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Titolo:
Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of beta-amyloid protein
Autore:
Kawahara, M; Kato, M; Kuroda, Y;
Indirizzi:
Tokyo Metropolitan Inst Neurosci, Dept Mol & Cellular Neurobiol, Tokyo 1838526, Japan Tokyo Metropolitan Inst Neurosci Tokyo Japan 1838526 okyo 1838526, Japan
Titolo Testata:
BRAIN RESEARCH BULLETIN
fascicolo: 2, volume: 55, anno: 2001,
pagine: 211 - 217
SICI:
0361-9230(20010515)55:2<211:EOAOTN>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMER A-BETA; PRECURSOR PROTEIN; CORTICAL-NEURONS; BRAIN ALUMINUM; DRINKING-WATER; RAT NEURONS; DISEASE; DIALYSIS; TAU; ENCEPHALOPATHY;
Keywords:
neurodegeneration; zinc; Alzheimer's disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Kawahara, M Tokyo Metropolitan Inst Neurosci, Dept Mol & Cellular Neurobiol, 26 Musashidai, Tokyo 1838526, Japan Tokyo Metropolitan Inst Neurosci 26 Musashidai Tokyo Japan 1838526
Citazione:
M. Kawahara et al., "Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of beta-amyloid protein", BRAIN RES B, 55(2), 2001, pp. 211-217

Abstract

Recent epidemiological, neuropathological, and biochemical studies have suggested a possible link between the neurotoxicity of aluminum and the pathogenesis of Alzheimer's disease. However, this relationship remains controversial. To investigate detailed characteristics of neurotoxicity of aluminum, we used primary cultured neurons of rat cerebral cortex as an in vitro model system for the observation of morphological changes induced by chronic exposure to aluminum. Although the exposure to aluminum chloride (10-100 muM) for 1 week did not cause marked neuronal death, degeneration of neuriticprocesses and accumulation of tau protein and beta -amyloid protein appeared after chronic exposure to 50 muM aluminum chloride for more than 3 weeks. We also investigated the polymerization of beta -amyloid protein in vitrousing the immunoblotting technique. We thus found that aluminum induced conformational changes in beta -amyloid protein and enhanced its aggregation in vitro. The aggregated beta -amyloid protein was dissolved by the addition of desferrioxamine, a chelator of aluminum. The aggregated beta -amyloid protein pre-incubated with aluminum formed fibrillar deposits on the surface of cultured neurons. (C) 2001 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:59:15