Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Polymorphism and signalling of melatonin receptors

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Brydon, L.
  • Petit, L.
  • de Coppet, P.
  • Barrett, P.
  • Morgan, P. J.
  • Strosberg, Donny
  • Jockers, R.

publication date

  • May 1999

journal

  • Reproduction Nutrition Development  Journal

abstract

  • Melatonin receptors belong to the superfamily of G protein-coupled receptors. Cloning of Mel1c receptors expressed in Xenopus skin revealed the existence of a polymorphism for these receptors. Heterologous expression of the two allelic isoforms, called Mel1c(alpha) and Mel1c(beta), indicated functional differences in their signalling properties. Both isoforms are coupled to the cAMP and cGMP pathways. However, the alpha isoform is preferentially coupled to the cAMP pathway, whereas the beta isoform couples preferentially to the cGMP pathway. Coupling differences may be explained by the fact that five of the six amino acid substitutions between the two isoforms are localized within intracellular receptor regions potentially involved in G protein coupling. Allelic isoforms were also observed for Mel1a receptors expressed in ovine pars tuberalis, suggesting that polymorphism is a general feature of the melatonin receptor family. We also evaluated the potential of the two human melatonin receptor subtypes, Mel1a and Mel1b, to modulate the cGMP pathway. Melatonin inhibited intracellular cGMP levels in a dose-dependent manner in HEK293 cells transfected with the human Mel1b receptor. This was not the case for HEK293 cells transfected with the human Mel1a receptor. In conclusion, our results indicate that the expression of receptor subtypes and isoforms may permit differential signalling between melatonin receptors.

subject areas

  • 1-Methyl-3-isobutylxanthine
  • Adenylyl Cyclases
  • Alleles
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cloning, Molecular
  • Colforsin
  • Cyclic AMP
  • Cyclic GMP
  • GTP-Binding Proteins
  • Guanylate Cyclase
  • HeLa Cells
  • Humans
  • Melatonin
  • Models, Biological
  • Molecular Sequence Data
  • Nitroprusside
  • Oxadiazoles
  • Pituitary Gland, Anterior
  • Polymorphism, Genetic
  • Protein Binding
  • Protein Isoforms
  • Quinoxalines
  • Receptors, Cell Surface
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Melatonin
  • Recombinant Fusion Proteins
  • Sheep
  • Signal Transduction
  • Skin
  • Species Specificity
  • Transfection
  • Xenopus laevis
scroll to property group menus

Research

keywords

  • melatonin receptor
  • polymorphism
  • signalling
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0926-5287

Digital Object Identifier (DOI)

  • 10.1051/rnd:19990304

PubMed ID

  • 10420434
scroll to property group menus

Additional Document Info

start page

  • 315

end page

  • 324

volume

  • 39

issue

  • 3

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support