 22908 USA Univ Virginia POB 800732 Charlottesville VA USA 22908 22908 USA
Citazione:
B.L. Daugherty e S.A. Green, "Endosomal sorting of amyloid precursor protein-P-selectin chimeras influences secretase processing", TRAFFIC, 2(12), 2001, pp. 908-916

Abstract

Amyloid beta protein, the major component of the senile plaques in Alzheimer's disease, is generated by secretory and endocytic processing of amyloidprecursor protein. Internalized amyloid precursor protein either recycles to the plasma membrane, where alpha -secretase resides, or moves to acidic compartment(s) for beta -secretase exposure. While the trans-Golgi network contains beta -secretase activity, recent examination of the subcellular distribution of this proteinase, called BACE, has led to the suggestion that beta -secretase activity might also reside at the plasma membrane and in endosomes. To examine the role of endocytic compartments in beta -secretase processing of amyloid precursor protein, the wild-type and endosomal sortingmutant P-selectin cytoplasmic domains were used to control movement of amyloid precursor protein through endosomes. Amyloid precursor protein/P-selectin, which is sorted from early to late endosomes, undergoes significantly less a-secretase cleavage, and more beta -secretase cleavage, than amyloid precursor protein/P-selectin768A, a mutant that recycles more efficiently to the cell surface. Our results demonstrate that endosomal sorting influences relative exposure of the amyloid precursor protein/P-selectin chimeras to alpha- and beta -secretase activities, and suggest that, because deliveryto late endocytic compartments favors beta -secretase processing of amyloid precursor protein, there is likely limited beta -secretase activity in early endosomes or at the cell surface. We propose that the trans-Golgi network may be involved in both secretory and endocytic generation of amyloid beta protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 06:46:43