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Titolo:
Brain-derived neurotrophic factor enhances neuronal translation by activating multiple initiation processes - Comparison with the effects of insulin
Autore:
Takei, N; Kawamura, M; Hara, K; Yonezawa, K; Nawa, H;
Indirizzi:
Niigata Univ, Inst Brain Res, Dept Mol Neurobiol, Niigata 9518585, Japan Niigata Univ Niigata Japan 9518585 Mol Neurobiol, Niigata 9518585, Japan Kobe Univ, Biosignal Res Ctr, Nada Ku, Kobe, Hyogo 6578501, Japan Kobe Univ Kobe Hyogo Japan 6578501 r, Nada Ku, Kobe, Hyogo 6578501, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 46, volume: 276, anno: 2001,
pagine: 42818 - 42825
SICI:
0021-9258(20011116)276:46<42818:BNFENT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOCAL PROTEIN-SYNTHESIS; P70 S6 KINASE; SIGNAL-TRANSDUCTION PATHWAYS; MESSENGER-RNA TRANSLATION; MAMMALIAN TARGET; SYNAPTIC PLASTICITY; CORTICAL-NEURONS; STIMULATED PHOSPHORYLATION; 4E-BP1 PHOSPHORYLATION; GLYCOGEN-SYNTHASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Takei, N Niigata Univ, Inst Brain Res, Dept Mol Neurobiol, Asahimachi 1, Niigata 9518585, Japan Niigata Univ Asahimachi 1 Niigata Japan 9518585 a 9518585, Japan
Citazione:
N. Takei et al., "Brain-derived neurotrophic factor enhances neuronal translation by activating multiple initiation processes - Comparison with the effects of insulin", J BIOL CHEM, 276(46), 2001, pp. 42818-42825

Abstract

The effects of neurotrophic factors on translational activation were investigated in cortical neurons. Brain-derived neurotrophic factor (BDNF) increased protein synthesis within 30 min, whereas insulin produced a weaker enhancement of protein synthesis. BDNF-triggered protein synthesis was inhibited by LY294002, PD98059, and rapamycin, whereas the effect of insulin was unaffected by PD98059. To explore the mechanisms underlying this effect, theprotein phosphorylation cascades that lead to the activation of translation initiation in neurons were examined. BDNF induced the phosphorylation of both eukaryote initiation factor (eIF) 4E and its binding protein (eIF4E-binding protein-1). The former reaction was inhibited by PD98059, whereas thelatter was inhibited by LY294002 or rapamycin. In agreement, BDNF induced the phosphorylation of mammalian TOR ((t) under bar arget (o) under barf (r) under bar apamycin) and enhanced its kinase activity toward eIF4E-bindingprotein-1. In contrast, insulin failed to activate MAPK and did not inducethe phosphorylation of eIF4E. Since BDNF and insulin increased the activity of eIF2B and eIF2, the only difference between them was eIF4E phosphorylation. Thus, this may explain the lower activity of insulin in potentiating neuronal protein synthesis. These results suggest strongly that BDNF simultaneously activates multiple signaling cascades consisting of phosphatidylinositol 3-kinase, mammalian TOR and MAPK to enhance translation initiation in neurons.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 12:38:04