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Titolo:
Neuronal nitric oxide synthase is a SHP-1 substrate involved in sst2 somatostatin receptor growth inhibitory signaling
Autore:
Lopez, F; Ferjoux, G; Cordelier, P; Saint-Laurent, N; Esteve, JP; Vaysse, N; Buscail, L; Susini, C;
Indirizzi:
CHU Rangueil, IFR 31, INSERM, U531, F-31403 Toulouse 4, France CHU Rangueil Toulouse France 4 INSERM, U531, F-31403 Toulouse 4, France
Titolo Testata:
FASEB JOURNAL
fascicolo: 10, volume: 15, anno: 2001,
pagine: NIL_4 - NIL_20
SICI:
0892-6638(200108)15:10<NIL_4:NNOSIA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE CELLS; PROTEIN-TYROSINE PHOSPHATASES; GASTROINTESTINAL-TRACT; GENE-EXPRESSION; TERMINAL REGION; TUMOR-GROWTH; CYCLE ARREST; PROLIFERATION; KINASE; PHOSPHORYLATION;
Keywords:
CHO; acini; pancreas; motheaten mice; cGMP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Susini, C CHU Rangueil, IFR 31, INSERM, U531, F-31403 Toulouse 4, France CHU Rangueil Toulouse France 4 531, F-31403 Toulouse 4, France
Citazione:
F. Lopez et al., "Neuronal nitric oxide synthase is a SHP-1 substrate involved in sst2 somatostatin receptor growth inhibitory signaling", FASEB J, 15(10), 2001, pp. NIL_4-NIL_20

Abstract

Somatostatin receptor sst2 is an inhibitory G protein-coupled receptor, which inhibits normal and tumor cell growth by a mechanism involving the tyrosine phosphatase SHP-1. We reported previously that SHP-1 associates transiently with and is activated by sst2 and is a critical component for sst2 growth inhibitory signaling. Here, we demonstrate that in Chinese hamster ovary cells expressing sst2, SHP-1 is associated at the basal level with the neuronal nitric oxide synthase (nNOS). Following sst2 activation by the somatostatin analog RC-160, SHP-1 rapidly recruits nNOS tyrosine dephosphorylates and activates it. The resulting NO activates guanylate cyclase and inhibits cell proliferation. Coexpression of a catalytically inactive SHP-1 mutant with sst2 blocks RC-160-induced nNOS dephosphorylation and activation, as well as guanylate cyclase activation. In mouse pancreatic acini, RC-160 treatment reduces nNOS tyrosine phosphorylation accompanied by an increase of its activity. By opposition, in acini from viable motheaten (me(v)/me(v))mice, which express a markedly inactive SHP-1, RC-160 has no effect on nNOS activity. Finally, expression of a dominant-negative form of nNOS prevents both RC-160-induced p27 up-regulation and cell proliferation inhibition. We therefore identified nNOS as a novel SHP-1 substrate critical for sst2-induced cell-growth arrest.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 01:36:24