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Titolo:
Mutated tau binds less avidly to microtubules than wildtype tau in living cells
Autore:
Nagiec, EE; Sampson, KE; Abraham, I;
Indirizzi:
Pharmacia Corp, Cell & Mol Biol, Kalamazoo, MI 49007 USA Pharmacia Corp Kalamazoo MI USA 49007 & Mol Biol, Kalamazoo, MI 49007 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE RESEARCH
fascicolo: 3, volume: 63, anno: 2001,
pagine: 268 - 275
SICI:
0360-4012(20010201)63:3<268:MTBLAT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PAIRED HELICAL FILAMENTS; PROTEIN-TAU; ALZHEIMERS-DISEASE; NEUROFIBRILLARY TANGLES; FRONTOTEMPORAL DEMENTIA; MUTATIONS; FTDP-17; PHOSPHORYLATION; PATHOLOGY; MISSENSE;
Keywords:
Alzheimer's disease; neurofibrillary tangles; paired helical filaments; PHF; FTDP-17; frontotemporal dementia with parkinsonism linked to chromosome 17;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Nagiec, EE Pharmacia Corp, Cell & Mol Biol, 7252-267-305, Kalamazoo, MI 49007 USA Pharmacia Corp 7252-267-305 Kalamazoo MI USA 49007 MI 49007 USA
Citazione:
E.E. Nagiec et al., "Mutated tau binds less avidly to microtubules than wildtype tau in living cells", J NEUROSC R, 63(3), 2001, pp. 268-275

Abstract

Some forms of genetically inherited dementia, including frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17), are caused by mutations in tau. We have examined several mutations in the microtubule-binding portion of tau for their effect on microtubule binding, cellular distribution and cytoskeletal structure in mammalian cells. Using constructs coding for mutant (P301L and V337M) and wildtype human tau fused to a green fluorescent protein analog (EGFP) we followed the disposition of tau in live cells after transient transfection using confocal microscopy. Most of the tauprotein localized to structures that resembled microtubules or microtubulebundles and cc-localized with tubulin. At 3 days post-transfection mutant tau proteins showed a higher abundance of free tau in the cytoplasm than did wildtype tau. Cells expressing the P301L mutation showed proportionally more cytoplasmic localization of tau. Confirming these results, fractionatedcells with mutant tau had a higher percentage of tau in the cytoplasmic compartment as compared to the cytoskeletal compartment. Cells with wildtype tau had most tau in the cytoskeletal fraction. Because the mutations (V337M, P301L) are associated with genetic tauopathies, these results suggest that a factor in disease etiology of genetic tauopathies and other dementias with altered tau is a greater abundance of tau in the cytoplasm due to decreased binding to microtubules. This increased cytoplasmic presence may be a significant factor in promoting tau aggregation. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 17/09/19 alle ore 18:56:15