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Titolo:
Modulation of nicotinic acetylcholine receptor turnover by tyrosine phosphorylation in rat myotubes
Autore:
Sava, A; Barisone, I; Di Mauro, D; Fumagalli, G; Sala, C;
Indirizzi:
Univ Verona, Sch Med, Pharmacol Sect, Dept Med & Publ Hlth,Policlin Borgo Roma, I-37134 Verona, Italy Univ Verona Verona Italy I-37134 iclin Borgo Roma, I-37134 Verona, Italy Univ Messina, Dept Biomorphol, I-90125 Messina, Italy Univ Messina Messina Italy I-90125 pt Biomorphol, I-90125 Messina, Italy CNR, Ctr Cellular & Mol Pharmacol, I-20129 Milan, Italy CNR Milan Italy I-20129 r Cellular & Mol Pharmacol, I-20129 Milan, Italy
Titolo Testata:
NEUROSCIENCE LETTERS
fascicolo: 1-2, volume: 313, anno: 2001,
pagine: 37 - 40
SICI:
0304-3940(20011102)313:1-2<37:MONART>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUROMUSCULAR-JUNCTIONS; STABILIZATION; DEGRADATION; MUSCLE; CALCIUM; SUBUNIT;
Keywords:
nicotinic acetylcholine receptor; neuromuscular junction; turnover; myotubes; tyrosine phosphatases; pervanadate; biotinylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Fumagalli, G Univ Verona, Sch Med, Pharmacol Sect, Dept Med & Publ Hlth,Policlin Borgo Roma, I-37134 Verona, Italy Univ Verona Verona Italy I-37134oma, I-37134 Verona, Italy
Citazione:
A. Sava et al., "Modulation of nicotinic acetylcholine receptor turnover by tyrosine phosphorylation in rat myotubes", NEUROSCI L, 313(1-2), 2001, pp. 37-40

Abstract

The muscle nicotinic acetylcholine receptor (AChR) turns over at differentrates depending on stage of synaptogenesis and innervation. Tyrosine phosphorylation modulates desensitization, interaction with cytoskeleton and lateral mobility in the membrane of AChR. To determine whether tyrosine phosphorylation also modulates the turnover of AChR, myotubes in vitro were exposed to the tyrosine phosphatase inhibitor pervanadate. Our data indicate that a transient increase of phosphotyrosine levels stabilized a fraction of AChRs. The effects were limited to the non-epsilon subunit-containing AChRs already present in the membrane. Tyrosine phosphorylation of the receptor occurred on the beta subunit, was transient and stable molecules were not selectively tyrosine phosphorylated. The data indicate that modulation of phosphotyrosine levels in muscle cells provides signals to control AChR metabolic stability. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:56:18