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Titolo:
VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration
Autore:
Hirabayashi, M; Inoue, K; Tanaka, K; Nakadate, K; Ohsawa, Y; Kamei, Y; Popiel, AH; Sinohara, A; Iwamatsu, A; Kimura, Y; Uchiyama, Y; Hori, S; Kakizuka, A;
Indirizzi:
Osaka Biosci Inst, Dept 4, Osaka 5650874, Japan Osaka Biosci Inst Osaka Japan 5650874 Inst, Dept 4, Osaka 5650874, Japan Osaka Biosci Inst, Dept 3, Osaka 5650874, Japan Osaka Biosci Inst Osaka Japan 5650874 Inst, Dept 3, Osaka 5650874, Japan Osaka Univ, Grad Sch Med, Dept Cell Biol & Neurosci, Suita, Osaka 5650871,Japan Osaka Univ Suita Osaka Japan 5650871 Neurosci, Suita, Osaka 5650871,Japan Kyoto Univ, Kyoto, Japan Kyoto Univ Kyoto JapanKyoto Univ, Kyoto, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanagawa 2360004, Japan KirinBrewery Co Ltd Kanagawa Japan 2360004 nol, Kanagawa 2360004, Japan Tokyo Metropolitan Inst Med Sci, Dept Tumor Cell Biol, Tokyo 1138613, Japan Tokyo Metropolitan Inst Med Sci Tokyo Japan 1138613 Tokyo 1138613, Japan
Titolo Testata:
CELL DEATH AND DIFFERENTIATION
fascicolo: 10, volume: 8, anno: 2001,
pagine: 977 - 984
SICI:
1350-9047(200110)8:10<977:VIAPAC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SENSITIVE FUSION PROTEIN; TRANSGENIC MICE; POLYGLUTAMINE; DISEASE; HUNTINGTIN; HSP104; LOCALIZATION; APOPTOSIS; EXPANSION; DISORDERS;
Keywords:
polyglutamine; protein accumulation; vacuole formation; neurodegeneration; neuronal cell death;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Kakizuka, A Kyoto Univ, Grad Sch Biostudies, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 studies, Kyoto 6068501, Japan
Citazione:
M. Hirabayashi et al., "VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration", CELL DEAT D, 8(10), 2001, pp. 977-984

Abstract

Neuronal cell death, abnormal protein aggregates, and cytoplasmic vacuolization are major pathologies observed in many neurodegenerative disorders such as the polyglutamine (polyQ) diseases, prion disease, Alzheimer disease,and the Lewy body diseases, suggesting common mechanisms underlying neurodegeneration. Here, we have identified VCP/p97, a member of the AAA+ family of ATPase proteins, as a polyQ-interacting protein in vitro and in vivo, and report on its characterization. Endogenous VCP co-localized with expandedpolyQ (ex-polyQ) aggregates in cultured cells expressing ex-polyQ, with nuclear inclusions in Huntington disease patient brains, and with Lewy bodiesin patient samples. Moreover, the expression of VCP mutants with mutationsin the 2nd ATP binding domain created cytoplasmic vacuoles, followed by cell death. Very similar vacuoles were also induced by ex-polyQ expression orproteasome inhibitor treatment. These results suggest that VCP functions not only as a recognition factor for abnormally folded proteins but also as a pathological effector for several neurodegenerative phenotypes. VCP may thus be an ideal molecular target for the treatment of neurodegenerative disorders.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/01/21 alle ore 04:05:56