PUBLICATION

Pharmacological characterization of a nociceptin receptor from zebrafish (Danio rerio)

Authors
Rivas-Boyero, A.A., Herrero-Turrion, M.J., Gonzalez-Nunez, V., Sanchez-Simon, F.M., Barreto-Valer, K., and Rodriguez, R.E.
ID
ZDB-PUB-110124-8
Date
2011
Source
Journal of molecular endocrinology   46(2): 111-123 (Journal)
Registered Authors
González Nuñez, Veronica, Rodriguez, Raquel E.
Keywords
none
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Brain Chemistry
  • Cloning, Molecular
  • DNA, Complementary
  • Gene Expression
  • Gills/chemistry
  • Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology
  • HEK293 Cells
  • Humans
  • Kinetics
  • Liver/chemistry
  • Models, Animal
  • Molecular Sequence Data
  • Opioid Peptides/metabolism
  • Opioid Peptides/pharmacology*
  • Phylogeny
  • Protein Binding/drug effects*
  • Protein Binding/physiology
  • Receptors, Opioid*/genetics
  • Receptors, Opioid*/isolation & purification
  • Receptors, Opioid*/metabolism
  • Receptors, Opioid, kappa/genetics
  • Receptors, Opioid, kappa/metabolism
  • Recombinant Proteins/genetics
  • Recombinant Proteins/metabolism*
  • Sequence Alignment
  • Zebrafish/genetics
  • Zebrafish/metabolism
PubMed
21247980 Full text @ J. Mol. Endocrinol.
Abstract
The nociceptin receptor (NOP) and its endogenous ligand, nociceptin/orphanin FQ, are involved in a wide range of biological functions, such as pain, anxiety, learning and memory. The zebrafish has been proposed as a candidate to study the in vivo effects of several drugs of abuse and to discover new pharmacological targets. We report the cloning, expression and pharmacological characterization of a NOP receptor from zebrafish (drNOP). The full-length cDNA codes a protein of 363 residues, which shows high sequence similarity to other NOPs. Phylogenetic analysis indicates that NOPs are broadly conserved during vertebrate evolution, and that they stand for the most divergent clade of the opioid/orphanin FQ receptor family. Expression studies have revealed that drNOP mRNA is highly expressed in the central nervous system, and low expression levels are also found in peripheral tissues such as gills, muscle and liver. Pharmacological analysis indicates that drNOP displays specific and saturable binding for [Leucyl-3,4,5-3H]-Nociceptin, with a KD = 0.20 ± 0.02 nM and a Bmax= 1703 ± 81 fmol/ mg protein. [3H]-Nociceptin binding is displaced by several opioid ligands such as dynorphin A, naloxone, bremazocine or the κ-selective antagonist nor-binaltorphimine. [35S]GTPγS stimulation studies showed that drNOP receptor is functional, as nociceptin is able to fully activate the receptor and dynorphin A behaves as a partial agonist (50% stimulation). Our results indicate that drNOP receptor displays mixed characteristics of both NOP and κ opioid receptors. Hence, drNOP, which has retained more of the likely ancestral features, bridges the gap between nociceptin and opiate pharmacology.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping