Extracellular calcium dependence of the neurotensin-induced relaxation of intestinal smooth muscles: Studies with calcium channel blockers and BAY K-8644

Kullak, A.; Donoso, M. Verónica; Huidobro‐Toro, J. Pablo

doi:10.1016/0014-2999(87)90678-9

Cited by 12 publications

(1 citation statement)

References 25 publications

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“…In these models, production of inositol trisphosphate induced by NT was further correlated with an increase in the cytosolic Ca 2+ concentration ([Ca 2+]i) (Snider et al, 1986;Bozou et al, 1989;Imaizumi et al, 1989;Sato et al, 1991) . In some cases, in addition to this major intracellular signaling pathway, the stimulation of the NTR promoted either activation or inhibition of adenylyl cyclase (Bozou et al, 1986;Yamada et al, 1993b) as well as influx of calcium from extracellular origin (Battaini et al, 1986 ;Memo et al ., 1986;Kullak et al, 1987) . Finally, in NIE-115 neuroblastoma cells, stimulation with NT gave rise to an increase in cyclic GMP levels, resulting from intracellular cascade events involving calcium-induced activation of nitric oxide synthase and nitric oxide-induced activation of guanylyl cyclase (Gilbert and Richelson, 1984) .…”

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Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Hermans¹,

Gailly

Gillis

et al. 1995

Journal of Neurochemistry

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Transfected Chinese hamster ovary cells were used as a model for the study of the desensitization of the neurotensin receptor at the second messenger 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. In contrast 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 ∼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 in these cells. A possible absence of desensitization of the neurotensin receptor itself is also discussed.

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Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Hermans¹,

Gailly

Gillis

et al. 1995

Journal of Neurochemistry

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Peptide Receptors and Signal Transduction in the Digestive Tract

Laburthe¹,

Kitabgi²,

Couvineau³

et al. 1993

Gastrointestinal Regulatory Peptides

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Neurotensin and prostaglandin interactions in smooth muscle of the guinea pig stomach

Katsoulis

Conlon

1988

European Journal of Pharmacology

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Extracellular calcium dependence of the neurotensin-induced relaxation of intestinal smooth muscles: Studies with calcium channel blockers and BAY K-8644

Cited by 12 publications

References 25 publications

Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Peptide Receptors and Signal Transduction in the Digestive Tract

Neurotensin and prostaglandin interactions in smooth muscle of the guinea pig stomach

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Extracellular calcium dependence of the neurotensin-induced relaxation of intestinal smooth muscles: Studies with calcium channel blockers and BAY K-8644

Cited by 12 publications

References 25 publications

Lack of Rapid Desensitization of Ca2+ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Lack of Rapid Desensitization of Ca2+ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Peptide Receptors and Signal Transduction in the Digestive Tract

Neurotensin and prostaglandin interactions in smooth muscle of the guinea pig stomach

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Product

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Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization

Lack of Rapid Desensitization of Ca²⁺ Responses in Transfected CHO Cells Expressing the Rat Neurotensin Receptor Despite Agonist‐Induced Internalization