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Titolo:
Systemic amyloid deposits in familial British dementia
Autore:
Ghiso, JA; Holton, J; Miravalle, L; Calero, M; Lashley, T; Vidal, R; Houlden, H; Wood, N; Neubert, TA; Rostagno, A; Plant, G; Revesz, T; Frangione, B;
Indirizzi:
NYU, Sch Med, Dept Pathol, New York, NY 10016 USA NYU New York NY USA 10016 U, Sch Med, Dept Pathol, New York, NY 10016 USA NYU, Sch Med, Dept Psychiat, New York, NY 10016 USA NYU New York NY USA 10016 Sch Med, Dept Psychiat, New York, NY 10016 USA NYU, Sch Med, Dept Pharmacol, New York, NY 10016 USA NYU New York NY USA 10016 Sch Med, Dept Pharmacol, New York, NY 10016 USA NYU, Sch Med, Skirball Inst Biomol Med, New York, NY 10016 USA NYU New York NY USA 10016 kirball Inst Biomol Med, New York, NY 10016 USA Inst Neurol, Div Neuropathol, London WC1N 3BG, England Inst Neurol London England WC1N 3BG europathol, London WC1N 3BG, England Natl Hosp Neurol & Neurosurg, Inst Neurol, Dept Mol Pathogenesis, London WC1N 3BG, England Natl Hosp Neurol & Neurosurg London England WC1N 3BG n WC1N 3BG, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 47, volume: 276, anno: 2001,
pagine: 43909 - 43914
SICI:
0021-9258(20011123)276:47<43909:SADIFB>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEREDITARY CEREBRAL-HEMORRHAGE; ALZHEIMERS-DISEASE; BETA-PROTEIN; CYTOSKELETAL PATHOLOGY; PYROGLUTAMYL-PEPTIDES; PLAQUE-FORMATION; CYSTATIN-C; ANGIOPATHY; BRAIN; TISSUES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Ghiso, JA NYU, Sch Med, Dept Pathol, 550 1st Ave,TH-432, New York, NY 10016 USA NYU 550 1st Ave,TH-432 New York NY USA 10016 York, NY 10016 USA
Citazione:
J.A. Ghiso et al., "Systemic amyloid deposits in familial British dementia", J BIOL CHEM, 276(47), 2001, pp. 43909-43914

Abstract

Familial British dementia (FBD) is an early onset inherited disorder that,like familial Alzheimer's disease (FAD), is characterized by progressive dementia, amyloid deposition in the brain, and neurofibrillary degeneration of limbic neurons. The primary structure of the amyloid subunit (ABri) extracted from FBD brain tissues (Vidal, R., Frangione, B., Rostagno, A., Mead,S., Revesz, T., Plant, G., and Ghiso, J. (1999) Nature 399, 776-781) is entirely different and unrelated to any previously known amyloid protein. Patients with FBD have a single nucleotide substitution at codon 267 in the BRI2 gene, resulting in an arginine replacing the stop codon and a longer open reading frame of 277 amino acids instead of 266. The ABri peptide comprises the 34 C-terminal residues of the mutated precursor ABriPP-277 and is generated via furin-like proteolytic processing. Here we report that carriersof the Stop-to-Arg mutation have a soluble form of the amyloid peptide (sABri) in the circulation with an estimated concentration in the range of 20 ng/ml, several fold higher than that of soluble A beta. In addition, ABri species identical to those identified in the brain were also found as fibrillar components of amyloid deposits predominantly in the blood vessels of several peripheral tissues, including pancreas and myocardium. We hypothesizethat the high concentration of the soluble de novo created amyloidogenic peptide and/or the insufficient tissue clearance are the main causative factors for the formation of amyloid deposits outside the brain. Thus, FBD constitutes the first documented cerebral amyloidosis associated with neurodegeneration and dementia in which the amyloid deposition is also systemic.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 16:31:50