LANT-6, xenopsin and neuromedin N stimulate cyclic GMP at neurotensin receptors.

Abstract

The naturally occurring analogs of neurotensin-(8-13), xenopsin, [Lys8,Asn9]neurotensin-(8-13) (LANT-6) and neuromedin N stimulated the production of intracellular cyclic GMP in murine neuroblastoma clone N1E-115, an adrenergic neuronal cell type. The order of potency was neurotensin-(8-13) greater than neurotensin greater than xenopsin greater than neuromedin N greater than LANT-6. Furthermore, xenopsin, LANT-6 and neuromedin N each inhibited the specific binding of [3H]neurotensin to intact N1E-115 cells in a dose-related fashion. The order of affinity of the peptides for the neurotensin receptor was neurotensin-(8-13) greater than xenopsin greater than neurotensin greater than neuromedin N greater than LANT-6.

• Authors: J A Gilbert, E Richelson
• Journal: European journal of pharmacology (Eur J Pharmacol) Vol. 129 Issue 3 Pg. 379-83 (Oct 07 1986) ISSN: 0014-2999 [Print] Netherlands
• PMID: 3023108 (Publication Type: Journal Article)

Chemical References

• Oligopeptides
• Peptide Fragments
• Peptides
• Receptors, Neurotensin
• Receptors, Neurotransmitter
• Xenopus Proteins
• neuromedin N
• Neurotensin
• xenopsin
• neurotensin-related hexapeptide
• Cyclic GMP

Topics

• Animals
• Clone Cells
• Cyclic GMP (biosynthesis)
• Mice
• Neuroblastoma (metabolism)
• Neurotensin (analogs & derivatives, metabolism, pharmacology)
• Oligopeptides (pharmacology)
• Peptide Fragments (pharmacology)
• Peptides
• Receptors, Neurotensin
• Receptors, Neurotransmitter (drug effects, metabolism)
• Xenopus Proteins