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Titolo:
Identification of amino-terminally and phosphotyrosine-modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain
Autore:
Russo, C; Salis, S; Dolcini, V; Venezia, V; Song, XH; Teller, JK; Schettini, G;
Indirizzi:
Case Western Reserve Univ, Dept Neuropathol, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Univ Genoa, Dept Oncol Biol Genet, Genoa, Italy Univ Genoa Genoa ItalyUniv Genoa, Dept Oncol Biol Genet, Genoa, Italy Natl Canc Inst, Adv Biotechnol Ctr, Sect Pharmacol & Neurosci, Genoa, Italy Natl Canc Inst Genoa Italy Ctr, Sect Pharmacol & Neurosci, Genoa, Italy
Titolo Testata:
NEUROBIOLOGY OF DISEASE
fascicolo: 1, volume: 8, anno: 2001,
pagine: 173 - 180
SICI:
0969-9961(200102)8:1<173:IOAAPC>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
A-BETA 3-PYROGLUTAMYL; TRANSGENIC MICE; INTRACELLULAR DOMAIN; SENILE PLAQUES; IN-VITRO; PEPTIDE; FE65; PRESENILIN-1; MUTATIONS; SECRETASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Teller, JK Case Western Reserve Univ, Dept Neuropathol, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 OH 44106 USA
Citazione:
C. Russo et al., "Identification of amino-terminally and phosphotyrosine-modified carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain", NEUROBIOL D, 8(1), 2001, pp. 173-180

Abstract

The carboxy-terminal fragments (CTFs) of the amyloid precursor protein (APP) are considered beta -amyloid (A beta) precursors as well as molecular species that are both amyloidogenic and neurotoxic by themselves in vitro or in animal models. However the CTFs' role in the pathogenesis of Alzheimer'sdisease (AD) is however relatively unexplored in human brain. In this study, we analylzed OTFs extracted from brains of subjects with AD, non-AD control, and Down's syndrome (DS) cases. Our data indicate that: (i) In fetal DS brains CTFs levels are increased in comparison to age-matched control, suggesting that the enhanced CTFs formation is important for the early occurrence of plaque deposition in DS. There is no significant difference in CTFslevel is present between AD and age-matched control cases. Iii) CTFs modified at their N-terminus appear to be the direct precursors of likewise N-terminally modified A beta peptides, which constitute the most abundant species in AD and DS plaques. This observation suggests that N-truncated A beta peptides are rather formed directly at beta -secretase level and not through a progressive proteolysis of full-length A beta1-40/42. (iii) Among the differently cleaved CTFs, only the 22- and 12.5-kDa polypeptides are tyrosine phosphorylated in both AD and control brains while the full-length APP and the CTFs migrating below the 12.5-kDa marker are not phosphorylated, suggesting that some APP and CTFs are processed through regulated pathways. This study provides further evidence that in human brain CTFs constitute a molecular species directly involved in AD pathogenesis and in the development of the AD-like pathology in DS subjects. (C) 2001 Academic Press.

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Documento generato il 09/04/20 alle ore 06:34:08