Abstract
We have identified cDNA encoding a functional growth hormone secretagogue-receptor 1a (GHS-R1a, ghrelin receptor) in two species of anuran amphibian, the bullfrog (Rana catesbeiana), and the Japanese tree frog (Hyla japonica). Deduced receptor protein for bullfrog and Japanese tree frog (tree frog) was comprised of 374- and 371-amino acids, respectively. The two receptors shared 86% identity, and are grouped to the clade of the tetrapod homologs by phylogenetic analysis. In functional analyses, ghrelin and GHS-R1a agonists increased intracellular Ca2+ concentration in GHS-R1a-transfected-HEK293 cell, but ligand selectivity of ghrelin with Ser3 and Thr3 was not observed between the two receptors. Bullfrog GHS-R1a mRNA was mainly expressed in the brain, stomach, and testis. In the brain, the gene expression was detected in the diencephalon and mesencephalon, but not in the pituitary. Tree frog GHS-R1a mRNA was predominantly expressed in the gastrointestinal tract and ovary, but not detected in the pituitary. In bullfrog stomach but not the brain, GHS-R1a mRNA expression increased after 10 days of fasting. For tree frog, GHS-R1a mRNA expression was increased in the brain, stomach and ventral skin by 10 days of fasting, and in the stomach and ventral skin by a dehydration treatment. Intracerebroventricular injection of ghrelin in dehydrated tree frog did not affect water absorption from the ventral skin. These results suggest that ghrelin is involved in energy homeostasis and possibly in osmoregulation in frogs.
Highlights
Ghrelin, a 28-amino-acid peptide in which the third serine residue (Ser3) has an n-octanoyl modification, is an endogenous ligand for the growth hormone (GH) secretagogue-receptor 1a (GHSR1a), and was first identified in the stomach of rats and humans (Kojima et al, 1999)
This suggests that bullfrog ghrelin binds to rat GHS-R1a with different affinity to rat ghrelin, and the reversed phenomenon could be seen for the bullfrog ghrelin receptor
IDENTIFICATION OF GHRELIN RECEPTOR-LIKE RECEPTOR cDNA We identified cDNA encoding GHS-Ra-like protein from each frog
Summary
A 28-amino-acid peptide in which the third serine residue (Ser3) has an n-octanoyl modification, is an endogenous ligand for the growth hormone (GH) secretagogue-receptor 1a (GHSR1a), and was first identified in the stomach of rats and humans (Kojima et al, 1999). The third acylated amino acid was changed to threonine instead of serine as seen in mammals This substitution of amino acid affects ghrelin’s biological activity: bullfrog ghrelin is 100-times stronger in stimulating both GH and prolactin (PRL) secretion from dispersed bullfrog pituitary cells, when compared to rat ghrelin. A weak effect is observed in GH secretion when bullfrog ghrelin was injected intravenously into rats (Kaiya et al, 2001). This suggests that bullfrog ghrelin binds to rat GHS-R1a with different affinity to rat ghrelin, and the reversed phenomenon could be seen for the bullfrog ghrelin receptor
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