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Titolo:
Regulation and deregulation of E2F1 in postmitotic neurons differentiated from embryonal carcinoma P19 cells
Autore:
Azuma-Hara, N; Taniura, H; Uetsuki, T; Niinobe, M; Yoshikawa, K;
Indirizzi:
Osaka Univ, Inst Prot Res, Div Regulat Macromol Funct, Osaka 5650871, Japan Osaka Univ Osaka Japan 5650871 ulat Macromol Funct, Osaka 5650871, Japan
Titolo Testata:
EXPERIMENTAL CELL RESEARCH
fascicolo: 2, volume: 251, anno: 1999,
pagine: 442 - 451
SICI:
0014-4827(19990915)251:2<442:RADOEI>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINOBLASTOMA FAMILY PROTEINS; UBIQUITIN-PROTEASOME PATHWAY; TUMOR-SUPPRESSOR PROTEIN; TRANSCRIPTION FACTOR E2F; S-PHASE ENTRY; NUCLEAR-PROTEIN; DNA-SYNTHESIS; TRANSFORMING PROTEINS; GROWTH SUPPRESSION; CYCLE REGULATION;
Keywords:
E2F1; postmitotic neurons; ubiquitination; proteasome; adenovirus vector; apoptosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Yoshikawa, K Osaka Univ, Inst Prot Res, Div Regulat Macromol Funct, Yamadaoka 3-2, Osaka 5650871, Japan Osaka Univ Yamadaoka 3-2 Osaka Japan 5650871 5650871, Japan
Citazione:
N. Azuma-Hara et al., "Regulation and deregulation of E2F1 in postmitotic neurons differentiated from embryonal carcinoma P19 cells", EXP CELL RE, 251(2), 1999, pp. 442-451

Abstract

Neurons withdraw from the cell cycle immediately after differentiation from their proliferative precursors. E2F1, a principal transcription factor that promotes cell cycle progression, must be silenced in neurons. We investigated the E2F1 system in postmitotic neurons derived from murine embryonal carcinoma P19 cells. P19 cells highly expressed the E2F1 gene during neuraldifferentiation, and enriched neurons contained a high abundance of E2F1 mRNA. In contrast, postmitotic neurons possessed extremely low levels of E2F1 protein as assessed by the electrophoretic mobility shift assay and Western blotting. A recombinant E2F1 fusion protein was ubiquitinated in vitro when incubated with neuronal lysates. In addition, treatment with the proteasome inhibitor MG132 increased the endogenous level of E2F1 protein in neurons. These results suggest that the ubiquitin-proteasome pathway contributes, at least in part, to the downregulation of E2F1 protein in postmitotic neurons. Adenovirus-mediated transfer of E2F1 cDNA into postmitotic neurons induced both bromodeoxyuridine incorporation and chromatin condensation, suggesting that deregulated E2F1 expression causes both aberrant S-phase entry and apoptosis of postmitotic neurons. Thus, downregulation of endogenous E2F1 protein in postmitotic neurons may be indispensable for the preventionof their reentry into the cell cycle. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 11:54:40