The secretin G-protein-coupled receptor family: teleost receptors. | - CCMAR -

Journal Article

TitleThe secretin G-protein-coupled receptor family: teleost receptors.
Publication TypeJournal Article
AuthorsCardoso, JCR, Clark, MS, Viera, FA, Bridge, PD, Gilles, A, Power, DM
Year of Publication2005
JournalJ Mol Endocrinol
Volume34
Issue3
Date Published2005 Jun
Pagination753-65
ISSN0952-5041
KeywordsAnimals, Calcitonin, Calcitonin Gene-Related Peptide, Fishes, Growth Hormone-Releasing Hormone, Humans, Nerve Growth Factors, Neuropeptides, Neurotransmitter Agents, Parathyroid Hormone, Parathyroid Hormone-Related Protein, Pituitary Adenylate Cyclase-Activating Polypeptide, Receptors, G-Protein-Coupled, Receptors, Vasoactive Intestinal Peptide, Secretin, Vasoactive Intestinal Peptide, Zebrafish Proteins
Abstract

Twenty-one members of the secretin family (family 2) of G-protein-coupled receptors (GPCRs) were identified via directed cloning and data-mining of the Fugu Genome Consortium database, representing the most comprehensive description of secretin GPCRs in a teleost fish to date. Duplicated genes were identified for many of the family members, namely the receptors for pituitary adenylate cyclase-activating polypeptide (PACAP)/vasoactive intestinal peptide (VIP), calcitonin, calcitonin gene-related peptide (CGRP), growth hormone releasing hormone (GHRH), glucagon receptor/glucagon-like peptide (GLP) and parathyroid hormone-related peptide (PTHrP)/PTH. Mining of other teleost genomes (zebrafish and Tetraodon) revealed that the duplicated genes identified in the Takifugu genome were also present in these fish. Additional database searching of the Escherichia coli, yeast, Drosophila, Caenorhabditis elegans and Ciona genomes revealed that the family 2 of GPCRs were only present in the multicellular organisms. Orthologues of all the human secretin receptors were identified with the exception of secretin itself. Additional database searches in the Fugu Genome Consortium database also failed to reveal a secretin ligand and so it is hypothesised that both the receptor and the ligand evolved after the divergence of teleost/tetrapod lineages. Phylogenetic analysis at both the protein and the DNA level provided strong support for each of the individual receptor family groupings, but weak support between groups, making evolutionary inferences difficult. A more critical analysis of the PACAP/VIP receptor family confirmed previous hypotheses that the vasoactive intestinal peptide receptor (VPAC(1)R) gene is the ancestral form of the receptor.

DOI10.1677/jme.1.01730
Sapientia

http://www.ncbi.nlm.nih.gov/pubmed/15956345?dopt=Abstract

Alternate JournalJ. Mol. Endocrinol.
PubMed ID15956345