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Titolo:
LACK OF RAPID DESENSITIZATION OF CA2-INDUCED INTERNALIZATION( RESPONSES IN TRANSFECTED CHO CELLS EXPRESSING THE RAT NEUROTENSIN RECEPTOR DESPITE AGONIST)
Autore:
HERMANS E; GAILLY P; GILLIS JM; OCTAVE JN; MALOTEAUX JM;
Indirizzi:
UNIV CATHOLIQUE LOUVAIN,NEUROCHEM LAB,10 AVE HIPPOCRATE B-1200 BRUSSELS BELGIUM UNIV CATHOLIQUE LOUVAIN,DEPT PHYSIOL B-1200 BRUSSELS BELGIUM
Titolo Testata:
Journal of neurochemistry
fascicolo: 6, volume: 64, anno: 1995,
pagine: 2518 - 2525
SICI:
0022-3042(1995)64:6<2518:LORDOC>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-CHANNEL BLOCKERS; BLASTOMA CLONE N1E-115; CYCLIC-AMP FORMATION; INOSITOL TRISPHOSPHATE; FUNCTIONAL EXPRESSION; DOPAMINE RELEASE; C ACTIVATION; NEUROMEDIN-N; HT29 CELLS; MOBILIZATION;
Keywords:
NEUROTENSIN; RECEPTOR; DESENSITIZATION; INTERNALIZATION; CALCIUM; SIGNALING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
E. Hermans et al., "LACK OF RAPID DESENSITIZATION OF CA2-INDUCED INTERNALIZATION( RESPONSES IN TRANSFECTED CHO CELLS EXPRESSING THE RAT NEUROTENSIN RECEPTOR DESPITE AGONIST)", Journal of neurochemistry, 64(6), 1995, pp. 2518-2525

Abstract

Transfected Chinese hamster ovary cells were used as a model for the study of the desensitization of the neurotensin receptor at the secondmessenger level. Stimulation with nanomolar concentrations of neurotensin elicited rapid rises in the cytosolic calcium concentration ([Ca2](i)), which remained elevated throughout the peptide application. A significant response was already detected with neurotensin concentrations as low as 0.01 nM. This high efficiency of neurotensin in mediating this calcium response contrasts with the nanomolar affinity of the peptide for its receptor measured in binding experiments. Evidence indicated that the initial elevation of the [Ca2+](i) resulted from release of Ca2+ from intracellular stores, whereas the sustained response involved an influx of extracellular origin. Return to the basal level was only reached after extensive washing of the peptide or its displacement with the neurotensin receptor antagonist SR48692. After washing, further stimulations were still able to mediate an increase in the [Ca2](i), indicating an apparent absence of rapid desensitization of the intracellular signaling pathway that mediates calcium mobilization. Incontrast with this absence of response desensitization, the neurotensin receptors were found to internalize after stimulation with the peptide. This internalization was maximal after 30 min and accounted for similar to 70% of the number of neurotensin binding sites located at the cell surface. These results indicate that despite the functional properties of the rat neurotensin receptor present in Chinese hamster ovary cells after transfection, the intracellular signaling pathway triggered by stimulation with neurotensin seems to be resistant to desensitization. This might be related to the high efficiency of the intracellular signaling pathway coupled to the neurotensin receptor observed inthese cells. A possible absence of desensitization of the neurotensinreceptor itself is also discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 23:08:56